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Induction and intracellular localization of HSP-72 after renal ischemia

American Journal of Physiology - Renal Fluid and Electrolyte Physiology, ISSN: 0363-6127, Vol: 263, Issue: 5 32-5, Page: F769-75
1992
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Article Description

To determine whether heat shock proteins (HSPs) might be active in cellular recovery following transient ischemia, we examined rat kidneys for 70-kDa HSP (HSP-70) mRNA expression, protein elaboration, and intracellular localization after 45 min of renal ischemia and reflow of 15 min, 2, 6, and 24 h. Inducible HSP-70 mRNA is present at 15 min of reperfusion, peaks between 2 and 6 h, and falls by 24 h. Inducible 72-kDa HSP (HSP-72) protein accumulates progressively through 24 h and is found in both soluble and microsomal fractions following ischemia. Within proximal tubules, immunofluorescent localization of HSP-72 is restricted to the apical domain at 15 min, is dispersed through the cytoplasm in a vesicular pattern at 2 and 6 h, and has migrated away from the apical domain at 24 h. A portion of the vesicular HSP-72 is associated with lysosomes; no intranuclear HSP-72 is detected. The course of mRNA induction, protein elaboration, and HSP-72 localization coincides with previously described changes in proximal tubule morphology and polarity following sublethal ischemic injury. HSP-72 may be instrumental in cellular remodeling and restitution of epithelial polarity during recovery from ischemic renal injury. © 1992 the American Physiological Society.

Bibliographic Details

Scott K. Van Why; Friedhelm Hildebrandt; Thomas Ardito; Andrea S. Mann; Norman J. Siegel; Michael Kashgarian

American Physiological Society

Biochemistry, Genetics and Molecular Biology

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