Nuclear cytoplasmic trafficking of proteins is a major response of human fibroblasts to oxidative stress.

ABSTRACT: We have used a subcellular spatial razor approach based on LC-MS/MS-based proteomics with SILAC isotope labeling to determine changes in protein abundances in the nuclear and cytoplasmic compartments of human IMR90 fibroblasts subjected to mild oxidative stress. We show that response to mild tert-butyl hydrogen peroxide treatment includes redistribution between the nucleus and cytoplasm of numerous proteins not previously associated with oxidative stress. The 121 proteins with the most significant changes encompass proteins with known functions in a wide variety of subcellular locations and of cellular functional processes (transcription, signal transduction, autophagy, iron metabolism, TCA cycle, ATP synthesis) and are consistent with functional networks that are spatially dispersed acros

SUBMITTER: Baqader NO 

PROVIDER: S-EPMC4259009 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature