title: Analysis of secreted proteins using SILAC.
abstract: Secreted proteins serve a crucial role in the communication between cells, tissues, and organs. Proteins released to the extracellular environment exert their function either locally or at distant points of the organism. Proteins are secreted in a highly dynamic fashion by cells and tissues in the body responding to the stimuli and requirements presented by the extracellular milieu. Characterization of secretomes derived from various cell types has been performed using different quantitative mass spectrometry-based proteomics strategies, several of them taking advantage of labeling with stable isotopes. Here, we describe the use of Stable Isotope Labeling by Amino acids in Cell culture (SILAC) for the quantitative analysis of the skeletal muscle secretome during myogenesis.
authors: Center for Experimental BioInformatics (CEBI), Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230, Odense, Denmark.
authors: Jeanette
authors: J
authors: Henningsen
authors: Blagoy
authors: B
authors: Blagoev
authors: Irina
authors: I
authors: Kratchmarova
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D002460:Cell Line; D002853:Chromatography, Liquid; D017077:Culture Media, Conditioned; D007553:Isotope Labeling / Q000379:methods*; D051379:Mice; D018482:Muscle, Skeletal / Q000166:cytology; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D059748:Proteolysis; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry
chemical_list: D000596:Amino Acids; D017077:Culture Media, Conditioned; D011506:Proteins