TY  - CONF
AU  - Kojić, Snežana
AU  - Bošković, Srđan
AU  - Milovanović, Mina
AU  - Stainie, Didier
AU  - Juez, Rubén Marín
AU  - Jasnić, Jovana
AU  - Novković, Mirjana
AU  - Milošević, Emilija
PY  - 2024
UR  - https://www.izfs.org/education/10sczi
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2309
AB  - In contrast to humans, zebrafish have a remarkable ability to regenerate their hearts after injury, while both humans and zebrafish efficiently repair the wounded skeletal muscle. Common players in these two processes might represent potential targets for the development of efficient therapies to stimulate human heart to regenerate after injury. We identified ankrd1a expression to be upregulated in both regenerating zebrafish hearts and in repairing skeletal muscle. Its mammalian homolog ANKRD1/CARP encodes a stress responsive cardiac ankyrin repeat protein involved in transcriptional regulation, sarcomere assembly and mechanosensing. Using a TgBAC(ankrd1a:EGFP) line, we showed that activation of ankrd1a in cryoinjured heart is restricted to border zone cardiomyocytes, implicating this gene in dedifferentiation and proliferation of regenerating cardiomyocytes. After stab wound injury of skeletal muscle expression of the fluorescent reporter was observed from 3 dpi, when new EGFP-positive muscle cells emerged inside the injury zone. At later time points, EGFP-positive myofibers were visible in the deeper tissue layers, concomitant with active repair of the injured tissue. In cryoinjured skeletal muscle, strong activation of ankrd1a was also observed in myofibers adjacent to the injury, and in those on uninjured side. Detection of the transgene in both newly formed myofibers that invade the wound and in the apparently uninjured tissue surrounding the injury suggests the role of ankrd1a in skeletal muscle tissue repair and adaptive processes in uninjured myofibers surrounding the injury site. Our results implicate ankrd1a in zebrafish muscle regeneration, repair and remodeling, promoting it as an attractive target for translational studies, as a player in muscle healing and as a sensor of stressed muscle.
PB  - Society for Zebrafish Research
C3  - 10th Strategic Conference of Zebrafish Investigators
T1  - Zebrafish ankrd1a as a common player  in heart regeneration and skeletal muscle repair
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2309
ER  - 

@conference{
author = "Kojić, Snežana and Bošković, Srđan and Milovanović, Mina and Stainie, Didier and Juez, Rubén Marín and Jasnić, Jovana and Novković, Mirjana and Milošević, Emilija",
year = "2024",
abstract = "In contrast to humans, zebrafish have a remarkable ability to regenerate their hearts after injury, while both humans and zebrafish efficiently repair the wounded skeletal muscle. Common players in these two processes might represent potential targets for the development of efficient therapies to stimulate human heart to regenerate after injury. We identified ankrd1a expression to be upregulated in both regenerating zebrafish hearts and in repairing skeletal muscle. Its mammalian homolog ANKRD1/CARP encodes a stress responsive cardiac ankyrin repeat protein involved in transcriptional regulation, sarcomere assembly and mechanosensing. Using a TgBAC(ankrd1a:EGFP) line, we showed that activation of ankrd1a in cryoinjured heart is restricted to border zone cardiomyocytes, implicating this gene in dedifferentiation and proliferation of regenerating cardiomyocytes. After stab wound injury of skeletal muscle expression of the fluorescent reporter was observed from 3 dpi, when new EGFP-positive muscle cells emerged inside the injury zone. At later time points, EGFP-positive myofibers were visible in the deeper tissue layers, concomitant with active repair of the injured tissue. In cryoinjured skeletal muscle, strong activation of ankrd1a was also observed in myofibers adjacent to the injury, and in those on uninjured side. Detection of the transgene in both newly formed myofibers that invade the wound and in the apparently uninjured tissue surrounding the injury suggests the role of ankrd1a in skeletal muscle tissue repair and adaptive processes in uninjured myofibers surrounding the injury site. Our results implicate ankrd1a in zebrafish muscle regeneration, repair and remodeling, promoting it as an attractive target for translational studies, as a player in muscle healing and as a sensor of stressed muscle.",
publisher = "Society for Zebrafish Research",
journal = "10th Strategic Conference of Zebrafish Investigators",
title = "Zebrafish ankrd1a as a common player  in heart regeneration and skeletal muscle repair",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2309"
}

Kojić, S., Bošković, S., Milovanović, M., Stainie, D., Juez, R. M., Jasnić, J., Novković, M.,& Milošević, E.. (2024). Zebrafish ankrd1a as a common player  in heart regeneration and skeletal muscle repair. in 10th Strategic Conference of Zebrafish Investigators
Society for Zebrafish Research..
https://hdl.handle.net/21.15107/rcub_imagine_2309

Kojić S, Bošković S, Milovanović M, Stainie D, Juez RM, Jasnić J, Novković M, Milošević E. Zebrafish ankrd1a as a common player  in heart regeneration and skeletal muscle repair. in 10th Strategic Conference of Zebrafish Investigators. 2024;.
https://hdl.handle.net/21.15107/rcub_imagine_2309 .

Kojić, Snežana, Bošković, Srđan, Milovanović, Mina, Stainie, Didier, Juez, Rubén Marín, Jasnić, Jovana, Novković, Mirjana, Milošević, Emilija, "Zebrafish ankrd1a as a common player  in heart regeneration and skeletal muscle repair" in 10th Strategic Conference of Zebrafish Investigators (2024),
https://hdl.handle.net/21.15107/rcub_imagine_2309 .

TY  - JOUR
AU  - Milošević, Emilija
AU  - Novković, Mirjana
AU  - Cenni, Vittoria
AU  - Bavelloni, Alberto
AU  - Kojić, Snežana
AU  - Jasnić, Jovana
PY  - 2024
UR  - https://doi.org/10.1007/s00418-024-02272-2
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2325
AB  - Rhabdomyosarcoma (RMS) is the most common soft tissue malignancy in children and adolescents. Respecting the age of the patients and the tumor aggressiveness, investigation of the molecular mechanisms of RMS tumorigenesis is directed toward the identification of novel therapeutic targets. To contribute to a better understanding of the molecular pathology of RMS, we investigated ankyrin repeat domain 1 (ANKRD1), designated as a potential marker for differential diagnostics. In this study, we used three RMS cell lines (SJRH30, RD, and HS-729) to assess its expression profile, intracellular localization, and turnover. They express wild-type ANKRD1, as judged by the sequencing of the open reading frame. Each cell line expressed a different amount of ANKRD1 protein, although the transcript level was similar. According to western blot analysis, ANKRD1 protein was expressed at detectable levels in the SJRH30 and RD cells (SJRH30 > RD), but not in the HS-729, even after immunoprecipitation. Immunocytochemistry revealed nuclear and cytoplasmic localization of ANKRD1 in all examined cell lines. Moreover, the punctate pattern of ANKRD1 staining in the nuclei of RD and HS-729 cells overlapped with coilin, indicating its association with Cajal bodies. We have shown that RMS cells are not able to overexpress ANKRD1 protein, which can be attributed to its proteasomal degradation. The unsuccessful attempt to overexpress ANKRD1 in RMS cells indicates the possibility that its overexpression may have detrimental effects for RMS cells and opens a window for further research into its role in RMS pathogenesis and for potential therapeutic targeting.
PB  - Springer Nature
T2  - Histochemistry and Cell Biology
T2  - Histochemistry and Cell BiologyHistochem Cell Biol
T1  - Molecular characterization of ANKRD1 in rhabdomyosarcoma cell lines: expression, localization, and proteasomal degradation
DO  - 10.1007/s00418-024-02272-2
ER  - 

@article{
author = "Milošević, Emilija and Novković, Mirjana and Cenni, Vittoria and Bavelloni, Alberto and Kojić, Snežana and Jasnić, Jovana",
year = "2024",
abstract = "Rhabdomyosarcoma (RMS) is the most common soft tissue malignancy in children and adolescents. Respecting the age of the patients and the tumor aggressiveness, investigation of the molecular mechanisms of RMS tumorigenesis is directed toward the identification of novel therapeutic targets. To contribute to a better understanding of the molecular pathology of RMS, we investigated ankyrin repeat domain 1 (ANKRD1), designated as a potential marker for differential diagnostics. In this study, we used three RMS cell lines (SJRH30, RD, and HS-729) to assess its expression profile, intracellular localization, and turnover. They express wild-type ANKRD1, as judged by the sequencing of the open reading frame. Each cell line expressed a different amount of ANKRD1 protein, although the transcript level was similar. According to western blot analysis, ANKRD1 protein was expressed at detectable levels in the SJRH30 and RD cells (SJRH30 > RD), but not in the HS-729, even after immunoprecipitation. Immunocytochemistry revealed nuclear and cytoplasmic localization of ANKRD1 in all examined cell lines. Moreover, the punctate pattern of ANKRD1 staining in the nuclei of RD and HS-729 cells overlapped with coilin, indicating its association with Cajal bodies. We have shown that RMS cells are not able to overexpress ANKRD1 protein, which can be attributed to its proteasomal degradation. The unsuccessful attempt to overexpress ANKRD1 in RMS cells indicates the possibility that its overexpression may have detrimental effects for RMS cells and opens a window for further research into its role in RMS pathogenesis and for potential therapeutic targeting.",
publisher = "Springer Nature",
journal = "Histochemistry and Cell Biology, Histochemistry and Cell BiologyHistochem Cell Biol",
title = "Molecular characterization of ANKRD1 in rhabdomyosarcoma cell lines: expression, localization, and proteasomal degradation",
doi = "10.1007/s00418-024-02272-2"
}

Milošević, E., Novković, M., Cenni, V., Bavelloni, A., Kojić, S.,& Jasnić, J.. (2024). Molecular characterization of ANKRD1 in rhabdomyosarcoma cell lines: expression, localization, and proteasomal degradation. in Histochemistry and Cell Biology
Springer Nature..
https://doi.org/10.1007/s00418-024-02272-2

Milošević E, Novković M, Cenni V, Bavelloni A, Kojić S, Jasnić J. Molecular characterization of ANKRD1 in rhabdomyosarcoma cell lines: expression, localization, and proteasomal degradation. in Histochemistry and Cell Biology. 2024;.
doi:10.1007/s00418-024-02272-2 .

Milošević, Emilija, Novković, Mirjana, Cenni, Vittoria, Bavelloni, Alberto, Kojić, Snežana, Jasnić, Jovana, "Molecular characterization of ANKRD1 in rhabdomyosarcoma cell lines: expression, localization, and proteasomal degradation" in Histochemistry and Cell Biology (2024),
https://doi.org/10.1007/s00418-024-02272-2 . .

