Abstract
Bax inhibitor-1 (BI-1) is an anti-apoptotic protein located in the endoplasmic reticulum (ER). The role of BI-1 has been studied in different physiopathological models including ischemia, diabetes, liver regeneration and cancer. However, fundamental knowledge about the effects of BI-1 deletion on the proteome is lacking. To further explore this protein, we compared the levels of different proteins in bi-1 −/− and bi-1 +/+ mouse tissues by two-dimensional electrophoresis (2-DE) and mass spectrometry (MS). In several bi-1 −/− mice, glucose-regulated protein 75 (GRP75/mortalin/ PBP74/mthsp70), peroxiredoxin6 (Prx6) and fumarylacetoacetate hydrolase (FAH) showed a pI shift that could be attributed to post-translational modifications. Seleniumbinding protein 2 (SBP2) and ferritin light chain 1 levels were significantly increased. Phosphatidylethanolaminebinding protein-1 (PEBP-1) was dramatically decreased in bi-1 −/− mice, which was confirmed by Western blotting. The phosphorylation of GRP75, Prx6 and FAH were compared between bi-1 +/+ and bi-1 −/− mice using liver tissue lysates. Of these three proteins, only one exhibited modified phosphorylation; Tyr phosphorylation of Prx6 was increased in bi-1 −/− mice. Our protein profiling results provide fundamental knowledge about the physiopathological function of BI-1.
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Li, B., Reed, J.C., Kim, HR. et al. Proteomic profiling of differentially expressed proteins from Bax inhibitor-1 knockout and wild type mice. Mol Cells 34, 15–23 (2012). https://doi.org/10.1007/s10059-012-0001-x
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DOI: https://doi.org/10.1007/s10059-012-0001-x