Unknown

Dataset Information

0

Proteomic profiling of differentially expressed proteins from Bax inhibitor-1 knockout and wild type mice.


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. Selenium-binding protein 2 (SBP2) and ferritin light chain 1 levels were significantly increased. Phosphatidylethanolamine-binding 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.

SUBMITTER: Li B 

PROVIDER: S-EPMC3887783 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Proteomic profiling of differentially expressed proteins from Bax inhibitor-1 knockout and wild type mice.

Li Bo B   Reed John C JC   Kim Hyung-Ryong HR   Chae Han-Jung HJ  

Molecules and cells 20120625 1


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 spect  ...[more]

Similar Datasets

| S-EPMC5319751 | biostudies-literature
| S-EPMC7561244 | biostudies-literature
| S-EPMC9147329 | biostudies-literature
| S-EPMC10154561 | biostudies-literature
| S-EPMC7657203 | biostudies-literature
| S-EPMC3848938 | biostudies-literature
| S-EPMC5482134 | biostudies-literature
| S-EPMC4224989 | biostudies-literature
| S-EPMC6154836 | biostudies-literature
| S-EPMC2743659 | biostudies-literature