TY  - CONF
AU  - Milovanović, Mina
AU  - Bošković, Srđan
AU  - Jasnić, Jovana
AU  - Novković, Mirjana
AU  - Milošević, Emilija
AU  - Kojić, Snežana
PY  - 2023
UR  - https://zebrafish2023.org/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2023
AB  - In our previous work, using transgenic zebrafish line TgBAC(ankrd1a:EGFP), we showed activation
of the zebrafish ankrd1a gene in border zone cardiomyocytes of cryoinjured heart and in close
proximity of needle-stab wounds in skeletal muscle, indicating its involvement in muscle
regeneration. Our results implicated ankrd1a in zebrafish skeletal muscle tissue repair and
remodeling, as a sensor of stressed muscle. Here we take a closer look at the spatio-temporal
expression profile of the ankrd1a gene in injured zebrafish skeletal muscle by analyzing cryosections
prepared from wounded tissue of TgBAC(ankrd1a:EGFP) adults at 1, 3, 5, 7 and 10 days post-injury
(dpi). The expression of the fluorescent reporter was observed from 3 dpi and remained until 10 dpi.
At 3dpi, new GFP-positive muscle cells emerged inside the injury zone, at the site of needle entry,
while in the later days (5, 7 and 10 dpi), newly formed GFP-positive myofibers were visible in the
deeper tissue layers within the injury, indicating active repair of the injured tissue. To identify cells
in which ankrd1a is activated after injury, we stained the sections for markers of satellite-like cells,
undifferentiated and differentiated muscle cells, and mature myofibers. Since the reporter was
detected both in the newly formed myofibers that invade the wound and in the apparently uninjured
tissue surrounding the injury, we hypothesize that ankrd1a is not only involved in satellite celldependent tissue repair, but its expression might be a hallmark of adaptive process in undamaged
myofibers surrounding the physical injury.
C3  - 12th European Zebrafish Meeting
T1  - Expression profile of ankrd1a during repair of injured zebrafish skeletal muscle
EP  - 276
SP  - 276
SP  - 0254
VL  - 14
VL  - 12
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2023
ER  - 

@conference{
author = "Milovanović, Mina and Bošković, Srđan and Jasnić, Jovana and Novković, Mirjana and Milošević, Emilija and Kojić, Snežana",
year = "2023",
abstract = "In our previous work, using transgenic zebrafish line TgBAC(ankrd1a:EGFP), we showed activation
of the zebrafish ankrd1a gene in border zone cardiomyocytes of cryoinjured heart and in close
proximity of needle-stab wounds in skeletal muscle, indicating its involvement in muscle
regeneration. Our results implicated ankrd1a in zebrafish skeletal muscle tissue repair and
remodeling, as a sensor of stressed muscle. Here we take a closer look at the spatio-temporal
expression profile of the ankrd1a gene in injured zebrafish skeletal muscle by analyzing cryosections
prepared from wounded tissue of TgBAC(ankrd1a:EGFP) adults at 1, 3, 5, 7 and 10 days post-injury
(dpi). The expression of the fluorescent reporter was observed from 3 dpi and remained until 10 dpi.
At 3dpi, new GFP-positive muscle cells emerged inside the injury zone, at the site of needle entry,
while in the later days (5, 7 and 10 dpi), newly formed GFP-positive myofibers were visible in the
deeper tissue layers within the injury, indicating active repair of the injured tissue. To identify cells
in which ankrd1a is activated after injury, we stained the sections for markers of satellite-like cells,
undifferentiated and differentiated muscle cells, and mature myofibers. Since the reporter was
detected both in the newly formed myofibers that invade the wound and in the apparently uninjured
tissue surrounding the injury, we hypothesize that ankrd1a is not only involved in satellite celldependent tissue repair, but its expression might be a hallmark of adaptive process in undamaged
myofibers surrounding the physical injury.",
journal = "12th European Zebrafish Meeting",
title = "Expression profile of ankrd1a during repair of injured zebrafish skeletal muscle",
pages = "276-276-0254",
volume = "14, 12",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2023"
}

Milovanović, M., Bošković, S., Jasnić, J., Novković, M., Milošević, E.,& Kojić, S.. (2023). Expression profile of ankrd1a during repair of injured zebrafish skeletal muscle. in 12th European Zebrafish Meeting, 14, 276-276.
https://hdl.handle.net/21.15107/rcub_imagine_2023

Milovanović M, Bošković S, Jasnić J, Novković M, Milošević E, Kojić S. Expression profile of ankrd1a during repair of injured zebrafish skeletal muscle. in 12th European Zebrafish Meeting. 2023;14:276-276.
https://hdl.handle.net/21.15107/rcub_imagine_2023 .

Milovanović, Mina, Bošković, Srđan, Jasnić, Jovana, Novković, Mirjana, Milošević, Emilija, Kojić, Snežana, "Expression profile of ankrd1a during repair of injured zebrafish skeletal muscle" in 12th European Zebrafish Meeting, 14 (2023):276-276,
https://hdl.handle.net/21.15107/rcub_imagine_2023 .

TY  - JOUR
AU  - Milošević, Emilija
AU  - Stanisavljević, Nemanja
AU  - Bošković, Srđan
AU  - Stamenković, Nemanja
AU  - Novković, Mirjana
AU  - Bavelloni, Alberto
AU  - Cenni, Vittoria
AU  - Kojić, Snežana
AU  - Jasnić, Jovana
PY  - 2023
UR  - https://doi.org/10.1007/s00432-023-04930-9
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1928
AB  - Sarcomas are rare and heterogenic tumors with unclear etiology. They develop in bone and connective tissue, mainly in pediatric patients. To increase efficacy of current therapeutic options, natural products showing selective toxicity to tumor cells are extensively investigated. Here, we evaluated antitumor activity of bacterial pigment violacein in osteosarcoma (OS) and rhabdomyosarcoma (RMS) cell lines.
PB  - Springer Nature
T2  - Journal of Cancer Research and Clinical Oncology
T1  - Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines
DO  - 10.1007/s00432-023-04930-9
ER  - 

@article{
author = "Milošević, Emilija and Stanisavljević, Nemanja and Bošković, Srđan and Stamenković, Nemanja and Novković, Mirjana and Bavelloni, Alberto and Cenni, Vittoria and Kojić, Snežana and Jasnić, Jovana",
year = "2023",
abstract = "Sarcomas are rare and heterogenic tumors with unclear etiology. They develop in bone and connective tissue, mainly in pediatric patients. To increase efficacy of current therapeutic options, natural products showing selective toxicity to tumor cells are extensively investigated. Here, we evaluated antitumor activity of bacterial pigment violacein in osteosarcoma (OS) and rhabdomyosarcoma (RMS) cell lines.",
publisher = "Springer Nature",
journal = "Journal of Cancer Research and Clinical Oncology",
title = "Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines",
doi = "10.1007/s00432-023-04930-9"
}

Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology
Springer Nature..
https://doi.org/10.1007/s00432-023-04930-9

Milošević E, Stanisavljević N, Bošković S, Stamenković N, Novković M, Bavelloni A, Cenni V, Kojić S, Jasnić J. Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. 2023;.
doi:10.1007/s00432-023-04930-9 .

Milošević, Emilija, Stanisavljević, Nemanja, Bošković, Srđan, Stamenković, Nemanja, Novković, Mirjana, Bavelloni, Alberto, Cenni, Vittoria, Kojić, Snežana, Jasnić, Jovana, "Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines" in Journal of Cancer Research and Clinical Oncology (2023),
https://doi.org/10.1007/s00432-023-04930-9 . .

TY  - CONF
AU  - Milovanović, Mina
AU  - Bošković, Srđan
AU  - Jasnić, Jovana
AU  - Novković, Mirjana
AU  - Milošević, Emilija
AU  - Kojić, Snežana
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2132
AB  - Introduction: In contrast to humans, zebrafish have a remarkable ability to regenerate injured heart
through a complex and highly orchestrated processinvolving all cardiac structures. The majorsource of
new myocardial cells are resident cardiomyocytes, which dedifferentiate and reinitiate proliferation, invading the area of injury to replace the lost myocardium. The response of the myocardium and coronary
vasculature is preceded by activation of epi- and endocardium, which form active scaffolds to guide regeneration. The aim of thisstudy wasto identify cardiac structuresin which ankrd1a gene is activated during zebrafish heart regeneration.
Methods: We crossed several zebrafish reporter lines: TgBAC(ankrd1a:EGFP) (to identify cells expressing
ankrd1a), Tg(myl7:nls-dsRedExpress) (for labeling cardiomyocyte nuclei) and Tg(kdrl:RAS-mCherry) (for labeling endocardial/endothelial cells). Zebrafish hearts were cryoinjured and left to regenerate for 3 and
7 days. Dedifferentiating cardiomyocytes and epicardial cells were immunostained with anti-MYH7 and
anti-caveolin1 antibody, respectively. Cells labeled with transgenes and immunostaining were visualized on tissue cryosections by fluorescent microscopy.
Results: Zebrafish ankrd1a was activated in the injury border zone cardiomyocytes, located between
the injured and remote myocardium. Its expression preceded that of a dedifferentiation marker, MYH7.
The TgBAC(ankrd1a:EGFP) transgene was not detected in epicardial or endocardial cells of regenerating
zebrafish heart.
Conclusion: Activation of ankrd1a during regeneration of zebrafish heart is restricted to borderzone
cardiomyocytes, implicating this gene in dedifferentiation and proliferation of cardiomyocytes. The absence of ankrd1a expression in epicardium and endocardium indicatesthat this gene does not contribute
to the regeneration process occuring in these layers of the heart.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Spatial profile of ankrd1a activation during regeneration of zebrafish heart
EP  - 141
SP  - 141
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2132
ER  - 

@conference{
author = "Milovanović, Mina and Bošković, Srđan and Jasnić, Jovana and Novković, Mirjana and Milošević, Emilija and Kojić, Snežana",
year = "2023",
abstract = "Introduction: In contrast to humans, zebrafish have a remarkable ability to regenerate injured heart
through a complex and highly orchestrated processinvolving all cardiac structures. The majorsource of
new myocardial cells are resident cardiomyocytes, which dedifferentiate and reinitiate proliferation, invading the area of injury to replace the lost myocardium. The response of the myocardium and coronary
vasculature is preceded by activation of epi- and endocardium, which form active scaffolds to guide regeneration. The aim of thisstudy wasto identify cardiac structuresin which ankrd1a gene is activated during zebrafish heart regeneration.
Methods: We crossed several zebrafish reporter lines: TgBAC(ankrd1a:EGFP) (to identify cells expressing
ankrd1a), Tg(myl7:nls-dsRedExpress) (for labeling cardiomyocyte nuclei) and Tg(kdrl:RAS-mCherry) (for labeling endocardial/endothelial cells). Zebrafish hearts were cryoinjured and left to regenerate for 3 and
7 days. Dedifferentiating cardiomyocytes and epicardial cells were immunostained with anti-MYH7 and
anti-caveolin1 antibody, respectively. Cells labeled with transgenes and immunostaining were visualized on tissue cryosections by fluorescent microscopy.
Results: Zebrafish ankrd1a was activated in the injury border zone cardiomyocytes, located between
the injured and remote myocardium. Its expression preceded that of a dedifferentiation marker, MYH7.
The TgBAC(ankrd1a:EGFP) transgene was not detected in epicardial or endocardial cells of regenerating
zebrafish heart.
Conclusion: Activation of ankrd1a during regeneration of zebrafish heart is restricted to borderzone
cardiomyocytes, implicating this gene in dedifferentiation and proliferation of cardiomyocytes. The absence of ankrd1a expression in epicardium and endocardium indicatesthat this gene does not contribute
to the regeneration process occuring in these layers of the heart.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Spatial profile of ankrd1a activation during regeneration of zebrafish heart",
pages = "141-141",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2132"
}

Milovanović, M., Bošković, S., Jasnić, J., Novković, M., Milošević, E.,& Kojić, S.. (2023). Spatial profile of ankrd1a activation during regeneration of zebrafish heart. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 141-141.
https://hdl.handle.net/21.15107/rcub_imagine_2132

Milovanović M, Bošković S, Jasnić J, Novković M, Milošević E, Kojić S. Spatial profile of ankrd1a activation during regeneration of zebrafish heart. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:141-141.
https://hdl.handle.net/21.15107/rcub_imagine_2132 .

Milovanović, Mina, Bošković, Srđan, Jasnić, Jovana, Novković, Mirjana, Milošević, Emilija, Kojić, Snežana, "Spatial profile of ankrd1a activation during regeneration of zebrafish heart" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):141-141,
https://hdl.handle.net/21.15107/rcub_imagine_2132 .

