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Induction and intracellular localization of HSP-72 after renal ischemia. Am J Physiol 1992 Nov;263(5 Pt 2):F769-75

Date

11/01/1992

Pubmed ID

1443167

DOI

10.1152/ajprenal.1992.263.5.F769

Scopus ID

2-s2.0-0026458207   99 Citations

Abstract

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.

Author List

Van Why SK, Hildebrandt F, Ardito T, Mann AS, Siegel NJ, Kashgarian M

Author

Scott K. Van Why MD Professor in the Pediatrics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Blotting, Northern
Blotting, Western
Heat-Shock Proteins
Immunohistochemistry
Intracellular Membranes
Ischemia
Male
Rats
Rats, Sprague-Dawley
Renal Circulation
Tissue Distribution