Circulation, Vol 87, 2023-2032, Copyright © 1993 by American Heart Association
K Iwaki, SH Chi, WH Dillmann and R Mestril
BACKGROUND. A cultured neonatal rat cardiomyocyte model is used to
investigate the expression of the inducible heat shock protein 70 (HSP70i)
during hypoxia/reoxygenation and metabolic stress. METHODS AND RESULTS. The
major HSP70i is increased in its expression at the mRNA and protein level
in myocytes exposed to hypoxia/reoxygenation and metabolic stress by the
addition of 2-deoxyglucose and sodium cyanide, which are inhibitors known
to block ATP production. Surprisingly, the appearance of HSP70 mRNA
precedes the intracellular ATP depletion caused by hypoxia, which is
contrary to what we observe when the cardiomyocytes are subjected to
metabolic stress. CONCLUSIONS. It has been postulated recently that the
decrease in intracellular ATP content in cells under stress may be the
trigger that leads to the induction of HSP70i by reducing the pool of free
HSP70, thus activating the stress response. Our results indicate that
although this may be the case during metabolic stress, another route of
activation must be used during the early stages of hypoxia in
cardiomyocytes. The induction of HSP70i also appears to precede the onset
of cellular damage as measured by the release of cytoplasmic enzymes and
preincorporated arachidonic acid. This indicates that cardiomyocytes are
able to respond to hypoxia/reoxygenation and metabolic stress with
increased HSP70i production and points to a potential protective role of
heat shock proteins during ischemia/reperfusion injury.
ARTICLES
Induction of HSP70 in cultured rat neonatal cardiomyocytes by hypoxia and metabolic stress
Department of Medicine, University of California, San Diego.
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