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  - 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 . .