Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress. J Clin Invest 1993 Jul;92(1):503-8
Date
07/01/1993Pubmed ID
8326014Pubmed Central ID
PMC293638DOI
10.1172/JCI116594Scopus ID
2-s2.0-0027203476 (requires institutional sign-in at Scopus site) 154 CitationsAbstract
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 IJAuthor
Ivor J. Benjamin MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsCell Line
Gene Expression
Glucose
Heat-Shock Proteins
Hot Temperature
Humans
Mice
RNA, Messenger
Stress, Physiological
Transfection