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Ezrin-calpain I interactions in gastric parietal cells

Ezrin-calpain I interactions in gastric parietal cells I interactions YAO, ALAIN of Molecular in gastric parietal AND JOHN University cells California THIBODEAU, and Cell Biology, G. FORTE of California, Berkeley, Yao, Xuebiao, Alain Thibodeau, and John G. Forte. I interactions in gastric parietal cells. Am. J. PhysioL. 265 (Cell Physiol. 34): C36-C46, 1993.-Gastric ezrin, a membrane-cytoskeletal linker with sequence homology to talin and erythrocyte band 4.1, has been associated with the remodeling of parietal cell apical membrane that occurs with adenosine 3’,5’-cyclic monophosphate (CAMP)-dependent protein kinase stimulation. Here we examine the interrelationship between parietal cell ezrin and Ca2+-dependent protease activity. Addition of Ca 2+ to sonicated gastric gland preparations rendered a relatively selective proteolysis of the BO-kDa ezrin, accompanied by the appearance of a 55kDa breakdown product. Ca2+-dependent proteolysis of ezrin was blocked by E64, a cysteine protease inhibitor, or calpastatin, indicating calpain as the responsible protease. Degradation of ezrin in intact gastric glands was achieved by varying extracellular [ Ca2+] and [ionomycin]. Ezrin degradation in situ was rapid and relatively selective, although Ca2+ -dependent degradation of some spectrinlike bands was also observed. The effect of activated calpain I on parietal cell function was assessed by probing the secretory response to histamine stimulation using [ http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Ezrin-calpain I interactions in gastric parietal cells

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Publisher
The American Physiological Society
Copyright
Copyright © 1993 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

I interactions YAO, ALAIN of Molecular in gastric parietal AND JOHN University cells California THIBODEAU, and Cell Biology, G. FORTE of California, Berkeley, Yao, Xuebiao, Alain Thibodeau, and John G. Forte. I interactions in gastric parietal cells. Am. J. PhysioL. 265 (Cell Physiol. 34): C36-C46, 1993.-Gastric ezrin, a membrane-cytoskeletal linker with sequence homology to talin and erythrocyte band 4.1, has been associated with the remodeling of parietal cell apical membrane that occurs with adenosine 3’,5’-cyclic monophosphate (CAMP)-dependent protein kinase stimulation. Here we examine the interrelationship between parietal cell ezrin and Ca2+-dependent protease activity. Addition of Ca 2+ to sonicated gastric gland preparations rendered a relatively selective proteolysis of the BO-kDa ezrin, accompanied by the appearance of a 55kDa breakdown product. Ca2+-dependent proteolysis of ezrin was blocked by E64, a cysteine protease inhibitor, or calpastatin, indicating calpain as the responsible protease. Degradation of ezrin in intact gastric glands was achieved by varying extracellular [ Ca2+] and [ionomycin]. Ezrin degradation in situ was rapid and relatively selective, although Ca2+ -dependent degradation of some spectrinlike bands was also observed. The effect of activated calpain I on parietal cell function was assessed by probing the secretory response to histamine stimulation using [

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Jul 1, 1993

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