TY  - JOUR
AU  - Milošević, Emilija
AU  - Stanisavljević, Nemanja
AU  - Bošković, Srđan
AU  - Stamenković, Nemanja
AU  - Novković, Mirjana
AU  - Bavelloni, Alberto
AU  - Cenni, Vittoria
AU  - Kojić, Snežana
AU  - Jasnić, Jovana
PY  - 2023
UR  - https://doi.org/10.1007/s00432-023-04930-9
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1918
AB  - Sarcomas are rare and heterogenic tumors with unclear etiology. They develop in bone and connective tissue, mainly in pediatric patients. To increase efficacy of current therapeutic options, natural products showing selective toxicity to tumor cells are extensively investigated. Here, we evaluated antitumor activity of bacterial pigment violacein in osteosarcoma (OS) and rhabdomyosarcoma (RMS) cell lines.
PB  - Springer Nature
T2  - Journal of Cancer Research and Clinical Oncology
T1  - Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines
DO  - 10.1007/s00432-023-04930-9
ER  - 

@article{
author = "Milošević, Emilija and Stanisavljević, Nemanja and Bošković, Srđan and Stamenković, Nemanja and Novković, Mirjana and Bavelloni, Alberto and Cenni, Vittoria and Kojić, Snežana and Jasnić, Jovana",
year = "2023",
abstract = "Sarcomas are rare and heterogenic tumors with unclear etiology. They develop in bone and connective tissue, mainly in pediatric patients. To increase efficacy of current therapeutic options, natural products showing selective toxicity to tumor cells are extensively investigated. Here, we evaluated antitumor activity of bacterial pigment violacein in osteosarcoma (OS) and rhabdomyosarcoma (RMS) cell lines.",
publisher = "Springer Nature",
journal = "Journal of Cancer Research and Clinical Oncology",
title = "Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines",
doi = "10.1007/s00432-023-04930-9"
}

Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology
Springer Nature..
https://doi.org/10.1007/s00432-023-04930-9

Milošević E, Stanisavljević N, Bošković S, Stamenković N, Novković M, Bavelloni A, Cenni V, Kojić S, Jasnić J. Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. 2023;.
doi:10.1007/s00432-023-04930-9 .

Milošević, Emilija, Stanisavljević, Nemanja, Bošković, Srđan, Stamenković, Nemanja, Novković, Mirjana, Bavelloni, Alberto, Cenni, Vittoria, Kojić, Snežana, Jasnić, Jovana, "Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines" in Journal of Cancer Research and Clinical Oncology (2023),
https://doi.org/10.1007/s00432-023-04930-9 . .

TY  - CONF
AU  - Novković, Mirjana
AU  - Vasić, Marko
AU  - Jasnić, Jovana
AU  - Milošević, Emilija
AU  - Milovanović, Mina
AU  - Savić, Slobodan
AU  - Kojić, Snežana
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2114
AB  - Introduction: Ankyrin Repeat Domain 2 (ANKRD2) is expressed in skeletal muscle, where plays a role in
muscle development, differentiation and adaptation to stress. Human skeletal muscle consists of three
major fiber types: type 1 (slow-twitch, oxidative), type 2A (fast-twitch, oxidative) and type 2X (fast-twitch,
glycolytic). ANKRD2 is reported to be primarily expressed in type 1 myofibers. However, recent findings
on human single myofibers and our study of chicken muscles have shown that this protein may also be
expressed in type 2A fibers. Hence, our objective was to examine whether ANKRD2 is present in human
fast, type 2A muscle fibers using immunohistochemistry.
Methods: Samples of large leg musclessoleus, gastrocnemius, vastusintermedius and vastuslateralis were
obtained from human cadaveric tissue. Serial cryosections were independently stained with anti-ANKRD2
and antibodies for different myosin heavy chain isoforms (6H1 for type 2X, BF35 for type 1 and 2A, antiMHCs for type 1 and anti-MHCf for type 2A and 2X fibers). Immunostained tissues were analyzed by fluorescent microscopy.
Results: In addition to slow, type 1, ANKRD2 wasfound expressed in fast, type 2A myofibers, which both
have oxidative metabolism. Further, we did not observe ANDRD2 expression in glycolytic, type 2X
myiofibers. This pattern of ANKRD2 expression was consistent across all examined muscles.
Conclusion: Our resultsimplicate that the regulatory mechanism of ANKRD2 expression in human skeletal muscle is associated with oxidative metabolism, rather than muscle contraction speed.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Determination of muscle fiber types expressing ANKRD2
EP  - 155
SP  - 155
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2114
ER  - 

@conference{
author = "Novković, Mirjana and Vasić, Marko and Jasnić, Jovana and Milošević, Emilija and Milovanović, Mina and Savić, Slobodan and Kojić, Snežana",
year = "2023",
abstract = "Introduction: Ankyrin Repeat Domain 2 (ANKRD2) is expressed in skeletal muscle, where plays a role in
muscle development, differentiation and adaptation to stress. Human skeletal muscle consists of three
major fiber types: type 1 (slow-twitch, oxidative), type 2A (fast-twitch, oxidative) and type 2X (fast-twitch,
glycolytic). ANKRD2 is reported to be primarily expressed in type 1 myofibers. However, recent findings
on human single myofibers and our study of chicken muscles have shown that this protein may also be
expressed in type 2A fibers. Hence, our objective was to examine whether ANKRD2 is present in human
fast, type 2A muscle fibers using immunohistochemistry.
Methods: Samples of large leg musclessoleus, gastrocnemius, vastusintermedius and vastuslateralis were
obtained from human cadaveric tissue. Serial cryosections were independently stained with anti-ANKRD2
and antibodies for different myosin heavy chain isoforms (6H1 for type 2X, BF35 for type 1 and 2A, antiMHCs for type 1 and anti-MHCf for type 2A and 2X fibers). Immunostained tissues were analyzed by fluorescent microscopy.
Results: In addition to slow, type 1, ANKRD2 wasfound expressed in fast, type 2A myofibers, which both
have oxidative metabolism. Further, we did not observe ANDRD2 expression in glycolytic, type 2X
myiofibers. This pattern of ANKRD2 expression was consistent across all examined muscles.
Conclusion: Our resultsimplicate that the regulatory mechanism of ANKRD2 expression in human skeletal muscle is associated with oxidative metabolism, rather than muscle contraction speed.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Determination of muscle fiber types expressing ANKRD2",
pages = "155-155",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2114"
}

Novković, M., Vasić, M., Jasnić, J., Milošević, E., Milovanović, M., Savić, S.,& Kojić, S.. (2023). Determination of muscle fiber types expressing ANKRD2. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 155-155.
https://hdl.handle.net/21.15107/rcub_imagine_2114

Novković M, Vasić M, Jasnić J, Milošević E, Milovanović M, Savić S, Kojić S. Determination of muscle fiber types expressing ANKRD2. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:155-155.
https://hdl.handle.net/21.15107/rcub_imagine_2114 .

Novković, Mirjana, Vasić, Marko, Jasnić, Jovana, Milošević, Emilija, Milovanović, Mina, Savić, Slobodan, Kojić, Snežana, "Determination of muscle fiber types expressing ANKRD2" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):155-155,
https://hdl.handle.net/21.15107/rcub_imagine_2114 .

TY  - DATA
AU  - Milošević, Emilija
AU  - Stanisavljević, Nemanja
AU  - Bošković, Srđan
AU  - Stamenković, Nemanja
AU  - Novković, Mirjana
AU  - Bavelloni, Alberto
AU  - Cenni, Vittoria
AU  - Kojić, Snežana
AU  - Jasnić, Jovana
PY  - 2023
UR  - https://doi.org/10.1007/s00432-023-04930-9
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1929
T2  - Journal of Cancer Research and Clinical Oncology
T1  - Supplementary data for the article: Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. https://doi.org/10.1007/s00432-023-04930-9
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1929
ER  - 

@misc{
author = "Milošević, Emilija and Stanisavljević, Nemanja and Bošković, Srđan and Stamenković, Nemanja and Novković, Mirjana and Bavelloni, Alberto and Cenni, Vittoria and Kojić, Snežana and Jasnić, Jovana",
year = "2023",
journal = "Journal of Cancer Research and Clinical Oncology",
title = "Supplementary data for the article: Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. https://doi.org/10.1007/s00432-023-04930-9",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1929"
}

Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Supplementary data for the article: Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. https://doi.org/10.1007/s00432-023-04930-9. in Journal of Cancer Research and Clinical Oncology.
https://hdl.handle.net/21.15107/rcub_imagine_1929

Milošević E, Stanisavljević N, Bošković S, Stamenković N, Novković M, Bavelloni A, Cenni V, Kojić S, Jasnić J. Supplementary data for the article: Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. https://doi.org/10.1007/s00432-023-04930-9. in Journal of Cancer Research and Clinical Oncology. 2023;.
https://hdl.handle.net/21.15107/rcub_imagine_1929 .

Milošević, Emilija, Stanisavljević, Nemanja, Bošković, Srđan, Stamenković, Nemanja, Novković, Mirjana, Bavelloni, Alberto, Cenni, Vittoria, Kojić, Snežana, Jasnić, Jovana, "Supplementary data for the article: Milošević, E., Stanisavljević, N., Bošković, S., Stamenković, N., Novković, M., Bavelloni, A., Cenni, V., Kojić, S.,& Jasnić, J.. (2023). Antitumor activity of natural pigment violacein against osteosarcoma and rhabdomyosarcoma cell lines. in Journal of Cancer Research and Clinical Oncology. https://doi.org/10.1007/s00432-023-04930-9" in Journal of Cancer Research and Clinical Oncology (2023),
https://hdl.handle.net/21.15107/rcub_imagine_1929 .

TY  - CONF
AU  - Milošević, Emilija
AU  - Jasnić, Jovana
AU  - Novković, Mirjana
AU  - Cenni, V.
AU  - Bavelloni, A.
AU  - Kojić, Snežana
PY  - 2023
UR  - https://febs.onlinelibrary.wiley.com/doi/10.1002/1878-0261.13471
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1911
AB  - Introduction: Rhabdomyosarcoma (RMS) is the most common soft tissue
malignancy in children and adolescents. Respecting the age
of the patients and the tumor aggressiveness, investigation
of the molecular mechanisms of RMS tumorigenesis is
essential, most notably due to the possible identification of
novel therapeutic targets. To contribute to a better
understanding of the molecular pathology of RMS, we
investigated ANKRD1 (ankyrin repeat domain 1) gene,
considered a potential RMS diagnostic marker. The
changes in its expression are related to carcinogenesis and
resistance to chemotherapy in several types of tumors.
PB  - Wiley
C3  - Molecular oncology
T1  - Expression profiling of ANKRD1 in rhabdomyosarcoma cell lines
EP  - 197
SP  - 196
VL  - 17
VL  - Supplement 1
DO  - doi.org/10.1002/1878-0261.13471
ER  - 

@conference{
author = "Milošević, Emilija and Jasnić, Jovana and Novković, Mirjana and Cenni, V. and Bavelloni, A. and Kojić, Snežana",
year = "2023",
abstract = "Introduction: Rhabdomyosarcoma (RMS) is the most common soft tissue
malignancy in children and adolescents. Respecting the age
of the patients and the tumor aggressiveness, investigation
of the molecular mechanisms of RMS tumorigenesis is
essential, most notably due to the possible identification of
novel therapeutic targets. To contribute to a better
understanding of the molecular pathology of RMS, we
investigated ANKRD1 (ankyrin repeat domain 1) gene,
considered a potential RMS diagnostic marker. The
changes in its expression are related to carcinogenesis and
resistance to chemotherapy in several types of tumors.",
publisher = "Wiley",
journal = "Molecular oncology",
title = "Expression profiling of ANKRD1 in rhabdomyosarcoma cell lines",
pages = "197-196",
volume = "17, Supplement 1",
doi = "doi.org/10.1002/1878-0261.13471"
}

Milošević, E., Jasnić, J., Novković, M., Cenni, V., Bavelloni, A.,& Kojić, S.. (2023). Expression profiling of ANKRD1 in rhabdomyosarcoma cell lines. in Molecular oncology
Wiley., 17, 196-197.
https://doi.org/doi.org/10.1002/1878-0261.13471

Milošević E, Jasnić J, Novković M, Cenni V, Bavelloni A, Kojić S. Expression profiling of ANKRD1 in rhabdomyosarcoma cell lines. in Molecular oncology. 2023;17:196-197.
doi:doi.org/10.1002/1878-0261.13471 .

Milošević, Emilija, Jasnić, Jovana, Novković, Mirjana, Cenni, V., Bavelloni, A., Kojić, Snežana, "Expression profiling of ANKRD1 in rhabdomyosarcoma cell lines" in Molecular oncology, 17 (2023):196-197,
https://doi.org/doi.org/10.1002/1878-0261.13471 . .

TY  - CONF
AU  - Milošević, Emilija
AU  - Jasnić, Jovana
AU  - Stanisavljević, Nemanja
AU  - Cenni, Vittoria
AU  - Bavelloni, Alberto
AU  - Kojić, Snežana
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2101
AB  - Investigati on of natural compounds showing specific toxicity to tumor cells aims to improve the efficacy
of available therapies. Our previous research demonstrated the cytotoxic acti vity of the bacterial pigment violacein
against rhabdomyosarcoma (RMS) cell lines. RMS is the most common soft tissue malignancy in children. In this
study, we evaluated the cytotoxicity of violacein on RMS cells in combinati on with conventi onal chemotherapeutics
doxorubicin, irinotecan, and vinflunine.
PB  - Belgrade :  Serbian Association on for Cancer Research
C3  - 6th Congress of the Serbian Association for Cancer Research (SDIR)
T1  - Violacein enhances the cytotoxic effect of commonly used chemotherapeutics on rhabdomyosarcoma cells
EP  - 94
IS  - 1
SP  - 94
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2101
ER  - 

@conference{
author = "Milošević, Emilija and Jasnić, Jovana and Stanisavljević, Nemanja and Cenni, Vittoria and Bavelloni, Alberto and Kojić, Snežana",
year = "2023",
abstract = "Investigati on of natural compounds showing specific toxicity to tumor cells aims to improve the efficacy
of available therapies. Our previous research demonstrated the cytotoxic acti vity of the bacterial pigment violacein
against rhabdomyosarcoma (RMS) cell lines. RMS is the most common soft tissue malignancy in children. In this
study, we evaluated the cytotoxicity of violacein on RMS cells in combinati on with conventi onal chemotherapeutics
doxorubicin, irinotecan, and vinflunine.",
publisher = "Belgrade :  Serbian Association on for Cancer Research",
journal = "6th Congress of the Serbian Association for Cancer Research (SDIR)",
title = "Violacein enhances the cytotoxic effect of commonly used chemotherapeutics on rhabdomyosarcoma cells",
pages = "94-94",
number = "1",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2101"
}

Milošević, E., Jasnić, J., Stanisavljević, N., Cenni, V., Bavelloni, A.,& Kojić, S.. (2023). Violacein enhances the cytotoxic effect of commonly used chemotherapeutics on rhabdomyosarcoma cells. in 6th Congress of the Serbian Association for Cancer Research (SDIR)
Belgrade :  Serbian Association on for Cancer Research.(1), 94-94.
https://hdl.handle.net/21.15107/rcub_imagine_2101

Milošević E, Jasnić J, Stanisavljević N, Cenni V, Bavelloni A, Kojić S. Violacein enhances the cytotoxic effect of commonly used chemotherapeutics on rhabdomyosarcoma cells. in 6th Congress of the Serbian Association for Cancer Research (SDIR). 2023;(1):94-94.
https://hdl.handle.net/21.15107/rcub_imagine_2101 .

Milošević, Emilija, Jasnić, Jovana, Stanisavljević, Nemanja, Cenni, Vittoria, Bavelloni, Alberto, Kojić, Snežana, "Violacein enhances the cytotoxic effect of commonly used chemotherapeutics on rhabdomyosarcoma cells" in 6th Congress of the Serbian Association for Cancer Research (SDIR), no. 1 (2023):94-94,
https://hdl.handle.net/21.15107/rcub_imagine_2101 .

TY  - JOUR
AU  - Stamenković, Nemanja
AU  - Jasnić, Jovana
AU  - Novković, Mirjana
AU  - Milošević, Emilija
AU  - Bošković, Srđan
AU  - Kojić, Ana
AU  - Popić, Kristina
AU  - Stanković, Marija
AU  - Wang, Yajun
AU  - Milenković, Sanja
AU  - Radojković, Dragica
AU  - Ma, Guada
AU  - Kojić, Snežana
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1307
AB  - Striated muscle signaling protein and transcriptional regulator ANKRD2 participates in myogenesis, myogenic differentiation, muscle adaptation and stress response. It is preferentially expressed in slow, oxidative fibers of mammalian skeletal muscle. In this study, we report on characterization of chickenANKRD2. The chickenANKRD2coding region contains 1002 bp and encodes a 334-amino acid protein which shares approximately 58% identity with human and mouse orthologs, mostly in the conserved region of ankyrin repeats. Comprehensive analysis of theANKRD2gene and protein expression in adult chicken demonstrated its predominant expression in red muscles of thigh and drumstick, compared to white muscle. It was not detected in heart and white pectoral muscle. Uneven expression of ANKRD2 in chicken skeletal muscles, observed by immunohistochemistry, was attributed to its selective expression in slow, oxidative, type I and fast, oxidative-glycolytic, type IIA myofibers. Association of chickenANKRD2with phenotypic differences between red and white muscles points to its potential role in the process of myofiber-type specification. In addition to expression in slow oxidative myofibers, as demonstrated for mammalian protein, chicken ANKRD2 was also detected in fast fibers with mixed oxidative and glycolytic metabolism. This finding suggests thatANKRD2is responsive to metabolic differences between types of avian myofibers and orientates future studies towards investigation of its role in molecular mechanisms of myofiber-type-specific gene expression.
PB  - Springer, New York
T2  - Histochemistry and Cell Biology
T1  - Cloning and expression profiling of muscle regulator ANKRD2 in domestic chickenGallus gallus
EP  - 396
IS  - 4
SP  - 383
VL  - 154
DO  - 10.1007/s00418-020-01899-1
ER  - 

@article{
author = "Stamenković, Nemanja and Jasnić, Jovana and Novković, Mirjana and Milošević, Emilija and Bošković, Srđan and Kojić, Ana and Popić, Kristina and Stanković, Marija and Wang, Yajun and Milenković, Sanja and Radojković, Dragica and Ma, Guada and Kojić, Snežana",
year = "2020",
abstract = "Striated muscle signaling protein and transcriptional regulator ANKRD2 participates in myogenesis, myogenic differentiation, muscle adaptation and stress response. It is preferentially expressed in slow, oxidative fibers of mammalian skeletal muscle. In this study, we report on characterization of chickenANKRD2. The chickenANKRD2coding region contains 1002 bp and encodes a 334-amino acid protein which shares approximately 58% identity with human and mouse orthologs, mostly in the conserved region of ankyrin repeats. Comprehensive analysis of theANKRD2gene and protein expression in adult chicken demonstrated its predominant expression in red muscles of thigh and drumstick, compared to white muscle. It was not detected in heart and white pectoral muscle. Uneven expression of ANKRD2 in chicken skeletal muscles, observed by immunohistochemistry, was attributed to its selective expression in slow, oxidative, type I and fast, oxidative-glycolytic, type IIA myofibers. Association of chickenANKRD2with phenotypic differences between red and white muscles points to its potential role in the process of myofiber-type specification. In addition to expression in slow oxidative myofibers, as demonstrated for mammalian protein, chicken ANKRD2 was also detected in fast fibers with mixed oxidative and glycolytic metabolism. This finding suggests thatANKRD2is responsive to metabolic differences between types of avian myofibers and orientates future studies towards investigation of its role in molecular mechanisms of myofiber-type-specific gene expression.",
publisher = "Springer, New York",
journal = "Histochemistry and Cell Biology",
title = "Cloning and expression profiling of muscle regulator ANKRD2 in domestic chickenGallus gallus",
pages = "396-383",
number = "4",
volume = "154",
doi = "10.1007/s00418-020-01899-1"
}

Stamenković, N., Jasnić, J., Novković, M., Milošević, E., Bošković, S., Kojić, A., Popić, K., Stanković, M., Wang, Y., Milenković, S., Radojković, D., Ma, G.,& Kojić, S.. (2020). Cloning and expression profiling of muscle regulator ANKRD2 in domestic chickenGallus gallus. in Histochemistry and Cell Biology
Springer, New York., 154(4), 383-396.
https://doi.org/10.1007/s00418-020-01899-1

Stamenković N, Jasnić J, Novković M, Milošević E, Bošković S, Kojić A, Popić K, Stanković M, Wang Y, Milenković S, Radojković D, Ma G, Kojić S. Cloning and expression profiling of muscle regulator ANKRD2 in domestic chickenGallus gallus. in Histochemistry and Cell Biology. 2020;154(4):383-396.
doi:10.1007/s00418-020-01899-1 .

Stamenković, Nemanja, Jasnić, Jovana, Novković, Mirjana, Milošević, Emilija, Bošković, Srđan, Kojić, Ana, Popić, Kristina, Stanković, Marija, Wang, Yajun, Milenković, Sanja, Radojković, Dragica, Ma, Guada, Kojić, Snežana, "Cloning and expression profiling of muscle regulator ANKRD2 in domestic chickenGallus gallus" in Histochemistry and Cell Biology, 154, no. 4 (2020):383-396,
https://doi.org/10.1007/s00418-020-01899-1 . .

TY  - JOUR
AU  - Bošković, Srđan
AU  - Marin-Juez, Ruben
AU  - Jasnić, Jovana
AU  - Reischauer, Sven
AU  - El Sammak, Hadil
AU  - Kojić, Ana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Stainier, Didier Y. R.
AU  - Kojić, Snežana
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1141
AB  - Muscle proteins with ankyrin repeats (MARPs) ANKRD1 and ANKRD2 are titin-associated proteins with a putative role as transcriptional co-regulators in striated muscle, involved in the cellular response to mechanical, oxidative and metabolic stress. Since many aspects of the biology of MARPs, particularly exact mechanisms of their action, in striated muscle are still elusive, research in this field will benefit from novel animal model system. Here we investigated the MARPs found in zebrafish for protein structure, evolutionary conservation, spatiotemporal expression profiles and response to increased muscle activity. Ankrd1 and Ankrd2 show overall moderate conservation at the protein level, more pronounced in the region of ankyrin repeats, motifs indispensable for their function. The two zebrafish genes, ankrd1a and ankrd1b, counterparts of mammalian ANKRD1/Ankrd1, have different expression profiles during first seven days of development. Mild increase of ankrd1a transcript levels was detected at 72 hpf (1.74 +/- 0.24 fold increase relative to 24 hpf time point), while ankrd1b expression was markedly upregulated from 24 hpf onward and peaked at 72 hpf (92.18 +/- 36.95 fold increase relative to 24 hpf time point). Spatially, they exhibited non-overlapping expression patterns during skeletal muscle development in trunk (ankrd1a) and tail (ankrd1b) somites. Expression of ankrd2 was barely detectable. Zebrafish MARPs, expressed at a relatively low level in adult striated muscle, were found to be responsive to endurance exercise training consisting of two bouts of 3 hours of forced swimming daily, for five consecutive days. Three hours after the last exercise bout, ankrd1a expression increased in cardiac muscle (6.19 +/- 5.05 fold change), while ankrd1b and ankrd2 were upregulated in skeletal muscle (1.97 +/- 1.05 and 1.84 +/- 0.58 fold change, respectively). This study provides the foundation to establish zebrafish as a novel in vivo model for further investigation of MARPs function in striated muscle.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise
IS  - 9
VL  - 13
DO  - 10.1371/journal.pone.0204312
ER  - 

@article{
author = "Bošković, Srđan and Marin-Juez, Ruben and Jasnić, Jovana and Reischauer, Sven and El Sammak, Hadil and Kojić, Ana and Faulkner, Georgine and Radojković, Dragica and Stainier, Didier Y. R. and Kojić, Snežana",
year = "2018",
abstract = "Muscle proteins with ankyrin repeats (MARPs) ANKRD1 and ANKRD2 are titin-associated proteins with a putative role as transcriptional co-regulators in striated muscle, involved in the cellular response to mechanical, oxidative and metabolic stress. Since many aspects of the biology of MARPs, particularly exact mechanisms of their action, in striated muscle are still elusive, research in this field will benefit from novel animal model system. Here we investigated the MARPs found in zebrafish for protein structure, evolutionary conservation, spatiotemporal expression profiles and response to increased muscle activity. Ankrd1 and Ankrd2 show overall moderate conservation at the protein level, more pronounced in the region of ankyrin repeats, motifs indispensable for their function. The two zebrafish genes, ankrd1a and ankrd1b, counterparts of mammalian ANKRD1/Ankrd1, have different expression profiles during first seven days of development. Mild increase of ankrd1a transcript levels was detected at 72 hpf (1.74 +/- 0.24 fold increase relative to 24 hpf time point), while ankrd1b expression was markedly upregulated from 24 hpf onward and peaked at 72 hpf (92.18 +/- 36.95 fold increase relative to 24 hpf time point). Spatially, they exhibited non-overlapping expression patterns during skeletal muscle development in trunk (ankrd1a) and tail (ankrd1b) somites. Expression of ankrd2 was barely detectable. Zebrafish MARPs, expressed at a relatively low level in adult striated muscle, were found to be responsive to endurance exercise training consisting of two bouts of 3 hours of forced swimming daily, for five consecutive days. Three hours after the last exercise bout, ankrd1a expression increased in cardiac muscle (6.19 +/- 5.05 fold change), while ankrd1b and ankrd2 were upregulated in skeletal muscle (1.97 +/- 1.05 and 1.84 +/- 0.58 fold change, respectively). This study provides the foundation to establish zebrafish as a novel in vivo model for further investigation of MARPs function in striated muscle.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise",
number = "9",
volume = "13",
doi = "10.1371/journal.pone.0204312"
}

Bošković, S., Marin-Juez, R., Jasnić, J., Reischauer, S., El Sammak, H., Kojić, A., Faulkner, G., Radojković, D., Stainier, D. Y. R.,& Kojić, S.. (2018). Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise. in PLoS One
Public Library Science, San Francisco., 13(9).
https://doi.org/10.1371/journal.pone.0204312

Bošković S, Marin-Juez R, Jasnić J, Reischauer S, El Sammak H, Kojić A, Faulkner G, Radojković D, Stainier DYR, Kojić S. Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise. in PLoS One. 2018;13(9).
doi:10.1371/journal.pone.0204312 .

Bošković, Srđan, Marin-Juez, Ruben, Jasnić, Jovana, Reischauer, Sven, El Sammak, Hadil, Kojić, Ana, Faulkner, Georgine, Radojković, Dragica, Stainier, Didier Y. R., Kojić, Snežana, "Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise" in PLoS One, 13, no. 9 (2018),
https://doi.org/10.1371/journal.pone.0204312 . .

TY  - JOUR
AU  - Bosnić, Predrag
AU  - Bosnić, Dragana
AU  - Jasnić, Jovana
AU  - Nikolić, Miroslav
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1154
AB  - Silicon (Si) is known to alleviate salt stress in various crops; however, the influence of Si on sodium (Na) transport and partitioning at the tissue, cell and organelle levels is poorly understood. Maize (Zea mays L.) hybrid sensitive to salt stress was exposed to moderate salt stress (40 mM NaCl; simulating conditions in salinized agricultural soils) without or with supply of 1.5 mM Si(OH)(4). We investigated the expression of SOS genes encoding Na+ efflux transporter in various root tissues of maize, paralleled by measurements of tissue Na concentration. In addition, subcellular localization of Na (using Na fluorescent dye) within the leaf mesophyll cells was also performed. Silicon supplied plants accumulate less Na in both root apex and cortex, but allocate more Na+ to the leaves via the xylem. This was accompanied by increased expression of ZrnSOS1 and ZmSOS2 in the root apex and cortex facilitating Na+ exclusion, and in the root stele for enhanced Na+ loading into the xylem. Also, Si down-regulated the expression of ZmHKT1 in the root stele, which further decreased Na+ unloading from the xylem. Consequently, Si increased accumulation of Na in leaves, but also enhances sequestration of Na+ into the vacuoles thereby decreasing Na+ accumulation in the chloroplasts. In response to moderate salt stress in maize, Si shifts the typical glycophyte behavior of this species towards that of halophytes.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Environmental and Experimental Botany
T1  - Silicon mediates sodium transport and partitioning in maize under moderate salt stress
EP  - 687
SP  - 681
VL  - 155
DO  - 10.1016/j.envexpbot.2018.08.018
ER  - 

@article{
author = "Bosnić, Predrag and Bosnić, Dragana and Jasnić, Jovana and Nikolić, Miroslav",
year = "2018",
abstract = "Silicon (Si) is known to alleviate salt stress in various crops; however, the influence of Si on sodium (Na) transport and partitioning at the tissue, cell and organelle levels is poorly understood. Maize (Zea mays L.) hybrid sensitive to salt stress was exposed to moderate salt stress (40 mM NaCl; simulating conditions in salinized agricultural soils) without or with supply of 1.5 mM Si(OH)(4). We investigated the expression of SOS genes encoding Na+ efflux transporter in various root tissues of maize, paralleled by measurements of tissue Na concentration. In addition, subcellular localization of Na (using Na fluorescent dye) within the leaf mesophyll cells was also performed. Silicon supplied plants accumulate less Na in both root apex and cortex, but allocate more Na+ to the leaves via the xylem. This was accompanied by increased expression of ZrnSOS1 and ZmSOS2 in the root apex and cortex facilitating Na+ exclusion, and in the root stele for enhanced Na+ loading into the xylem. Also, Si down-regulated the expression of ZmHKT1 in the root stele, which further decreased Na+ unloading from the xylem. Consequently, Si increased accumulation of Na in leaves, but also enhances sequestration of Na+ into the vacuoles thereby decreasing Na+ accumulation in the chloroplasts. In response to moderate salt stress in maize, Si shifts the typical glycophyte behavior of this species towards that of halophytes.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Environmental and Experimental Botany",
title = "Silicon mediates sodium transport and partitioning in maize under moderate salt stress",
pages = "687-681",
volume = "155",
doi = "10.1016/j.envexpbot.2018.08.018"
}

Bosnić, P., Bosnić, D., Jasnić, J.,& Nikolić, M.. (2018). Silicon mediates sodium transport and partitioning in maize under moderate salt stress. in Environmental and Experimental Botany
Pergamon-Elsevier Science Ltd, Oxford., 155, 681-687.
https://doi.org/10.1016/j.envexpbot.2018.08.018

Bosnić P, Bosnić D, Jasnić J, Nikolić M. Silicon mediates sodium transport and partitioning in maize under moderate salt stress. in Environmental and Experimental Botany. 2018;155:681-687.
doi:10.1016/j.envexpbot.2018.08.018 .

Bosnić, Predrag, Bosnić, Dragana, Jasnić, Jovana, Nikolić, Miroslav, "Silicon mediates sodium transport and partitioning in maize under moderate salt stress" in Environmental and Experimental Botany, 155 (2018):681-687,
https://doi.org/10.1016/j.envexpbot.2018.08.018 . .

TY  - JOUR
AU  - Samardzija, Dragana
AU  - Pogrmić-Majkić, Kristina
AU  - Fa, Svetlana
AU  - Stanić, Bojana
AU  - Jasnić, Jovana
AU  - Andrić, Nebojša
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1193
AB  - Bisphenol A (BPA) is an endocrine disruptor used in a variety of consumer products. Exposure to BPA leads to alterations in steroidogenesis of ovarian granulosa cells. Here, we analyzed the mechanism by which BPA alters progesterone biosynthesis in immature rat granulosa cells. BPA increased expression of steroidogenic acute regulatory protein (StAR), cholesterol side-chain cleavage enzyme and 3 beta-hydroxysteroid dehydrogenase in granulosa cells; however, BPA prevented the basal and the FSH-induced progesterone production. BPA caused sequestration of cholesterol to the perinuclear area, as evident by the Filipin staining. BPA decreased mRNA expression of ATP binding cassette transporter-A1 (Abca1) and increased level of sterol regulatory element binding protein 1. Addition of exogenous cell-permeable cholesterol restored the effect of BPA on Abca1 and Star mRNA expression and partially reversed BPA's effect on progesterone production. These results indicate that exposure to BPA disrupts cholesterol homeostasis leading to decreased progesterone production in immature rat granulosa cells.
PB  - Elsevier Ireland Ltd, Clare
T2  - Molecular and Cellular Endocrinology
T1  - Bisphenol A decreases progesterone synthesis by disrupting cholesterol homeostasis in rat granulosa cells
EP  - 63
IS  - C
SP  - 55
VL  - 461
DO  - 10.1016/j.mce.2017.08.013
ER  - 

@article{
author = "Samardzija, Dragana and Pogrmić-Majkić, Kristina and Fa, Svetlana and Stanić, Bojana and Jasnić, Jovana and Andrić, Nebojša",
year = "2018",
abstract = "Bisphenol A (BPA) is an endocrine disruptor used in a variety of consumer products. Exposure to BPA leads to alterations in steroidogenesis of ovarian granulosa cells. Here, we analyzed the mechanism by which BPA alters progesterone biosynthesis in immature rat granulosa cells. BPA increased expression of steroidogenic acute regulatory protein (StAR), cholesterol side-chain cleavage enzyme and 3 beta-hydroxysteroid dehydrogenase in granulosa cells; however, BPA prevented the basal and the FSH-induced progesterone production. BPA caused sequestration of cholesterol to the perinuclear area, as evident by the Filipin staining. BPA decreased mRNA expression of ATP binding cassette transporter-A1 (Abca1) and increased level of sterol regulatory element binding protein 1. Addition of exogenous cell-permeable cholesterol restored the effect of BPA on Abca1 and Star mRNA expression and partially reversed BPA's effect on progesterone production. These results indicate that exposure to BPA disrupts cholesterol homeostasis leading to decreased progesterone production in immature rat granulosa cells.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Molecular and Cellular Endocrinology",
title = "Bisphenol A decreases progesterone synthesis by disrupting cholesterol homeostasis in rat granulosa cells",
pages = "63-55",
number = "C",
volume = "461",
doi = "10.1016/j.mce.2017.08.013"
}

Samardzija, D., Pogrmić-Majkić, K., Fa, S., Stanić, B., Jasnić, J.,& Andrić, N.. (2018). Bisphenol A decreases progesterone synthesis by disrupting cholesterol homeostasis in rat granulosa cells. in Molecular and Cellular Endocrinology
Elsevier Ireland Ltd, Clare., 461(C), 55-63.
https://doi.org/10.1016/j.mce.2017.08.013

Samardzija D, Pogrmić-Majkić K, Fa S, Stanić B, Jasnić J, Andrić N. Bisphenol A decreases progesterone synthesis by disrupting cholesterol homeostasis in rat granulosa cells. in Molecular and Cellular Endocrinology. 2018;461(C):55-63.
doi:10.1016/j.mce.2017.08.013 .

Samardzija, Dragana, Pogrmić-Majkić, Kristina, Fa, Svetlana, Stanić, Bojana, Jasnić, Jovana, Andrić, Nebojša, "Bisphenol A decreases progesterone synthesis by disrupting cholesterol homeostasis in rat granulosa cells" in Molecular and Cellular Endocrinology, 461, no. C (2018):55-63,
https://doi.org/10.1016/j.mce.2017.08.013 . .

