Literature DB >> 15075916

Myostatin: a therapeutic target for skeletal muscle wasting.

Stephen M Roth1, Sean Walsh.   

Abstract

PURPOSE OF REVIEW: This review discusses recent developments in myostatin research, focusing on the basic actions of myostatin on skeletal muscle, the identification of key regulatory elements of the myostatin pathway, and the promise of myostatin as a therapeutic target in muscle-related disorders. RECENT
FINDINGS: In addition to a well-characterized role in muscle development, recent research advances have solidified the importance of myostatin in adult muscle, although questions remain. A number of possible regulatory proteins for myostatin have been identified, showing a complex picture of myostatin regulation that requires clarification. The identification of an antimyostatin monoclonal antibody (JA16) shows the promise of myostatin as a target for muscle-wasting disorders; the antibody has already been shown to increase muscle mass in healthy older mice and muscle function in postnatal mdx mice.
SUMMARY: Since its discovery in 1997, myostatin has quickly been established as a key regulator of skeletal muscle mass. Recent developments strengthen the idea that myostatin will be an important therapeutic target for muscle-wasting-related disorders, and as more details of myostatin regulation and its mechanisms of action are clarified, myostatin will continue to dominate the skeletal muscle development and muscle-wasting literature.

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Year:  2004        PMID: 15075916     DOI: 10.1097/00075197-200405000-00004

Source DB:  PubMed          Journal:  Curr Opin Clin Nutr Metab Care        ISSN: 1363-1950            Impact factor:   4.294


  12 in total

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Authors:  Christopher L Mendias; James E Marcin; Daniel R Calerdon; John A Faulkner
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Authors:  Hang Wang; Tsung-Lin Li; Simon Hsia; I-Li Su; Yi-Lin Chan; Chang-Jer Wu
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7.  Targeted Myostatin Gene Editing in Multiple Mammalian Species Directed by a Single Pair of TALE Nucleases.

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8.  Latent myostatin has significant activity and this activity is controlled more efficiently by WFIKKN1 than by WFIKKN2.

Authors:  György Szláma; Mária Trexler; László Patthy
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Journal:  FASEB J       Date:  2016-10-12       Impact factor: 5.191

10.  Overexpression of Latent TGFβ Binding Protein 4 in Muscle Ameliorates Muscular Dystrophy through Myostatin and TGFβ.

Authors:  Kay-Marie Lamar; Sasha Bogdanovich; Brandon B Gardner; Quan Q Gao; Tamari Miller; Judy U Earley; Michele Hadhazy; Andy H Vo; Lisa Wren; Jeffery D Molkentin; Elizabeth M McNally
Journal:  PLoS Genet       Date:  2016-05-05       Impact factor: 5.917

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