Microgravity induces proteomics changes involved in endoplasmic reticulum stress and mitochondrial protection

To reveal outcomes of microgravity on molecular processes within the cellular environment we have employed a mass-spectrometry based proteomics approach. Proteomics analysis based on mass spectrometry allows for the relative quantitation of a large number of proteins concurrently, and in a relatively unbiased manner. Mass spectrometry based proteomics can be rendered even more informative by addition of a labeling component to understand the dynamics of the changing protein content. In this study, we utilized a combination of proteomics techniques, namely label-free quantification and dynamic stable-isotope labeling by amino acids in cell culture (Dynamic SILAC) to characterize the microgravity stress response in primary cardiomyocytes.