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.
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| description | 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. |
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| identifier | 10.26030/j21n-tx59 |
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| modified | 2025-08-21 |
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| title | Microgravity induces proteomics changes involved in endoplasmic reticulum stress and mitochondrial protection |
