Identification of secreted proteins during skeletal muscle development.
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.
Chan
X'avia C Y
XC
Department of Biology, Centre for Research in Mass Spectrometry, York University, 4700 Keele Street, Toronto, Ontario, Canada M3J 1P3.
McDermott
John C
JC
Siu
K W Michael
KW
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D051379:Mice; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000254:growth & development*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D014357:Trypsin
D009124:Muscle Proteins; D010446:Peptide Fragments; D014357:Trypsin