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Regulation of Myostatin in Vivo by Growth and Differentiation Factor-Associated Serum Protein-1: A Novel Protein with Protease Inhibitor and Follistatin
| Citations: | 12 - 0 self |
BibTeX
@MISC{Hill_regulationof,
author = {Jennifer J. Hill and Yongchang Qiu and Rodney M. Hewick and Neil and M. Wolfman},
title = {Regulation of Myostatin in Vivo by Growth and Differentiation Factor-Associated Serum Protein-1: A Novel Protein with Protease Inhibitor and Follistatin},
year = {}
}
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Abstract
Myostatin, a member of the TGF � superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene (FLRG). Here, we report the identification of an additional protein associated with endogenous myostatin in normal mouse and human serum, discovered by affinity purification and mass spectrometry. This protein, which we have named growth and differentiation factor-associated serum protein-1 (GASP-1), contains multiple domains associated with protease-inhibitory proteins, including a whey acidic protein domain, a Kazal domain, two Kunitz domains, and a netrin domain. GASP-1 also contains
Keyphrases
differentiation factor-associated serum protein-1 protease inhibitor novel protein latent complex specific negative regulator affinity purification multiple domain whey acidic protein domain protease-inhibitory protein netrin domain skeletal muscle mass myostatin circulates additional protein endogenous myostatin mass spectrometry myostatin propeptide human serum kunitz domain kazal domain normal mouse follistatin-related gene
