Faculty Collaboration Database

Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress. J Clin Invest 1993 Jul;92(1):503-8

Date

07/01/1993

Pubmed ID

8326014

Pubmed Central ID

PMC293638

DOI

10.1172/JCI116594

Scopus ID

2-s2.0-0027203476   150 Citations

Abstract

Expression of heat shock protein 70 (hsp70) is stimulated during ischemia, but its proposed cytoprotective function during metabolic stress has remained conjectural. We introduced a human hsp70 gene into mouse 10T1/2 cells and assessed the susceptibility of these cells to injury in response to conditions that mimic ischemia. Transiently transfected cells, in the absence of stress, expressed human hsp70 to levels equal to or greater than those induced by heat shock, as assessed by RNAse protection, immunoblot, and immunohistochemical analyses. By comparison to cells transfected with a control plasmid, cells expressing the human hsp70 transgene were resistant to injury induced by glucose deprivation and inhibition of mitochondrial respiration. These results provide direct evidence for a cytoprotective function of hsp70 during metabolic stress.

Author List

Williams RS, Thomas JA, Fina M, German Z, Benjamin IJ

Author

Ivor J. Benjamin MD Center Director, Professor in the Medicine department at Medical College of Wisconsin

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

Animals
Cell Line
Gene Expression
Glucose
Heat-Shock Proteins
Hot Temperature
Humans
Mice
RNA, Messenger
Stress, Physiological
Transfection