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.
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Acknowledgments
We thank all CEBI group members for useful discussions. This work was supported by funding obtained from the Novo Nordisk Foundation, the Lundbeck Foundation, and the Augustinus Foundation.
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Henningsen, J., Blagoev, B., Kratchmarova, I. (2014). Analysis of Secreted Proteins Using SILAC. In: Warscheid, B. (eds) Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC). Methods in Molecular Biology, vol 1188. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1142-4_22
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DOI: https://doi.org/10.1007/978-1-4939-1142-4_22
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