2/28/2024 0 Comments Er lumen oxidizingReducing agents disrupt the oxidizing ER environment critical for disulfide bond formation, which leads to accumulation of unfolded and misfolded proteins causing ER stress. The ER lumen has a high calcium concentration and an oxidizing environment compared to the cytosol that are important for normal ER chaperone function and for proper folding of proteins that contain disulfide bonds –. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist.īiosynthesis, folding and maturation of membrane and secretory proteins occur in the ER. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: Funding was provided by the Canadian Institutes of Health Research (CIHR, MOP-114922 ). Received: JAccepted: OctoPublished: November 8, 2012Ĭopyright: © 2012 Schuiki et al. University of Pittsburgh, United States of America Thus, unlike in yeast cells, ER stress in pancreatic β-cells is not associated with a more reducing ER environment.Ĭitation: Schuiki I, Zhang L, Volchuk A (2012) Endoplasmic Reticulum Redox State Is Not Perturbed by Pharmacological or Pathological Endoplasmic Reticulum Stress in Live Pancreatic β-Cells. Comparable results were obtained with dispersed rat islet cells expressing eroGFP. Unexpectedly however, other treatments including tunicamycin, thapsigargin, DL-homocysteine, elevated free fatty acids or high glucose had essentially no influence on the ER redox state, despite inducing ER stress. As expected, treatment of the cells with the reducing agent dithiothreitol caused a decrease in the oxidation state of the ER accompanied by an increase in XBP-1 splicing. Live cell imaging, flow cytometry and biochemical characterization were used to examine these parameters in response to various conditions known to induce ER stress. Here we monitored ER redox together with transcriptional output of the Unfolded Protein Response (UPR) in INS-1 insulinoma cells stably expressing eroGFP (ER-redox-sensor) and mCherry protein driven by a GRP78 promoter (UPR-sensor). ER stress can result from physiological situations such as acute increases in secretory protein biosynthesis or pathological conditions that perturb ER homeostasis such as alterations in the ER redox state. Accumulation of unfolded, misfolded and aggregated proteins in the endoplasmic reticulum (ER) causes ER stress.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |