Cloning and expression profiling of muscle regulator ANKRD2 in domestic chicken Gallus gallus

• Published in: Histochemistry and cell biology 2020-10, Vol.154 (4), p.383-396
• Main Authors: Stamenkovic, Nemanja, Jasnic, Jovana, Novkovic, Mirjana, Milosevic, Emilija, Boskovic, Srdjan, Kojic, Ana, Popic, Kristina, Stankovic, Marija, Wang, Yajun, Milenkovic, Sanja, Radojkovic, Dragica, Ma, Guoda, Kojic, Snezana
• Format: Article
• Language: English
• Subjects: Animals; Ankyrins; Biochemistry; Biomedical and Life Sciences; Biomedicine; Cell Biology; Chickens; Cloning; Cloning, Molecular; Developmental Biology; Gene expression; Gene Expression Profiling; Glycolysis; Immunohistochemistry; Molecular modelling; Muscle Proteins - genetics; Muscle Proteins - metabolism; Muscle, Skeletal - metabolism; Myogenesis; Original Paper; Oxidative metabolism; Proteins; Skeletal muscle; Transcription
• ISSN: 0948-6143; 1432-119X
• DOI: 10.1007/s00418-020-01899-1

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 chicken ANKRD2 . The chicken ANKRD2 coding 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 the ANKRD2 gene 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 chicken ANKRD2 with 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 that ANKRD2 is 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.