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Proteomic screening of glucose‐responsive and glucose non‐responsive MIN‐6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress
Author(s) -
Dowling Paul,
O'Driscoll Lorraine,
O'Sullivan Finbarr,
Dowd Andrew,
Henry Michael,
Jeppesen Per Bendix,
Meleady Paula,
Clynes Martin
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600298
Subject(s) - endoplasmic reticulum , unfolded protein response , protein disulfide isomerase , secretory protein , secretion , oxidative stress , proteome , glucose regulated protein , biochemistry , biology , superoxide dismutase , chemistry , microbiology and biotechnology
The glucose‐sensitive insulin‐secretion (GSIS) phenotype is relatively unstable in long‐term culture of beta cells. The purpose of this study was to investigate relative changes in the proteome between glucose‐responsive (low passage) and glucose non‐responsive (high passage) murine MIN‐6 pancreatic beta cells. The 2D‐DIGE and subsequent DeCyder analysis detected 3351 protein spots in the pH range of 4–7. Comparing MIN‐6(H) to MIN‐6(L) and using a threshold of 1.2‐fold, the number of proteins with a decrease in expression level was 152 (4.5%), similar was 3140 (93.7%) and increased 59 (1.8%). From the differentially expressed proteins identified in this study, groups of proteins associated with the endoplasmic reticulum (ER) and proteins involved in oxidative stress were found to be significantly decreased in the high‐passage (H passage) cells. These proteins included endoplasmic reticulum protein 29 (ERp29); 78‐kDa glucose‐related protein, (GRP78); 94‐kDa glucose‐related protein (GRP94); protein disulphide isomerase; carbonyl reductase 3; peroxidoxin 4 and superoxide dismutase 1. These results suggest that non‐GSIS MIN‐6 cells do not have the same ability/capacity of glucose‐responsive MIN‐6 cells to successfully fold, modify or secrete proteins and counteract the problems associated with oxidative stress.