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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Shirriff, Cody S. Heikkila, John J. |
| Description | Country affiliation: Canada Author Affiliation: Shirriff CS ( Department of Biology, University of Waterloo, Waterloo, ON N2L 3G1, Canada.); Heikkila JJ ( Department of Biology, University of Waterloo, Waterloo, ON N2L 3G1, Canada. Electronic address: heikkila@uwaterloo.ca.) |
| Abstract | Endoplasmic reticulum (ER) stress can result in the accumulation of unfolded/misfolded protein in the ER lumen, which can trigger the unfolded protein response (UPR) resulting in the activation of various genes including immunoglobulin-binding protein (BiP; also known as glucose-regulated protein 78 or HSPA5). BiP, an ER heat shock protein 70 (HSP70) family member, binds to unfolded protein, inhibits their aggregation and re-folds them in an ATP-dependent manner. While cadmium, an environmental contaminant, was shown to induce the accumulation of HSP70 in vertebrate cells, less information is available regarding the effect of this metal on BiP accumulation or function. In this study, cadmium chloride treatment of Xenopus laevis A6 kidney epithelial cells induced a dose- and time-dependent increase in BiP, HSP70 and heme oxygenase-1 (HO-1) accumulation. Exposure of cells to a relatively low cadmium concentration at a mild heat shock temperature of 30°C greatly enhanced BiP and HSP70 accumulation compared to cadmium at 22°C. Treatment of cells with the glutathione synthesis inhibitor, buthionine sulfoximine, enhanced cadmium-induced BiP and HSP70 accumulation. Immunocytochemistry revealed that cadmium-induced BiP accumulation occurred in a punctate pattern in the perinuclear region. In some cells treated with cadmium chloride or the proteasomal inhibitor, MG132, large BiP complexes were observed that co-localized with aggregated protein or aggresome-like structures. These BiP/aggresome-like structures were also observed in cells treated simultaneously with cadmium at 30°C or in the presence of buthionine sulfoximine. In amphibians, the association of BiP with unfolded protein and its possible role in aggresome function may be vital in the maintenance of cellular proteostasis. |
| File Format | HTM / HTML |
| ISSN | 15320456 |
| Volume Number | 191 |
| Journal | Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2017-01-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Toxicology Discipline Pharmacology Cadmium Chloride Toxicity Environmental Pollutants Epithelial Cells Drug Effects Heat-shock Proteins Metabolism Kidney Xenopus Proteins Xenopus Laevis Animals Buthionine Sulfoximine Pharmacology Calcimycin Cell Line Dose-response Relationship, Drug Glutamate-cysteine Ligase Antagonists & Inhibitors Hsp70 Heat-shock Proteins Heat-shock Response Heme Oxygenase-1 Leupeptins Oxidative Stress Proteasome Inhibitors Time Factors Tunicamycin Unfolded Protein Response Up-regulation Journal Article |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Physiology Health, Toxicology and Mutagenesis Medicine Aquatic Science Biochemistry Toxicology Animal Science and Zoology |
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