Source:http://linkedlifedata.com/resource/pubmed/id/12195293
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2002-8-26
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pubmed:abstractText |
Ion transporters play a central role in gastric acid secretion. To determine whether some of these transporters are necessary for the normal ultrastructure of secretory membranes in gastric parietal cells, mice lacking transporters for H+, K+, Cl-, and Na+ were examined for alterations in volume density (Vd) of basolateral, apical, tubulovesicular and canalicular membranes, microvillar dimensions, membrane flexibility, and ultrastructure. In mice lacking Na+/H+ exchanger 1 (NHE1) or the Na+-K+-2Cl- cotransporter (NKCC1), the ultrastructure and Vd of secretory membranes and the secretory canalicular to tubulovesicular membrane ratio (SC/TV), a morphological correlate of secretory activity, were similar to those of wild-type mice. In mice lacking Na+/H+ exchanger 2 (NHE2) or gastric H+, K+ -ATPase alpha- or beta-subunits, the SC/TV ratio and Vd of secretory membranes were decreased, though canaliculi were often dilated. In H+, K+ -ATPase-deficient parietal cells, canalicular folds were decreased, normally abundant tubulovesicles were replaced with a few rigid round vesicles, and microvilli were sparse, stiff and short, in contrast to the long and flexible microvilli in wild-type cells. In addition, microvilli of the H+, K+ -ATPase-deficient parietal cells had centrally bundled F-actin filaments, unlike the microvilli of wild-type cells, in which actin filaments were peripherally positioned concentric to the plasmalemma. Data showed that the absence of H+, K+ -ATPase produced fundamental changes in parietal cell membrane ultrastructure, suggesting that the pump provides an essential link between the membranes and F-actin, critical to the gross architecture and suppleness of the secretory membranes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/H( )-K( )-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Slc9a2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter,
http://linkedlifedata.com/resource/pubmed/chemical/growth factor-activatable Na-H...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0302-766X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
369-80
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12195293-Animals,
pubmed-meshheading:12195293-Genotype,
pubmed-meshheading:12195293-H(+)-K(+)-Exchanging ATPase,
pubmed-meshheading:12195293-Intracellular Membranes,
pubmed-meshheading:12195293-Mice,
pubmed-meshheading:12195293-Mice, Knockout,
pubmed-meshheading:12195293-Microscopy, Electron,
pubmed-meshheading:12195293-Microvilli,
pubmed-meshheading:12195293-Parietal Cells, Gastric,
pubmed-meshheading:12195293-Protein Subunits,
pubmed-meshheading:12195293-Secretory Vesicles,
pubmed-meshheading:12195293-Sodium-Hydrogen Antiporter
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pubmed:year |
2002
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pubmed:articleTitle |
The unique ultrastructure of secretory membranes in gastric parietal cells depends upon the presence of H+, K+ -ATPase.
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pubmed:affiliation |
Department of Environmental Health, College of Medicine, University of Cincinnati, Cincinnati, 3223 Eden Avenue, Cincinnati, OH 45267-0056, USA. millermn@email.uc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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