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Proteome analysis of tunicamycin‐induced ER stress
Author(s) -
Bull Vibeke Hervik,
Thiede Bernd
Publication year - 2012
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100565
Subject(s) - tunicamycin , unfolded protein response , stable isotope labeling by amino acids in cell culture , endoplasmic reticulum , protein disulfide isomerase , proteome , protein folding , downregulation and upregulation , endoplasmic reticulum associated protein degradation , microbiology and biotechnology , chemistry , protein biosynthesis , biochemistry , biology , proteomics , gene
Endoplasmic reticulum ( ER ) stress occurs upon increased levels of unfolded proteins and results in activation of cellular responses such as the unfolded protein response ( UPR ) and ER ‐associated protein degradation ( ERAD ). To examine ER stress, we performed a quantitative proteome analysis of human neuroblastoma cells using stable isotope labeling with amino acids in cell culture ( SILAC ) in combination with SDS ‐ PAGE and LC ‐ MS / MS . Proteins associated with the ER were overrepresented in the dataset of altered proteins. In particular, ER chaperones responsible for protein folding were significantly upregulated in response to ER stress. The important ER stress regulator 78 k D a glucose‐regulated protein ( GRP ‐78 or B i P ) was highly upregulated together with several proteins that have been found to form a multiprotein complex with B i P including cyclophilin B , D na J homolog subfamily B member 11, endoplasmin, hypoxia upregulated protein 1, protein disulfide isomerase and protein disulfide isomerase A 4 upon tunicamycin‐induced ER stress. Furthermore, seven aminoacyl‐t RNA synthetases and five proteins belonging to the S ec61 complex were increased in response to tunicamycin‐induced ER stress.