TY  - JOUR
AU  - Bosnic, Predrag
AU  - Bosnić, Dragana
AU  - Jasnić, Jovana
AU  - Nikolic, Miroslav
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1606
AB  - Silicon (Si) is known to alleviate salt stress in various crops; however, the influence of Si on sodium (Na) transport and partitioning at the tissue, cell and organelle levels is poorly understood. Maize (Zea mays L.) hybrid sensitive to salt stress was exposed to moderate salt stress (40 mM NaCl; simulating conditions in salinized agricultural soils) without or with supply of 1.5 mM Si(OH)4. We investigated the expression of SOS genes encoding Na+ efflux transporter in various root tissues of maize, paralleled by measurements of tissue Na concentration. In addition, subcellular localization of Na (using Na fluorescent dye) within the leaf mesophyll cells was also performed. Silicon supplied plants accumulate less Na in both root apex and cortex, but allocate more Na+ to the leaves via the xylem. This was accompanied by increased expression of ZmSOS1 and ZmSOS2 in the root apex and cortex facilitating Na+ exclusion, and in the root stele for enhanced Na+ loading into the xylem. Also, Si down-regulated the expression of ZmHKT1 in the root stele, which further decreased Na+ unloading from the xylem. Consequently, Si increased accumulation of Na in leaves, but also enhances sequestration of Na+ into the vacuoles thereby decreasing Na+ accumulation in the chloroplasts. In response to moderate salt stress in maize, Si shifts the typical glycophyte behavior of this species towards that of halophytes.
T2  - Environmental and Experimental Botany
T2  - Environmental and Experimental BotanyEnvironmental and Experimental Botany
T1  - Silicon mediates sodium transport and partitioning in maize under moderate salt stress
EP  - 687
SP  - 681
VL  - 155
DO  - 10.1016/j.envexpbot.2018.08.018
ER  - 

@article{
author = "Bosnic, Predrag and Bosnić, Dragana and Jasnić, Jovana and Nikolic, Miroslav",
year = "2018",
abstract = "Silicon (Si) is known to alleviate salt stress in various crops; however, the influence of Si on sodium (Na) transport and partitioning at the tissue, cell and organelle levels is poorly understood. Maize (Zea mays L.) hybrid sensitive to salt stress was exposed to moderate salt stress (40 mM NaCl; simulating conditions in salinized agricultural soils) without or with supply of 1.5 mM Si(OH)4. We investigated the expression of SOS genes encoding Na+ efflux transporter in various root tissues of maize, paralleled by measurements of tissue Na concentration. In addition, subcellular localization of Na (using Na fluorescent dye) within the leaf mesophyll cells was also performed. Silicon supplied plants accumulate less Na in both root apex and cortex, but allocate more Na+ to the leaves via the xylem. This was accompanied by increased expression of ZmSOS1 and ZmSOS2 in the root apex and cortex facilitating Na+ exclusion, and in the root stele for enhanced Na+ loading into the xylem. Also, Si down-regulated the expression of ZmHKT1 in the root stele, which further decreased Na+ unloading from the xylem. Consequently, Si increased accumulation of Na in leaves, but also enhances sequestration of Na+ into the vacuoles thereby decreasing Na+ accumulation in the chloroplasts. In response to moderate salt stress in maize, Si shifts the typical glycophyte behavior of this species towards that of halophytes.",
journal = "Environmental and Experimental Botany, Environmental and Experimental BotanyEnvironmental and Experimental Botany",
title = "Silicon mediates sodium transport and partitioning in maize under moderate salt stress",
pages = "687-681",
volume = "155",
doi = "10.1016/j.envexpbot.2018.08.018"
}

Bosnic, P., Bosnić, D., Jasnić, J.,& Nikolic, M.. (2018). Silicon mediates sodium transport and partitioning in maize under moderate salt stress. in Environmental and Experimental Botany, 155, 681-687.
https://doi.org/10.1016/j.envexpbot.2018.08.018

Bosnic P, Bosnić D, Jasnić J, Nikolic M. Silicon mediates sodium transport and partitioning in maize under moderate salt stress. in Environmental and Experimental Botany. 2018;155:681-687.
doi:10.1016/j.envexpbot.2018.08.018 .

Bosnic, Predrag, Bosnić, Dragana, Jasnić, Jovana, Nikolic, Miroslav, "Silicon mediates sodium transport and partitioning in maize under moderate salt stress" in Environmental and Experimental Botany, 155 (2018):681-687,
https://doi.org/10.1016/j.envexpbot.2018.08.018 . .

TY  - THES
AU  - Jasnić, Jovana
PY  - 2016
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=4812
UR  - https://nardus.mpn.gov.rs/handle/123456789/7886
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:15118/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=1025148594
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/43
AB  - Protein Ankrd2 pripada familiji mišićnih proteina sa ankirinskim ponovcima (eng. Muscle Ankyrin Repeat Proteins – MARP). U sarkomeri ima ulogu strukturnog elementa i signalnog molekula u procesu mehanotransdukcije. Pod dejstvom fiziĉkih i hemijskih stresora migrira u jedro, gde ostvaruje ulogu regulatora transkripcije. Ekspresija Ankrd2 je indukovana mehaniĉkim stresom i zavisna od stepena diferencijacije mišićne ćelije i faze razvića organizma. Osim u skeletnim mišićima, protein ANKRD2 je u manjoj meri eksprimiran i u srcu ĉoveka. U cilju otkrivanja novih funkcija koje ANKRD2 ima u ovom organu odreĊeni su njegov profil ekspresije i lokalizacija u srcu ĉoveka i uporeĊeni sa karakteristikama homolognog ANKRD1, koji je eksprimiran samo u srcu i detaljno okarakterisan. Utvrdili smo da je nivo ekspresije ANKRD2 dosta niţi u poreĊenju sa ANKRD1 i da je preteţno lokalizovan u sarkomeri kardiomiocita. Interkalirajući diskovi su identifikovani kao novo mesto lokalizacije oba proteina. S obzirom da su ĉesto i uspešno korišćen model sistem za prouĉavanje funkcije srĉano-specifiĉnih gena, kardiomiociti neonatalnih pacova (KMNP) su okarakterisani po pitanju ekspresije i lokalizacije endogenog Ankrd2 i egzogenog ANKRD2. Ankrd2 je lokalizovan i u jedru i u citoplazmi KMNP, a sliĉnu dualnu lokalizaciju je pokazivao i egzogeno eksprimirani ANKRD2. Za razliku od inhibitornog dejstva na ekspresiju Ankrd1, kardiotoksiĉni agens doksorubicin nije doveo do promene nivoa ekspresije proteina Ankrd2 u KMNP. U ovoj tezi su okarakterisane tri izoforme ANKRD2 od 446 (L-ANKRD2), 360 (M-ANKRD2) i 333 (S-ANKRD2) aminokiselina. Diskriminacija izoformi u popreĉno prugastim mišićima ĉoveka je postignuta korišćenjem specifiĉno dizajniranih antitela i graniĉnika. Utvrdili smo brojne sliĉnosti izmeĊu izoformi S- i M-ANKRD2, kao i znaĉajne razlike koje mogu da se odraze na njihove specifiĉne funkcije. Izoforma LANKRD2 nije detektovana ni u srcu, ni u skeletnim mišićima...
AB  - Ankrd2 is a member MARP (Muscle Ankyrin Repeat Proteins) protein family. In sarcomere, it has a role of a structural element and signaling molecule in mechanotransduction. Ankrd2 is highly responsive to physical and chemical stress, which results in its translocation to the nucleus where it acts as a transcriptional regulator. Expression of Ankrd2 is upregulated in response to mechanical stresses such as exercise and stretch, as well as during muscle development and myoblast differentiation. Apart from skeletal muscles, ANKRD2 has been also detected in adult human heart, but at lower levels. In order to explore the cardiac-specific function of ANKRD2, we determined its expression and localization in human heart and compared them with the profiles of homologous cardiac protein ANKRD1. It was found that ANKRD2 is preferentially localized in sarcomere of cardiomyocytes and that level of its expression was lower when compared to ANKRD1. Intercalated disks were identified as a novel site of localization of both proteins. Neonatal rat cardiomyocytes (NRCM) are commonly used as a model system for functional analysis of cardiac-specific genes. One of the goals of this thesis was to characterize this model regarding expression and intracellular localization of endogenous Ankrd2 and exogenous ANKRD2. Nuclear and cytoplasmic localization of Ankrd2 was observed in NRCM, while similar dual localization was established for exogenous ANKRD2 as well. In the contrast to inhibitory effect on Ankrd1 expression, cardio-toxic drug doxorubicin did not change the protein level of Ankrd2 in NRCM. In this thesis we also characterized three ANKRD2 isoforms, containing 446 (LANKRD2), 360 (M-ANKRD2) i 333 (S-ANKRD2) amino acids. Their discrimination in human striated muscles was achieved by specifically designed antibodies and PCR primers. Various similarities between S- and M-ANKRD2 isoforms were discovered, as well as several significant differences, which could reflect on their specific functions...
PB  - Univerzitet u Beogradu, Biološki fakultet
T1  - Određivanje profila ekspresije i unutarćelijske lokalizacije proteina ANKRD2 u srcu i skeletnim mišićima čoveka
T1  - Determination of expression profile and localization of ANKRD2 protein in human cardiac and skeletal muscle
UR  - https://hdl.handle.net/21.15107/rcub_nardus_7886
ER  - 

@phdthesis{
author = "Jasnić, Jovana",
year = "2016",
abstract = "Protein Ankrd2 pripada familiji mišićnih proteina sa ankirinskim ponovcima (eng. Muscle Ankyrin Repeat Proteins – MARP). U sarkomeri ima ulogu strukturnog elementa i signalnog molekula u procesu mehanotransdukcije. Pod dejstvom fiziĉkih i hemijskih stresora migrira u jedro, gde ostvaruje ulogu regulatora transkripcije. Ekspresija Ankrd2 je indukovana mehaniĉkim stresom i zavisna od stepena diferencijacije mišićne ćelije i faze razvića organizma. Osim u skeletnim mišićima, protein ANKRD2 je u manjoj meri eksprimiran i u srcu ĉoveka. U cilju otkrivanja novih funkcija koje ANKRD2 ima u ovom organu odreĊeni su njegov profil ekspresije i lokalizacija u srcu ĉoveka i uporeĊeni sa karakteristikama homolognog ANKRD1, koji je eksprimiran samo u srcu i detaljno okarakterisan. Utvrdili smo da je nivo ekspresije ANKRD2 dosta niţi u poreĊenju sa ANKRD1 i da je preteţno lokalizovan u sarkomeri kardiomiocita. Interkalirajući diskovi su identifikovani kao novo mesto lokalizacije oba proteina. S obzirom da su ĉesto i uspešno korišćen model sistem za prouĉavanje funkcije srĉano-specifiĉnih gena, kardiomiociti neonatalnih pacova (KMNP) su okarakterisani po pitanju ekspresije i lokalizacije endogenog Ankrd2 i egzogenog ANKRD2. Ankrd2 je lokalizovan i u jedru i u citoplazmi KMNP, a sliĉnu dualnu lokalizaciju je pokazivao i egzogeno eksprimirani ANKRD2. Za razliku od inhibitornog dejstva na ekspresiju Ankrd1, kardiotoksiĉni agens doksorubicin nije doveo do promene nivoa ekspresije proteina Ankrd2 u KMNP. U ovoj tezi su okarakterisane tri izoforme ANKRD2 od 446 (L-ANKRD2), 360 (M-ANKRD2) i 333 (S-ANKRD2) aminokiselina. Diskriminacija izoformi u popreĉno prugastim mišićima ĉoveka je postignuta korišćenjem specifiĉno dizajniranih antitela i graniĉnika. Utvrdili smo brojne sliĉnosti izmeĊu izoformi S- i M-ANKRD2, kao i znaĉajne razlike koje mogu da se odraze na njihove specifiĉne funkcije. Izoforma LANKRD2 nije detektovana ni u srcu, ni u skeletnim mišićima..., Ankrd2 is a member MARP (Muscle Ankyrin Repeat Proteins) protein family. In sarcomere, it has a role of a structural element and signaling molecule in mechanotransduction. Ankrd2 is highly responsive to physical and chemical stress, which results in its translocation to the nucleus where it acts as a transcriptional regulator. Expression of Ankrd2 is upregulated in response to mechanical stresses such as exercise and stretch, as well as during muscle development and myoblast differentiation. Apart from skeletal muscles, ANKRD2 has been also detected in adult human heart, but at lower levels. In order to explore the cardiac-specific function of ANKRD2, we determined its expression and localization in human heart and compared them with the profiles of homologous cardiac protein ANKRD1. It was found that ANKRD2 is preferentially localized in sarcomere of cardiomyocytes and that level of its expression was lower when compared to ANKRD1. Intercalated disks were identified as a novel site of localization of both proteins. Neonatal rat cardiomyocytes (NRCM) are commonly used as a model system for functional analysis of cardiac-specific genes. One of the goals of this thesis was to characterize this model regarding expression and intracellular localization of endogenous Ankrd2 and exogenous ANKRD2. Nuclear and cytoplasmic localization of Ankrd2 was observed in NRCM, while similar dual localization was established for exogenous ANKRD2 as well. In the contrast to inhibitory effect on Ankrd1 expression, cardio-toxic drug doxorubicin did not change the protein level of Ankrd2 in NRCM. In this thesis we also characterized three ANKRD2 isoforms, containing 446 (LANKRD2), 360 (M-ANKRD2) i 333 (S-ANKRD2) amino acids. Their discrimination in human striated muscles was achieved by specifically designed antibodies and PCR primers. Various similarities between S- and M-ANKRD2 isoforms were discovered, as well as several significant differences, which could reflect on their specific functions...",
publisher = "Univerzitet u Beogradu, Biološki fakultet",
title = "Određivanje profila ekspresije i unutarćelijske lokalizacije proteina ANKRD2 u srcu i skeletnim mišićima čoveka, Determination of expression profile and localization of ANKRD2 protein in human cardiac and skeletal muscle",
url = "https://hdl.handle.net/21.15107/rcub_nardus_7886"
}

