Literature DB >> 15473835

Regulation of muscle mass by myostatin.

Se-Jin Lee1.   

Abstract

Myostatin is a secreted protein that acts as a negative regulator of skeletal muscle mass. During embryogenesis, myostatin is expressed by cells in the myotome and in developing skeletal muscle and acts to regulate the final number of muscle fibers that are formed. During adult life, myostatin protein is produced by skeletal muscle, circulates in the blood, and acts to limit muscle fiber growth. The existence of circulating tissue-specific growth inhibitors of this type was hypothesized over 40 years ago to explain how sizes of individual tissues are controlled. Skeletal muscle appears to be the first example of a tissue whose size is controlled by this type of regulatory mechanism, and myostatin appears to be the first example of the long-sought chalone.

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Year:  2004        PMID: 15473835     DOI: 10.1146/annurev.cellbio.20.012103.135836

Source DB:  PubMed          Journal:  Annu Rev Cell Dev Biol        ISSN: 1081-0706            Impact factor:   13.827


  287 in total

1.  Organization and functional analysis of the 5' flanking regions of myostatin-1 and 2 genes from Larimichthys crocea.

Authors:  Liangyi Xue; Xiaojing Dong; Xiaoju Zhang; Amadou Diallo
Journal:  DNA Cell Biol       Date:  2011-12-07       Impact factor: 3.311

2.  The influence of skeletal muscle on the regulation of liver:body mass and liver regeneration.

Authors:  Jiansheng Huang; Martin Glauber; Zhaohua Qiu; Vered Gazit; Dennis J Dietzen; David A Rudnick
Journal:  Am J Pathol       Date:  2011-12-05       Impact factor: 4.307

3.  Administration of a soluble activin type IIB receptor promotes skeletal muscle growth independent of fiber type.

Authors:  Samuel M Cadena; Kathleen N Tomkinson; Travis E Monnell; Matthew S Spaits; Ravindra Kumar; Kathryn W Underwood; R Scott Pearsall; Jennifer L Lachey
Journal:  J Appl Physiol (1985)       Date:  2010-05-13

4.  Normalizing RT-qPCR data: are we getting the right answers? An appraisal of normalization approaches and internal reference genes from a case study in the finfish Lates calcarifer.

Authors:  Christian De Santis; Carolyn Smith-Keune; Dean R Jerry
Journal:  Mar Biotechnol (NY)       Date:  2010-03-23       Impact factor: 3.619

5.  METABOLIC FUNCTIONS OF MYOSTATIN AND GDF11.

Authors:  Alexandra C McPherron
Journal:  Immunol Endocr Metab Agents Med Chem       Date:  2010-12

6.  Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production.

Authors:  Elisabeth R Barton; SooHyun Park; Jose K James; Catherine A Makarewich; Anastassios Philippou; Davide Eletto; Hanqin Lei; Becky Brisson; Olga Ostrovsky; Zihai Li; Yair Argon
Journal:  FASEB J       Date:  2012-05-30       Impact factor: 5.191

7.  Sulforaphane causes a major epigenetic repression of myostatin in porcine satellite cells.

Authors:  Huitao Fan; Rui Zhang; Dawit Tesfaye; Ernst Tholen; Christian Looft; Michael Hölker; Karl Schellander; Mehmet Ulas Cinar
Journal:  Epigenetics       Date:  2012-10-23       Impact factor: 4.528

Review 8.  Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions.

Authors:  Maria A Gubbiotti; Sylvain D Vallet; Sylvie Ricard-Blum; Renato V Iozzo
Journal:  Matrix Biol       Date:  2016-09-30       Impact factor: 11.583

9.  High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo.

Authors:  Michiko Yamada; Ryuichi Tatsumi; Keitaro Yamanouchi; Tohru Hosoyama; Sei-ichi Shiratsuchi; Akiko Sato; Wataru Mizunoya; Yoshihide Ikeuchi; Mitsuhiro Furuse; Ronald E Allen
Journal:  Am J Physiol Cell Physiol       Date:  2009-12-09       Impact factor: 4.249

10.  Myostatin and follistatin expression in skeletal muscles of rats with chronic heart failure.

Authors:  Aline Regina Ruiz Lima; Paula Felippe Martinez; Katashi Okoshi; Daniele Mendes Guizoni; Leonardo A Mamede Zornoff; Dijon Henrique Salomé Campos; Sílvio Assis Oliveira; Camila Bonomo; Maeli Dal Pai-Silva; Marina Politi Okoshi
Journal:  Int J Exp Pathol       Date:  2009-12-03       Impact factor: 1.925

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