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KMID : 0578319950050020176
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Molecules and Cells
1995 Volume.5 No. 2 p.176 ~ p.180
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Induction of the glucose-regulated Proteins by Ca2+-ATPase Inhibitors and Brefeldin A
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Kang, Ho sung
Park, Young Chul/Han, Song Iy/Kim, Byeong Gee/Kim, Chong-Rak/Lee, Kong-Joo/Kim, Han Do
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Abstract
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Glucose-regulated proteins (grp´s) are a group of stress proteins whose syntheses are geatly enhaued when cells are exposed to stressful conditions including glucose stravation and Ca^(2+) ionophore which perturbs intracellular Ca^(2+) Homeostasis. In this study, we examined the ability of endomembrane Ca^(2+)-ATPase inhibitors, thapsigargin, 2,5-di(tert-butyl)-1,4-hydroquinone and cyclopiazonic acid, and brefeldin A, an inhibitor of intracellular protein transport as inducers of grp’s. The treatment of either Ca^(2+)-ATPase inhibitors or brefeldin A markedly increased the syntheses of grp´s, whereas BAPTA-AM, a cell permeant Ca^(2+) chelator, did not induce the grp’s. In addition, grp induclion by Ca^(2+)-ATPase inhibitors was not inhibited by BAPTA-AM preloading which blocked increases in cytosolic Ca^(2+), resulting from Ca^(2+)-ATPase inhibitor treament. Thus, these results indicate that grp expression is closely coupled to the depletion of the intracellular Ca^(2+) store as well as protein trafficking from the endoplasmic reticulum to Golgi.
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