Induction of heat shock protein 72 protects intestinal epithelial
iec18 cells from oxidant and thermal injury.
Musch, Mark W., Mae J. Ciancio, Kevin Sarge, and Eugene B. Chang.
Department of Medicine, Inflammatory Bowel Disease Center, The
University of Chicago, Chicago, IL 60637, Department of Biochemistry,
Molecular and Cell Biology, Northwestern University, Evanston, IL
60015
APStracts 2:0296C, 1995.
The potential importance of inducible heat shock proteins in
conferring protection to intestinal epithelial cells was investigated
using IEC 18 cells. To establish optimal hsp induction, [35S]
-methionine/cysteine incorporation was assessed. Two [35S]-labeled
proteins of 70 and 90 kDa were preferentially synthesized. Western
and Northern blot analyses confirmed induction of hsp70. This
induction provided significant protection to the cells treated with
the oxidant monochloramine or lethal heat (49 C). To better establish
the protective role of hsp70, cells were stably transfected with
human hsp70 under control of the lac operator. When these cells were
subjected to injury, they were protected by IPTG-stimulated hsp70
induction under non-stress conditions. Additionally, the rate of
protein synthesis (assessed by [3H]-leucine incorporation) was
protected. These results demonstrate that hsps are preferentially and
rapidly induced in IEC18 cells and that induction of inducible hsp70
is important in promoting protection against cellular injury.
Received 22 June 1995; accepted in final form 2 August 1995.
APS Manuscript Number C366-5.
Article publication pending Am. J. Physiol. (Cell Physiology).
ISSN 1080-4757 Copyright 1995 The American Physiological Society.
Published in APStracts on 14 August 1995.