Membrane and protein recycling associated with gastric HCl secretion
作者:
J. G. FORTE,
D. K. HANZEL,
C. OKAMOTO,
D. CHOW,
T. URUSHIDANI,
期刊:
Journal of Internal Medicine
(WILEY Available online 1990)
卷期:
Volume 228,
issue S732
页码: 17-26
ISSN:0954-6820
年代: 1990
DOI:10.1111/j.1365-2796.1990.tb01467.x
出版商: Blackwell Publishing Ltd
关键词: ATPase;ezrin;glycoprotein;parietal;phosphoprotein;proton transport
数据来源: WILEY
摘要:
Abstract.Stimulation of the gastric parietal cell requires massive membrane transformations as H+‐pumps from the domain of cytoplasmic tubulovesicles are recruited into the apical plasma membrane domain. The recycling of membrane pools, through fusion and fission processes that accompany stimulation and inhibition of HCl secretion, also involves highly selective events of protein incorporation and segregation. This manuscript describes several proteins that have been identified with the apical plasma membrane from maximally stimulated parietal cells, and broadly characterizes them either as permanent resident proteins of the apical membrane, or transient proteins that move into and out of the apical membrane as the cell progresses through the secretory cycle. A typical example of transient association with the apical membrane concerns the pump proteins, including the 94 kDa catalytic α‐subunit of the H+K+‐ATPase and its newly discovered β‐subunit glycoprotein, which move between tubulovesicles. Proteins that remain associated with the apical plasma membrane during rest and secretion include actin, and an 80‐kDa phosphoprotein, which has been variously called 80 K, ezrin, p81 and cytovillin, and whose phosphorylation is increased by the histamine/cAMP pathway of parietal cell stimulation. An example of a cytosolic protein that becomes associated with the apical plasma membrane after stimulation is a 120‐kDa protein, which appears to have protein kinase activity. Note that the identification, localization and characterization of the K+and Cl−transport proteins, which participate in net HCl secretion, are of immed
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