Molecular cloning of the Atlantic salmon activin receptor IIB cDNA - Localization of the receptor and myostatin in vivo and in vitro in muscle cells

Tone-Kari K Ostbye; Tora Bardal; Anne Vegusdal; Ola T Frang; Elin Kjørsvik; Oivind Andersen

doi:10.1016/j.cbd.2006.12.003

Molecular cloning of the Atlantic salmon activin receptor IIB cDNA - Localization of the receptor and myostatin in vivo and in vitro in muscle cells

Comp Biochem Physiol Part D Genomics Proteomics. 2007 Jun;2(2):101-11. doi: 10.1016/j.cbd.2006.12.003. Epub 2007 Jan 23.

Authors

Tone-Kari K Ostbye¹, Tora Bardal, Anne Vegusdal, Ola T Frang, Elin Kjørsvik, Oivind Andersen

Affiliation

¹ Institute of Aquaculture Research, P.O. Box 5010, N-1432 As, Norway.

PMID: 20483283
DOI: 10.1016/j.cbd.2006.12.003

Abstract

In mammals, the activin receptor type IIB (ActRIIB) binds with high affinity several members of the transforming growth factor-beta (TGF-beta) superfamily, including the negative muscle regulator myostatin (MSTN). In this study, an actRIIB cDNA of 1443 bp was isolated by reverse transcription (RT)-PCR from the liver of Atlantic salmon (Salmo salar) encoding almost the complete receptor. The deduced salmon ActRIIB of 481 amino acids (aa) contained the conserved catalytic domain of serine/threonine protein kinases, and showed the highest sequence identity (83-87%) to the zebrafish, chicken and goldfish ActRIIB. Salmon actRIIB mRNA was identified by RT-PCR in all the examined tissues of juvenile fish that was confirmed by in situ hybridization. In comparison, the salmon MSTN signal was less widespread, and co-expression of the receptor and this putative ligand was only demonstrated in skeletal muscle. Consistently, both ActRIIB and MSTN were immunocytologically identified in salmon myoblasts and differentiated myotubes in culture.