Source:http://linkedlifedata.com/resource/pubmed/id/10511382
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1999-10-28
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| pubmed:abstractText |
Several members of the H+,K+-ATPase family of ion pumps participate in renal K transport. This class of P-type ATPases includes the gastric H+,K+-ATPase as well as a number of nongastric H+,K+-ATPase isoforms. Physiological studies suggest that these enzymes operate predominantly at the apical surfaces of tubule epithelial cells. Although much has been learned about the pattern of H+,K+-ATPase isoform expression and its response to stress, the functional and cell biologic attributes of these pumps remain largely unelucidated. We have studied the properties of renal H+,K+-ATPases both in vitro and in situ. Our analysis of ion fluxes driven by a nongastric H+,K+-ATPase isoform suggests that it exchanges Na (rather than H) for K under normal circumstances. Thus, the individual H+,K+-ATPase isoforms may make diverse contributions to renal cation transport. We find that the activities of renal H+,K+-ATPases in situ are regulated by endocytosis, which is mediated by an endocytosis signal in the cytoplasmic tail of the gastric H+,K+-ATPase beta-subunit. Transgenic mice expressing a version of this protein in which the signal has been disabled show constitutively active renal K resorption. The identities of the H+,K+-ATPase isoforms that are normally subject to endocytic regulation and the nature of the participating epithelial cell machinery have yet to be established.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0270-9295
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
19
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
421-30
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10511382-Animals,
pubmed-meshheading:10511382-Cells, Cultured,
pubmed-meshheading:10511382-H(+)-K(+)-Exchanging ATPase,
pubmed-meshheading:10511382-Humans,
pubmed-meshheading:10511382-Ion Transport,
pubmed-meshheading:10511382-Kidney Tubules, Collecting,
pubmed-meshheading:10511382-Mice,
pubmed-meshheading:10511382-Mice, Transgenic,
pubmed-meshheading:10511382-Stomach,
pubmed-meshheading:10511382-Urothelium,
pubmed-meshheading:10511382-Water-Electrolyte Balance
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| pubmed:year |
1999
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| pubmed:articleTitle |
Nongastric H+,K+-ATPase: cell biologic and functional properties.
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| pubmed:affiliation |
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
|