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Calreticulin (CRT) is an ubiquitous, highly conserved,
Ca
Volume 270,
Number 28,
Issue of July 14, pp. 17011-17016, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
IN VITRO AND INVIVO UP-REGULATION
-binding protein of the sarcoplasmic and
endoplasmic reticulum. The precise function(s) of CRT is unknown.
However, based on sequence analyses and observations that it may bind
to steroid receptors and integrins and store Ca
within the cell, it has been postulated to play a
``housekeeping'' role. To determine whether the level of
expression of CRT is affected by stress, we examined the heat shock
response of CRT from a variety of cultured cells, including vascular
endothelial, lung epithelial, and lung fibroblasts. Following exposure
of the cells to 42 °C, CRT mRNA transiently accumulated
2.5-4.2-fold at 1-6 h. Nuclear run-on studies and mRNA
stability experiments confirmed that the predominant mechanism of
augmentation was transcriptional. Chloramphenicol acetyltransferase
assays further indicated that the promoter region, containing a
putative heat shock element between -172 and -158 of the
human CRT gene, is heat shock-sensitive. Finally, we demonstrated the in vivo significance of these findings by exposing rats to
hyperthermia. This resulted in accumulation of CRT mRNA and an
augmentation of CRT protein in lung tissue. We hypothesize that this
stress-induced up-regulation of CRT contributes to the mechanism(s) by
which the vascular endothelium and lung tissue, and possibly other
organ systems, maintain homeostasis when exposed to a variety of
pathophysiological conditions.
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