Accumulation of heme oxygenase-1 (HSP32) in Xenopus laevis A6 kidney epithelial cells treated with sodium arsenite, cadmium chloride or proteasomal inhibitors
Data(s) |
23/07/2014
|
---|---|
Resumo |
The present study examined the effect of sodium arsenite, cadmium chloride, heat shock and the proteasomal inhibitors MG132, withaferin A and celastrol on heme oxygenase-1 (HO-1; also known as HSP32) accumulation in Xenopus laevis A6 kidney epithelial cells. Immunoblot analysis revealed that HO-1 accumulation was not induced by heat shock but was enhanced by sodium arsenite and cadmium chloride in a dose- and time-dependent fashion. Immunocytochemistry revealed that these metals induced HO-1 accumulation in a granular pattern primarily in the cytoplasm. Additionally, in 20% of the cells arsenite induced the formation of large HO-1-containing perinuclear structures. In cells recovering from sodium arsenite or cadmium chloride treatment, HO-1 accumulation initially increased to a maximum at 12h followed by a 50% reduction at 48 h. This initial increase in HO-1 levels was likely the result of new synthesis as it was inhibited by cycloheximide. Interestingly, treatment of cells with a mild heat shock enhanced HO-1 accumulation induced by low concentrations of sodium arsenite and cadmium chloride. Finally, we determined that HO-1 accumulation was induced in A6 cells by the proteasomal inhibitors, MG132, withaferin A and celastrol. An examination of heavy metal and proteasomal inhibitor-induced HO-1 accumulation in amphibians is of importance given the presence of toxic heavy metals in aquatic habitats. |
Formato |
application/pdf |
Identificador | |
Publicador |
Elsevier |
Relação |
http://eprints.qut.edu.au/78347/1/CBP_MS23697-2_Manuscript_from_Revision_2.pdf DOI:10.1016/j.cbpc.2014.07.007 Music, Ena, Khan, Saad, Khamis, Imran, & Heikkila, John J. (2014) Accumulation of heme oxygenase-1 (HSP32) in Xenopus laevis A6 kidney epithelial cells treated with sodium arsenite, cadmium chloride or proteasomal inhibitors. Comparative Biochemistry and Physiology Part C : Toxicology & Pharmacology, 166, pp. 75-87. NSERC/NSERC-RGPIN2820-09 29883 |
Direitos |
Copyright 2014 Elsevier This is the author’s version of a work that was accepted for publication in Comparative Biochemistry and Physiology Part C. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Comparative Biochemistry and Physiology Part C, [VOL 166, (2014)] DOI: 10.1016/j.cbpc.2014.07.007 |
Fonte |
School of Biomedical Sciences; Faculty of Health; Institute of Health and Biomedical Innovation |
Palavras-Chave | #060000 BIOLOGICAL SCIENCES #060100 BIOCHEMISTRY AND CELL BIOLOGY #060802 Animal Cell and Molecular Biology #111506 Toxicology (incl. Clinical Toxicology) #Xenopus #Heavy metals #Proteasome #Stress #Heat shock proteins |
Tipo |
Journal Article |