TY  - JOUR
AU  - Rakićević, Ljiljana
AU  - Nestorović, Aleksandra
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1277
AB  - Genetics has given a real boost to personalized and precision medicine, providing data used either for precise diagnostics, prediction of the course of illness, or for selecting therapy and tailoring it. Pharmacogenetics, as a discipline researching connection between genetic background of an individual and the effect of a certain drug, has created new possibilities in medicine. One of the most researched drugs in pharmacogenetics is certainly clopidogrel.
PB  - Wiley, Hoboken
T2  - Clinical Pharmacology & Therapeutics
T1  - Pharmacogenetics of Clopidogrel Therapy and Neurointerventional Procedures: We Need Precision Data for Precision Medicine
EP  - 549
IS  - 3
SP  - 547
VL  - 105
DO  - 10.1002/cpt.1105
ER  - 

@article{
author = "Rakićević, Ljiljana and Nestorović, Aleksandra",
year = "2019",
abstract = "Genetics has given a real boost to personalized and precision medicine, providing data used either for precise diagnostics, prediction of the course of illness, or for selecting therapy and tailoring it. Pharmacogenetics, as a discipline researching connection between genetic background of an individual and the effect of a certain drug, has created new possibilities in medicine. One of the most researched drugs in pharmacogenetics is certainly clopidogrel.",
publisher = "Wiley, Hoboken",
journal = "Clinical Pharmacology & Therapeutics",
title = "Pharmacogenetics of Clopidogrel Therapy and Neurointerventional Procedures: We Need Precision Data for Precision Medicine",
pages = "549-547",
number = "3",
volume = "105",
doi = "10.1002/cpt.1105"
}

Rakićević, L.,& Nestorović, A.. (2019). Pharmacogenetics of Clopidogrel Therapy and Neurointerventional Procedures: We Need Precision Data for Precision Medicine. in Clinical Pharmacology & Therapeutics
Wiley, Hoboken., 105(3), 547-549.
https://doi.org/10.1002/cpt.1105

Rakićević L, Nestorović A. Pharmacogenetics of Clopidogrel Therapy and Neurointerventional Procedures: We Need Precision Data for Precision Medicine. in Clinical Pharmacology & Therapeutics. 2019;105(3):547-549.
doi:10.1002/cpt.1105 .

Rakićević, Ljiljana, Nestorović, Aleksandra, "Pharmacogenetics of Clopidogrel Therapy and Neurointerventional Procedures: We Need Precision Data for Precision Medicine" in Clinical Pharmacology & Therapeutics, 105, no. 3 (2019):547-549,
https://doi.org/10.1002/cpt.1105 . .

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  - 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  - Đorđević, Valentina
AU  - Pruner, Iva
AU  - Tomić, Branko
AU  - Nestorović, Aleksandra
AU  - Gvozdenov, Maja
AU  - Kovač, Mirjana
AU  - Radojković, Dragica
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/739
AB  - Background: Prothrombin (FII) A19911G and C20221T gene variants are associated with increased prothrombin levels and potentially represent thrombotic risk factors. Objective: To determine the frequency of A19911G and C20221T FII gene variants in patients with thrombotic disorders and in women who have experienced pregnancy loss (PL). Methods: We determined the frequency of these variants in 133 patients with deep venous thrombosis (DVT), 80 patients with isolated pulmonary embolism (PE), 101 patients with idiopathic PL, and 180 control individuals. Results: The FII A19911G variant was more prevalent in patients with DVT and with PL compared with controls; however, these differences were not statistically significant. The 19911GG genotype was associated with increased risk of PE (odds ratio, 1.91; 95% confidence interval, 1.04-3.51). We did not detect carriers of the FII C20221T gene variant in this study. Conclusions: This is the first study, to our knowledge, that demonstrates the FII 1991199 genotype may represent a risk factor for isolated PE. Also, our results show that the FII C20221T is a rare variant in this population and therefore, routine thrombophilia screening should not include screening for this genotype.
PB  - Amer Soc Clinical Pathology, Chicago
T2  - Laboratory Medicine
T1  - The 3 ' End Prothrombin Gene Variants in Patients With Different Thrombotic Events
EP  - 311
IS  - 4
SP  - 307
VL  - 45
DO  - 10.1309/LM8E84ZSLPDMWZCM
ER  - 

@article{
author = "Đorđević, Valentina and Pruner, Iva and Tomić, Branko and Nestorović, Aleksandra and Gvozdenov, Maja and Kovač, Mirjana and Radojković, Dragica",
year = "2014",
abstract = "Background: Prothrombin (FII) A19911G and C20221T gene variants are associated with increased prothrombin levels and potentially represent thrombotic risk factors. Objective: To determine the frequency of A19911G and C20221T FII gene variants in patients with thrombotic disorders and in women who have experienced pregnancy loss (PL). Methods: We determined the frequency of these variants in 133 patients with deep venous thrombosis (DVT), 80 patients with isolated pulmonary embolism (PE), 101 patients with idiopathic PL, and 180 control individuals. Results: The FII A19911G variant was more prevalent in patients with DVT and with PL compared with controls; however, these differences were not statistically significant. The 19911GG genotype was associated with increased risk of PE (odds ratio, 1.91; 95% confidence interval, 1.04-3.51). We did not detect carriers of the FII C20221T gene variant in this study. Conclusions: This is the first study, to our knowledge, that demonstrates the FII 1991199 genotype may represent a risk factor for isolated PE. Also, our results show that the FII C20221T is a rare variant in this population and therefore, routine thrombophilia screening should not include screening for this genotype.",
publisher = "Amer Soc Clinical Pathology, Chicago",
journal = "Laboratory Medicine",
title = "The 3 ' End Prothrombin Gene Variants in Patients With Different Thrombotic Events",
pages = "311-307",
number = "4",
volume = "45",
doi = "10.1309/LM8E84ZSLPDMWZCM"
}

