Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles
Autor: | Benedikt Schoser, Sabine Krause, Snezana Kojic, Slobodan Savic, Dragica Radojkovic, Olivia Schreiber-Katz, Johannes G. Vogel, Vlado Kovcic, Georgine Faulkner, Ljiljana Rakicevic, Ana Kojic, Maggie C. Walter, Jovana Jasnic-Savovic, Srdjan Boskovic, Aleksandra Nestorovic, Giorgio Valle |
---|---|
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Gene isoform ANKRD2 medicine.medical_specialty Histology Skeletal muscle Muscle Proteins Ankrd2 Biology 03 medical and health sciences Internal medicine medicine Humans Protein Isoforms Myocyte Amino Acid Sequence Muscle Skeletal Molecular Biology Cells Cultured Myogenesis Myocardium Heart Human Isoforms Cell Biology Medical Laboratory Technology Nuclear Proteins Cell biology Repressor Proteins 030104 developmental biology Endocrinology medicine.anatomical_structure Cytoplasm MYH7 Sequence Alignment Nuclear localization sequence |
Zdroj: | Histochemistry and Cell Biology. 146:569-584 |
ISSN: | 1432-119X 0948-6143 |
Popis: | 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. |
Databáze: | OpenAIRE |
Externí odkaz: |