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J Proteome Res. 2007 Feb;6(2):698-710.

Identification of secreted proteins during skeletal muscle development.

Author information

1
Department of Biology, Centre for Research in Mass Spectrometry, York University, 4700 Keele Street, Toronto, Ontario, Canada M3J 1P3.

Abstract

The differentiation program of skeletal muscle cells is exquisitely sensitive to secreted proteins. We developed a strategy to maximize the discovery of secreted proteins, using mass spectrometry-based proteomics, from cultured muscle cells, C2C12, grown in a serum-free medium. This strategy led to the identification of 80 nonredundant proteins, of which 27 were secretory proteins that were identified with a minimum of two tryptic peptides. A number of the identified secretory proteins are involved in extracellular matrix remodeling, cellular proliferation, migration, and signaling. A putative network of proteins involving matrix metalloproteinase 2, SPARC, and cystatin C that all interact with TGFbeta signaling has been postulated to contribute toward a functional role in the myogenic differentiation program.

PMID:
17269726
DOI:
10.1021/pr060448k
[Indexed for MEDLINE]

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