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GRP94 is an endoplasmic reticulum (ER) localized glycoprotein
with Ca
Volume 270,
Number 16,
Issue of April 21, pp. 9526-9534, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
binding and protein chaperoning properties.
Using a ribozyme driven by a stress-inducible promoter and targeted
against grp94 mRNA, we have generated a cell line deficient in its
ability to induce GRP94. The effect of the ribozyme is mediated by the
cleavage of the grp94 message just downstream of the initiation codon,
and not by an antisense effect, as determined by the level of intact
grp94 mRNA. Unexpectedly, this cell line's ability to induce
GRP78 is also impaired. Transient overexpression of recombinant human
lysosomal hydrolase
-
L-iduronidase in the ribozyme
expressing cells indicates that the secretion ratio of this enzyme is
reduced by about 6-fold. Additionally, the ribozyme expressing cells
showed increased sensitivity to Cadepletion from ER
caused by either A23187 or thapsigargin, an
ER-Ca
-ATPase inhibitor, but not to tunicamycin. These
combined results show that the induction of GRP94 may play important
roles in ER to nuclear signaling, protein sorting and secretion, and
specific protection against Ca
depletion stress.
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