help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rodgers, B. D.
Right arrow Articles by Levine, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rodgers, B. D.
Right arrow Articles by Levine, M. A.
Endocrinology Vol. 142, No. 4 1412-1418
Copyright © 2001 by The Endocrine Society


ARTICLES

Isolation and Characterization of Myostatin Complementary Deoxyribonucleic Acid Clones from Two Commercially Important Fish: Oreochromis mossambicus and Morone chrysops1

Buel D. Rodgers, Gregory M. Weber, Craig V. Sullivan and Michael A. Levine

Pediatric Endocrinology and The Ilyssa Center for Molecular and Cellular Endocrinology (B.D.R., M.A.L.), The Johns Hopkins University School of Medicine, Baltimore, Maryland 21287; and Department of Zoology (G.M.W., C.V.S.), North Carolina State University, Raleigh, North Carolina 27695

Address all correspondence and requests for reprints to: Dr. Buel D. Rodgers, Pediatric Endocrinology, The Johns Hopkins University School of Medicine, 600 North Wolf Street, Park 211, Baltimore, Maryland 21287. E-mail: drodgers{at}jhmi.edu

In mammals, skeletal muscle mass is negatively regulated by a muscle-derived growth/differentiating factor named myostatin (MSTN) that belongs to the transforming growth factor-ß superfamily. Although putative MSTN homologs have been identified from several vertebrates, nonmammalian orthologs remained poorly defined. Thus, we isolated and characterized MSTN complementary DNA clones from the skeletal muscle of the tilapia Oreochromis mossambicus and the white bass Morone chrysops. The nucleic and amino acid sequences from both fish species are highly homologous to the previously identified mammalian and avian orthologs, and both possess conserved cysteine residues and putative RXXR proteolytic processing sites that are common to all transforming growth factor-ß family members. Western blotting of conditioned medium from human embryonal kidney (HEK293) cells overexpressing a His-tagged tilapia MSTN indicates that the secreted fish protein is processed in a manner similar to mouse MSTN. However, in contrast to mice, MSTN expression in tilapia is not limited to skeletal muscle as it occurs in many tissues. Furthermore, the timing of MSTN expression in developing tilapia larvae coincides with myogenesis. These results suggest that the biological actions of MSTN in the tilapia and possibly in other fishes may not be limited to myocyte growth repression, but may additionally influence different cell types and organ systems.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 2001 by The Endocrine Society