Đorđević, V., Pruner, I., Tomić, B., Nestorović, A., Gvozdenov, M., Kovač, M.,& Radojković, D.. (2014). The 3 ' End Prothrombin Gene Variants in Patients With Different Thrombotic Events. in Laboratory Medicine
Amer Soc Clinical Pathology, Chicago., 45(4), 307-311.
https://doi.org/10.1309/LM8E84ZSLPDMWZCM

Đorđević V, Pruner I, Tomić B, Nestorović A, Gvozdenov M, Kovač M, Radojković D. The 3 ' End Prothrombin Gene Variants in Patients With Different Thrombotic Events. in Laboratory Medicine. 2014;45(4):307-311.
doi:10.1309/LM8E84ZSLPDMWZCM .

Đorđević, Valentina, Pruner, Iva, Tomić, Branko, Nestorović, Aleksandra, Gvozdenov, Maja, Kovač, Mirjana, Radojković, Dragica, "The 3 ' End Prothrombin Gene Variants in Patients With Different Thrombotic Events" in Laboratory Medicine, 45, no. 4 (2014):307-311,
https://doi.org/10.1309/LM8E84ZSLPDMWZCM . .

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 . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Belgrano, Anna
AU  - Stanković, Marija
AU  - Divac Rankov, Aleksandra
AU  - Faulkner, Georgine
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/445
AB  - The muscle ankyrin repeat protein (MARP) family member Ankrd1/CARP is a part of the titin-mechanosensory signaling complex in the sarcomere and in response to stretch it translocates to the nucleus where it participates in the regulation of cardiac genes as a transcriptional co-repressor. Several studies have focused on its structural role in muscle, but its regulatory role is still poorly understood To gain more insight into the regulatory function of Ankrd1/CARP we searched for transcription factors that could interact and modulate its activity. Using protein array methodology we identified the tumor suppressor protein p53 as an Ankrd1/CARP interacting partner and confirmed their interaction both in vivo and in vitro We demonstrate a novel role for Ankrd1/CARP as a transcriptional co-activator, moderately up regulating p53 activity Furthermore, we show that p53 operates as an upstream effector of Ankrd1/CARP, by up regulating the proximal ANKRD1 promoter Our findings suggest that, besides acting as a transcriptional co-repressor, Ankrd1/CARP could have a stimulatory effect on gene expression in cultured skeletal muscle cells It is probable that Ankrd1 /CARP has a role in the propagation of signals initiated by myogenic regulatory factors (MRFs) during myogenesis
PB  - Elsevier Science Inc, New York
T2  - Archives of Biochemistry and Biophysics
T1  - A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein
EP  - 67
IS  - 1
SP  - 60
VL  - 502
DO  - 10.1016/j.abb.2010.06.029
ER  - 

@article{
author = "Kojić, Snežana and Nestorović, Aleksandra and Rakićević, Ljiljana and Belgrano, Anna and Stanković, Marija and Divac Rankov, Aleksandra and Faulkner, Georgine",
year = "2010",
abstract = "The muscle ankyrin repeat protein (MARP) family member Ankrd1/CARP is a part of the titin-mechanosensory signaling complex in the sarcomere and in response to stretch it translocates to the nucleus where it participates in the regulation of cardiac genes as a transcriptional co-repressor. Several studies have focused on its structural role in muscle, but its regulatory role is still poorly understood To gain more insight into the regulatory function of Ankrd1/CARP we searched for transcription factors that could interact and modulate its activity. Using protein array methodology we identified the tumor suppressor protein p53 as an Ankrd1/CARP interacting partner and confirmed their interaction both in vivo and in vitro We demonstrate a novel role for Ankrd1/CARP as a transcriptional co-activator, moderately up regulating p53 activity Furthermore, we show that p53 operates as an upstream effector of Ankrd1/CARP, by up regulating the proximal ANKRD1 promoter Our findings suggest that, besides acting as a transcriptional co-repressor, Ankrd1/CARP could have a stimulatory effect on gene expression in cultured skeletal muscle cells It is probable that Ankrd1 /CARP has a role in the propagation of signals initiated by myogenic regulatory factors (MRFs) during myogenesis",
publisher = "Elsevier Science Inc, New York",
journal = "Archives of Biochemistry and Biophysics",
title = "A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein",
pages = "67-60",
number = "1",
volume = "502",
doi = "10.1016/j.abb.2010.06.029"
}

Kojić, S., Nestorović, A., Rakićević, L., Belgrano, A., Stanković, M., Divac Rankov, A.,& Faulkner, G.. (2010). A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein. in Archives of Biochemistry and Biophysics
Elsevier Science Inc, New York., 502(1), 60-67.
https://doi.org/10.1016/j.abb.2010.06.029

Kojić S, Nestorović A, Rakićević L, Belgrano A, Stanković M, Divac Rankov A, Faulkner G. A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein. in Archives of Biochemistry and Biophysics. 2010;502(1):60-67.
doi:10.1016/j.abb.2010.06.029 .

Kojić, Snežana, Nestorović, Aleksandra, Rakićević, Ljiljana, Belgrano, Anna, Stanković, Marija, Divac Rankov, Aleksandra, Faulkner, Georgine, "A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein" in Archives of Biochemistry and Biophysics, 502, no. 1 (2010):60-67,
https://doi.org/10.1016/j.abb.2010.06.029 . .