Nephrology Dialysis Transplantation, Vol 14, Issue 6 1385-1390, Copyright © 1999 by Oxford University Press
A Komatsuda, H Wakui, Y Oyama, H Imai, A Miura, H Itoh and Y Tashima
Background: Recent studies have shown that the 72-kDa
heat shock protein (HSP72) can be induced in renal tubular cells by a
variety of stress conditions, and suggested its cytoprotective function. We
have tested this hypothesis directly by transfection studies.
Methods: LLC-PK1 cells (porcine renal tubular
epithelial cells) were stably transfected with pKB-CMV or pBK-CMV
containing the human HSP72 gene (pBK-CMV-HSP72). These cells were then
treated with various concentrations of hydrogen peroxide or cisplatin. The
cell viability and lytic cell damage were determined by the MTT
(3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide) assay and
lactate dehydrogenase release assay. Results:
Immunoblot and immunocytochemical analyses showed the high level expression
of HSP72 in LLC-PK1 cells transfected with pBK-CMV-HSP72. In addition, the
expression of other major HSPs (HSP90, HSP73, HSP60 and HSP27) was not
affected by transfection. LLC-PK1 cells overexpressing HSP72 were
significantly more resistant to hydrogen peroxide and cisplatin treatments
than control cells. Conclusion: These results indicate
that overexpressed HSP72 plays a direct role in protecting renal tubular
cells against oxidative injury and cisplatin toxicity. Key
words: HSP72; hydrogen peroxide; LLC-PK1 cells; molecular
chaperone; nephrotoxicity; transfection
ORIGINAL ARTICLES
Overexpression of the human 72 kDa heat shock protein in renal tubular cells confers resistance against oxidative injury and cisplatin toxicity
Third Department of Internal Medicine and Second Department of Biochemistry, Akita University School of Medicine, 1-1-1 Hondo, Akita-shi, Akita 010-8543, Japan; Corresponding author
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