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Regulation of human heme oxygenase-1 gene expression under thermal stress
S Okinaga, K Takahashi, K Takeda, M Yoshizawa, H Fujita, H Sasaki and S Shibahara
Department of Applied Physiology and Molecular Biology, Tohoku University
School of Medicine, Japan.
Heme oxygenase-1 is an essential enzyme in heme catabolism, and its human
gene promoter contains a putative heat shock element (HHO-HSE). This study
was designed to analyze the regulation of human heme oxygenase-1 gene
expression under thermal stress. The amounts of heme oxygenase-1 protein
were not increased by heat shock (incubation at 42 degrees C) in human
alveolar macrophages and in a human erythroblastic cell line, YN-1-0-A,
whereas heat shock protein 70 (HSP70) was noticeably induced. However, heat
shock factor does bind in vitro to HHO-HSE and the synthetic HHO-HSE by
itself is sufficient to confer the increase in the transient expression of
a reporter gene upon heat shock. The deletion of the sequence, located
downstream from HHO-HSE, resulted in the activation of a reporter gene by
heat shock. These results suggest that HHO-HSE is potentially functional
but is repressed in vivo. Interestingly, heat shock abolished the
remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1-0-A
cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably
induced. Furthermore, transient expression assays showed that heat shock
inhibits the cadmium-mediated activation of the heme oxygenase-1 promoter,
whereas the HSP70 gene promoter was activated upon heat shock. Such
regulation of heme oxygenase-1 under thermal stress may be of physiologic
significance in erythroid cells.
Volume 87,
Issue 12,
pp. 5074-5084,
06/15/1996
Copyright © 1996 by The American Society of Hematology
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