Jasnić, J.. (2016). Određivanje profila ekspresije i unutarćelijske lokalizacije proteina ANKRD2 u srcu i skeletnim mišićima čoveka. 
Univerzitet u Beogradu, Biološki fakultet..
https://hdl.handle.net/21.15107/rcub_nardus_7886

Jasnić J. Određivanje profila ekspresije i unutarćelijske lokalizacije proteina ANKRD2 u srcu i skeletnim mišićima čoveka. 2016;.
https://hdl.handle.net/21.15107/rcub_nardus_7886 .

Jasnić, Jovana, "Određivanje profila ekspresije i unutarćelijske lokalizacije proteina ANKRD2 u srcu i skeletnim mišićima čoveka" (2016),
https://hdl.handle.net/21.15107/rcub_nardus_7886 .

TY  - JOUR
AU  - Jasnić, Jovana
AU  - Krause, Sabine
AU  - Savić, Slobodan
AU  - Kojić, Ana
AU  - Kovcić, Vlado
AU  - Bošković, Srđan
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Schreiber-Katz, Olivia
AU  - Vogel, Johannes G.
AU  - Schoser, Benedikt G.
AU  - Walter, Maggie C.
AU  - Valle, Giorgio
AU  - Radojković, Dragica
AU  - Faulkner, Georgine
AU  - Kojić, Snežana
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/933
AB  - Four human Ankrd2 transcripts, reported in the Ensembl database, code for distinct protein isoforms (360, 333, 327 and 300 aa), and so far, their existence, specific expression and localization patterns have not been studied in detail. Ankrd2 is preferentially expressed in the slow fibers of skeletal muscle. It is found in both the nuclei and the cytoplasm of skeletal muscle cells, and its localization is prone to change during differentiation and upon stress. Ankrd2 has also been detected in the heart, in ventricular cardiomyocytes and in the intercalated disks (ICDs). The main objective of this study was to distinguish between the Ankrd2 isoforms and to determine the contribution of each one to the general profile of Ankrd2 expression in striated muscles. We demonstrated that the known expression and localization pattern of Ankrd2 in striated muscle can be attributed to the isoform of 333 aa which is dominant in both tissues, while the designated cardiac and canonical isoform of 360 aa was less expressed in both tissues. The 360 aa isoform has a distinct nuclear localization in human skeletal muscle, as well as in primary myoblasts and myotubes. In contrast to the isoform of 333 aa, it was not preferentially expressed in slow fibers and not localized to the ICDs of human cardiomyocytes. Regulation of the expression of both isoforms is achieved at the transcriptional level. Our results set the stage for investigation of the specific functions and interactions of the Ankrd2 isoforms in healthy and diseased human striated muscles.
PB  - Springer, New York
T2  - Histochemistry and Cell Biology
T1  - Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles
EP  - 584
IS  - 5
SP  - 569
VL  - 146
DO  - 10.1007/s00418-016-1465-0
ER  - 

@article{
author = "Jasnić, Jovana and Krause, Sabine and Savić, Slobodan and Kojić, Ana and Kovcić, Vlado and Bošković, Srđan and Nestorović, Aleksandra and Rakićević, Ljiljana and Schreiber-Katz, Olivia and Vogel, Johannes G. and Schoser, Benedikt G. and Walter, Maggie C. and Valle, Giorgio and Radojković, Dragica and Faulkner, Georgine and Kojić, Snežana",
year = "2016",
abstract = "Four human Ankrd2 transcripts, reported in the Ensembl database, code for distinct protein isoforms (360, 333, 327 and 300 aa), and so far, their existence, specific expression and localization patterns have not been studied in detail. Ankrd2 is preferentially expressed in the slow fibers of skeletal muscle. It is found in both the nuclei and the cytoplasm of skeletal muscle cells, and its localization is prone to change during differentiation and upon stress. Ankrd2 has also been detected in the heart, in ventricular cardiomyocytes and in the intercalated disks (ICDs). The main objective of this study was to distinguish between the Ankrd2 isoforms and to determine the contribution of each one to the general profile of Ankrd2 expression in striated muscles. We demonstrated that the known expression and localization pattern of Ankrd2 in striated muscle can be attributed to the isoform of 333 aa which is dominant in both tissues, while the designated cardiac and canonical isoform of 360 aa was less expressed in both tissues. The 360 aa isoform has a distinct nuclear localization in human skeletal muscle, as well as in primary myoblasts and myotubes. In contrast to the isoform of 333 aa, it was not preferentially expressed in slow fibers and not localized to the ICDs of human cardiomyocytes. Regulation of the expression of both isoforms is achieved at the transcriptional level. Our results set the stage for investigation of the specific functions and interactions of the Ankrd2 isoforms in healthy and diseased human striated muscles.",
publisher = "Springer, New York",
journal = "Histochemistry and Cell Biology",
title = "Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles",
pages = "584-569",
number = "5",
volume = "146",
doi = "10.1007/s00418-016-1465-0"
}

Jasnić, J., Krause, S., Savić, S., Kojić, A., Kovcić, V., Bošković, S., Nestorović, A., Rakićević, L., Schreiber-Katz, O., Vogel, J. G., Schoser, B. G., Walter, M. C., Valle, G., Radojković, D., Faulkner, G.,& Kojić, S.. (2016). Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles. in Histochemistry and Cell Biology
Springer, New York., 146(5), 569-584.
https://doi.org/10.1007/s00418-016-1465-0

Jasnić J, Krause S, Savić S, Kojić A, Kovcić V, Bošković S, Nestorović A, Rakićević L, Schreiber-Katz O, Vogel JG, Schoser BG, Walter MC, Valle G, Radojković D, Faulkner G, Kojić S. Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles. in Histochemistry and Cell Biology. 2016;146(5):569-584.
doi:10.1007/s00418-016-1465-0 .

Jasnić, Jovana, Krause, Sabine, Savić, Slobodan, Kojić, Ana, Kovcić, Vlado, Bošković, Srđan, Nestorović, Aleksandra, Rakićević, Ljiljana, Schreiber-Katz, Olivia, Vogel, Johannes G., Schoser, Benedikt G., Walter, Maggie C., Valle, Giorgio, Radojković, Dragica, Faulkner, Georgine, Kojić, Snežana, "Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles" in Histochemistry and Cell Biology, 146, no. 5 (2016):569-584,
https://doi.org/10.1007/s00418-016-1465-0 . .

TY  - JOUR
AU  - Jasnić, Jovana
AU  - Nestorović, Aleksandra
AU  - Savić, Slobodan
AU  - Karasek, Sinisa
AU  - Vitulo, Nicola
AU  - Valle, Giorgio
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Kojić, Snežana
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/814
AB  - Muscle-specific mechanosensors Ankrd2/Arpp (ankyrin repeat protein 2) and Ankrd1/CARP (cardiac ankyrin repeat protein) have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. In skeletal muscle myofibrils, Ankrd2 has a structural role as a component of a titin associated stretch-sensing complex, while in the nucleus it exerts regulatory function as transcriptional co-factor. It is also involved in myogenic differentiation and coordination of myoblast proliferation. Although expressed in the heart, the role of Ankrd2 in the cardiac muscle is completely unknown. Recently, we have shown that hypertrophic and dilated cardiomyopathy pathways are altered upon Ankrd2 silencing suggesting the importance of this protein in cardiac tissue. Here we provide the underlying basis for the functional investigation of Ankrd2 in the heart. We confirmed reduced Ankrd2 expression levels in human heart in comparison with Ankrd1 using RNAseq and Western blot. For the first time we demonstrated that, apart from the sarcomere and nucleus, both proteins are localized to the intercalated disks of human cardiomyocytes. We further tested the expression and localization of endogenous Ankrd2 in rat neonatal cardiomyocytes, a well-established model for studying cardiac-specific proteins. Ankrd2 was found to be expressed in both the cytoplasm and nucleus, independently from maturation status of cardiomyocytes. In contrast to Ankrd1, it is not responsive to the cardiotoxic drug Doxorubicin, suggesting that different mechanisms govern their expression in cardiac cells.
PB  - Springer, New York
T2  - Histochemistry and Cell Biology
T1  - Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes
EP  - 597
IS  - 6
SP  - 583
VL  - 143
DO  - 10.1007/s00418-015-1307-5
ER  - 

@article{
author = "Jasnić, Jovana and Nestorović, Aleksandra and Savić, Slobodan and Karasek, Sinisa and Vitulo, Nicola and Valle, Giorgio and Faulkner, Georgine and Radojković, Dragica and Kojić, Snežana",
year = "2015",
abstract = "Muscle-specific mechanosensors Ankrd2/Arpp (ankyrin repeat protein 2) and Ankrd1/CARP (cardiac ankyrin repeat protein) have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. In skeletal muscle myofibrils, Ankrd2 has a structural role as a component of a titin associated stretch-sensing complex, while in the nucleus it exerts regulatory function as transcriptional co-factor. It is also involved in myogenic differentiation and coordination of myoblast proliferation. Although expressed in the heart, the role of Ankrd2 in the cardiac muscle is completely unknown. Recently, we have shown that hypertrophic and dilated cardiomyopathy pathways are altered upon Ankrd2 silencing suggesting the importance of this protein in cardiac tissue. Here we provide the underlying basis for the functional investigation of Ankrd2 in the heart. We confirmed reduced Ankrd2 expression levels in human heart in comparison with Ankrd1 using RNAseq and Western blot. For the first time we demonstrated that, apart from the sarcomere and nucleus, both proteins are localized to the intercalated disks of human cardiomyocytes. We further tested the expression and localization of endogenous Ankrd2 in rat neonatal cardiomyocytes, a well-established model for studying cardiac-specific proteins. Ankrd2 was found to be expressed in both the cytoplasm and nucleus, independently from maturation status of cardiomyocytes. In contrast to Ankrd1, it is not responsive to the cardiotoxic drug Doxorubicin, suggesting that different mechanisms govern their expression in cardiac cells.",
publisher = "Springer, New York",
journal = "Histochemistry and Cell Biology",
title = "Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes",
pages = "597-583",
number = "6",
volume = "143",
doi = "10.1007/s00418-015-1307-5"
}

Jasnić, J., Nestorović, A., Savić, S., Karasek, S., Vitulo, N., Valle, G., Faulkner, G., Radojković, D.,& Kojić, S.. (2015). Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes. in Histochemistry and Cell Biology
Springer, New York., 143(6), 583-597.
https://doi.org/10.1007/s00418-015-1307-5

Jasnić J, Nestorović A, Savić S, Karasek S, Vitulo N, Valle G, Faulkner G, Radojković D, Kojić S. Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes. in Histochemistry and Cell Biology. 2015;143(6):583-597.
doi:10.1007/s00418-015-1307-5 .

