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. © 2014 Springer Science+Business Media New York.
CITATION STYLE
Henningsen, J., Blagoev, B., & Kratchmarova, I. (2014). Analysis of secreted proteins using SILAC. Methods in Molecular Biology, 1188, 313–326. https://doi.org/10.1007/978-1-4939-1142-4_22
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