Jasnić, Jovana, Nestorović, Aleksandra, Savić, Slobodan, Karasek, Sinisa, Vitulo, Nicola, Valle, Giorgio, Faulkner, Georgine, Radojković, Dragica, Kojić, Snežana, "Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes" in Histochemistry and Cell Biology, 143, no. 6 (2015):583-597,
https://doi.org/10.1007/s00418-015-1307-5 . .

TY  - JOUR
AU  - Jasnić, Jovana
AU  - Lazić, Andrijana
AU  - Milivojević, Milena
AU  - Mojsin, Marija
AU  - Nikčević, Gordana
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/807
AB  - Serum is generally regarded as an essential component of many eukaryotic cell culture media, despite the fact that serum composition varies greatly and may be the source of a wide range of artefacts. The objective of this study was to assess serum-free growth conditions for the human embryonal carcinoma cell line, NT2/D1. These cells greatly resemble embryonic stem cells. In the presence of retinoic acid (RA), NT2/D1 cells irreversibly differentiate along the neuronal lineage. We have previously shown that the early phases of neural induction of these cells by RA involve the up-regulation of SOX3 gene expression. Our goal was to compare RA-induced differentiation of NT2/D1 cells in serum-containing and serum-free media, by using SOX3 protein levels as a marker of differentiation. We found that NT2/D1 cells can be successfully grown under serum-free conditions, and that the presence or absence of serum does not affect the level of SOX3 protein after a 48-hour RA induction. However, six days of RA treatment resulted in a marked increase in SOX3 protein levels in serum-free media compared to serum-containing media, indicating that serum might have an inhibitory effect on the expression of this neural differentiation marker. This finding is important for both basic and translational studies that hope to exploit cell culture conditions that are free of animal-derived products.
PB  - Sage Publications Ltd, London
T2  - ATLA-Alternatives To Laboratory Animals
T1  - Human Embryonal Carcinoma Cells in Serum-free Conditions as an In Vitro Model System of Neural Differentiation
EP  - 18
IS  - 1
SP  - 9
VL  - 43
DO  - 10.1177/026119291504300105
ER  - 

@article{
author = "Jasnić, Jovana and Lazić, Andrijana and Milivojević, Milena and Mojsin, Marija and Nikčević, Gordana",
year = "2015",
abstract = "Serum is generally regarded as an essential component of many eukaryotic cell culture media, despite the fact that serum composition varies greatly and may be the source of a wide range of artefacts. The objective of this study was to assess serum-free growth conditions for the human embryonal carcinoma cell line, NT2/D1. These cells greatly resemble embryonic stem cells. In the presence of retinoic acid (RA), NT2/D1 cells irreversibly differentiate along the neuronal lineage. We have previously shown that the early phases of neural induction of these cells by RA involve the up-regulation of SOX3 gene expression. Our goal was to compare RA-induced differentiation of NT2/D1 cells in serum-containing and serum-free media, by using SOX3 protein levels as a marker of differentiation. We found that NT2/D1 cells can be successfully grown under serum-free conditions, and that the presence or absence of serum does not affect the level of SOX3 protein after a 48-hour RA induction. However, six days of RA treatment resulted in a marked increase in SOX3 protein levels in serum-free media compared to serum-containing media, indicating that serum might have an inhibitory effect on the expression of this neural differentiation marker. This finding is important for both basic and translational studies that hope to exploit cell culture conditions that are free of animal-derived products.",
publisher = "Sage Publications Ltd, London",
journal = "ATLA-Alternatives To Laboratory Animals",
title = "Human Embryonal Carcinoma Cells in Serum-free Conditions as an In Vitro Model System of Neural Differentiation",
pages = "18-9",
number = "1",
volume = "43",
doi = "10.1177/026119291504300105"
}

Jasnić, J., Lazić, A., Milivojević, M., Mojsin, M.,& Nikčević, G.. (2015). Human Embryonal Carcinoma Cells in Serum-free Conditions as an In Vitro Model System of Neural Differentiation. in ATLA-Alternatives To Laboratory Animals
Sage Publications Ltd, London., 43(1), 9-18.
https://doi.org/10.1177/026119291504300105

Jasnić J, Lazić A, Milivojević M, Mojsin M, Nikčević G. Human Embryonal Carcinoma Cells in Serum-free Conditions as an In Vitro Model System of Neural Differentiation. in ATLA-Alternatives To Laboratory Animals. 2015;43(1):9-18.
doi:10.1177/026119291504300105 .

Jasnić, Jovana, Lazić, Andrijana, Milivojević, Milena, Mojsin, Marija, Nikčević, Gordana, "Human Embryonal Carcinoma Cells in Serum-free Conditions as an In Vitro Model System of Neural Differentiation" in ATLA-Alternatives To Laboratory Animals, 43, no. 1 (2015):9-18,
https://doi.org/10.1177/026119291504300105 . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Protić, Olga
AU  - Jasnić, Jovana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/879
AB  - Transcription factor Nkx2.5, essential for heart development, regulates cardiomyocyte-specific gene expression through combinatorial interactions with other cardiac-restricted (GATA4 and dHAND) or ubiquitous (p300) transcription regulators. Here we demonstrate that Nkx2.5 and p53 synergistically activate the promoter of the striated muscle stress responsive transcriptional cofactor Ankrd2, involved in coordination of proliferation and apoptosis during myogenic differentiation. Moreover, the p53 protein is able to interact with both wild type Nkx2.5 and its mutant Delta Nkx2.5 (aa 1-198) found in patients with diverse cardiac malformations. Nkx2.5 interaction site of p53 maps to the C terminal region, while p53 binding site on Nkx2.5 lies outside its C terminus. In addition, overexpression of Nkx2.5 has a modulatory, promoter dependent effect on p53 transactivation, while the mutant significantly abolished p53 activity on the Mdm2, p21(WAF1/CIP1) and Box promoters. Their physical interaction contributes to the observed behavior in the case of the Mdm2 promoter. Our data provide a new evidence for the role of p53 in cardiac function through interaction with Nkx2.5.
PB  - Elsevier Science Inc, New York
T2  - Archives of Biochemistry and Biophysics
T1  - Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity
EP  - 53
SP  - 45
VL  - 569
DO  - 10.1016/j.abb.2015.02.001
ER  - 

@article{
author = "Kojić, Snežana and Nestorović, Aleksandra and Rakićević, Ljiljana and Protić, Olga and Jasnić, Jovana and Faulkner, Georgine and Radojković, Dragica",
year = "2015",
abstract = "Transcription factor Nkx2.5, essential for heart development, regulates cardiomyocyte-specific gene expression through combinatorial interactions with other cardiac-restricted (GATA4 and dHAND) or ubiquitous (p300) transcription regulators. Here we demonstrate that Nkx2.5 and p53 synergistically activate the promoter of the striated muscle stress responsive transcriptional cofactor Ankrd2, involved in coordination of proliferation and apoptosis during myogenic differentiation. Moreover, the p53 protein is able to interact with both wild type Nkx2.5 and its mutant Delta Nkx2.5 (aa 1-198) found in patients with diverse cardiac malformations. Nkx2.5 interaction site of p53 maps to the C terminal region, while p53 binding site on Nkx2.5 lies outside its C terminus. In addition, overexpression of Nkx2.5 has a modulatory, promoter dependent effect on p53 transactivation, while the mutant significantly abolished p53 activity on the Mdm2, p21(WAF1/CIP1) and Box promoters. Their physical interaction contributes to the observed behavior in the case of the Mdm2 promoter. Our data provide a new evidence for the role of p53 in cardiac function through interaction with Nkx2.5.",
publisher = "Elsevier Science Inc, New York",
journal = "Archives of Biochemistry and Biophysics",
title = "Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity",
pages = "53-45",
volume = "569",
doi = "10.1016/j.abb.2015.02.001"
}

Kojić, S., Nestorović, A., Rakićević, L., Protić, O., Jasnić, J., Faulkner, G.,& Radojković, D.. (2015). Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity. in Archives of Biochemistry and Biophysics
Elsevier Science Inc, New York., 569, 45-53.
https://doi.org/10.1016/j.abb.2015.02.001

Kojić S, Nestorović A, Rakićević L, Protić O, Jasnić J, Faulkner G, Radojković D. Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity. in Archives of Biochemistry and Biophysics. 2015;569:45-53.
doi:10.1016/j.abb.2015.02.001 .

Kojić, Snežana, Nestorović, Aleksandra, Rakićević, Ljiljana, Protić, Olga, Jasnić, Jovana, Faulkner, Georgine, Radojković, Dragica, "Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity" in Archives of Biochemistry and Biophysics, 569 (2015):45-53,
https://doi.org/10.1016/j.abb.2015.02.001 . .

TY  - JOUR
AU  - Nestorović, Aleksandra
AU  - Jasnić, Jovana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Kojić, Snežana
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/736
AB  - The muscle ankyrin repeat protein Ankrd1 is localized in a mechanosensory complex of the sarcomeric I-band. It is involved in signaling pathways activated in response to mechanical stretch. It also acts as a transcriptional cofactor in the nucleus, playing an important role in cardiogenesis and skeletal muscle differentiation. To investigate its regulatory function in signaling we employed protein array methodology and identified 10 novel Ankrd1 binding partners among PDZ domain proteins known to act as platforms for multiprotein complex assembly. The zonula occludens protein-1 (ZO-1) was chosen for further analysis since its interaction with Ankrd2 had already been demonstrated. Both Ankrd2 and Ankrd1 have similar functions and localize in the same regions. We confirmed the interaction of Ankrd1 with ZO-1 protein and determined their subcellular distribution in HeLa cells, showing their colocalization in the cytoplasm. Our findings corroborate the role of Ankrd1 in intracellular signaling.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1
EP  - 1242
IS  - 3
SP  - 1233
VL  - 66
DO  - 10.2298/ABS1403233N
ER  - 

@article{
author = "Nestorović, Aleksandra and Jasnić, Jovana and Faulkner, Georgine and Radojković, Dragica and Kojić, Snežana",
year = "2014",
abstract = "The muscle ankyrin repeat protein Ankrd1 is localized in a mechanosensory complex of the sarcomeric I-band. It is involved in signaling pathways activated in response to mechanical stretch. It also acts as a transcriptional cofactor in the nucleus, playing an important role in cardiogenesis and skeletal muscle differentiation. To investigate its regulatory function in signaling we employed protein array methodology and identified 10 novel Ankrd1 binding partners among PDZ domain proteins known to act as platforms for multiprotein complex assembly. The zonula occludens protein-1 (ZO-1) was chosen for further analysis since its interaction with Ankrd2 had already been demonstrated. Both Ankrd2 and Ankrd1 have similar functions and localize in the same regions. We confirmed the interaction of Ankrd1 with ZO-1 protein and determined their subcellular distribution in HeLa cells, showing their colocalization in the cytoplasm. Our findings corroborate the role of Ankrd1 in intracellular signaling.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1",
pages = "1242-1233",
number = "3",
volume = "66",
doi = "10.2298/ABS1403233N"
}

Nestorović, A., Jasnić, J., Faulkner, G., Radojković, D.,& Kojić, S.. (2014). Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(3), 1233-1242.
https://doi.org/10.2298/ABS1403233N

Nestorović A, Jasnić J, Faulkner G, Radojković D, Kojić S. Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1. in Archives of Biological Sciences. 2014;66(3):1233-1242.
doi:10.2298/ABS1403233N .

Nestorović, Aleksandra, Jasnić, Jovana, Faulkner, Georgine, Radojković, Dragica, Kojić, Snežana, "Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1" in Archives of Biological Sciences, 66, no. 3 (2014):1233-1242,
https://doi.org/10.2298/ABS1403233N . .