pubmed-article:8415663 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C1522642 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0002502 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C1420234 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C1621574 | lld:lifeskim |
pubmed-article:8415663 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
pubmed-article:8415663 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:8415663 | pubmed:dateCreated | 1993-11-10 | lld:pubmed |
pubmed-article:8415663 | pubmed:abstractText | We previously cloned an isoform Na+/H+ exchanger (NHE3), which was expressed only in intestine, kidney, and stomach. We show here the functional characteristics of NHE3 as a Na+/H+ exchanger by stably transfecting NHE3 cDNA into PS120 cells, a fibroblast cell line that lacks endogenous Na+/H+ exchangers. NHE3 was 39- and 160-fold more resistant to inhibition by amiloride and ethylisopropyl amiloride, respectively, than NHE1, the housekeeping Na+/H+ exchanger isoform. Although both exchangers were stimulated by serum, NHE3 was inhibited by phorbol 12-myristate 13-acetate (PMA), which stimulated NHE1. Mechanistically, serum and PMA stimulated NHE1 by an increase in the apparent affinity of the exchanger for intracellular H+. In contrast, serum stimulated and PMA inhibited NHE3 by a Vmax change. When NHE3 was stably expressed in Caco-2 cells, an intestinal epithelial cell line, NHE3 was functionally expressed in the apical membrane. Thus, NHE3 is a good candidate to be an epithelial brush border Na+/H+ exchanger. Furthermore, Na+/H+ exchangers can be rapidly regulated by mechanisms that change either the Vmax or the affinity for intracellular H+, depending on the Na+/H+ exchanger subtype. | lld:pubmed |
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pubmed-article:8415663 | pubmed:language | eng | lld:pubmed |
pubmed-article:8415663 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8415663 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8415663 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8415663 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8415663 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:DonowitzMM | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:PouyssegurJJ | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:LevineS ASA | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:MontroseM HMH | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:YukC SCS | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:TseC MCM | lld:pubmed |
pubmed-article:8415663 | pubmed:author | pubmed-author:BrantS RSR | lld:pubmed |
pubmed-article:8415663 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8415663 | pubmed:day | 1 | lld:pubmed |
pubmed-article:8415663 | pubmed:volume | 90 | lld:pubmed |
pubmed-article:8415663 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8415663 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8415663 | pubmed:pagination | 9110-4 | lld:pubmed |
pubmed-article:8415663 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8415663 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8415663 | pubmed:articleTitle | Functional characteristics of a cloned epithelial Na+/H+ exchanger (NHE3): resistance to amiloride and inhibition by protein kinase C. | lld:pubmed |
pubmed-article:8415663 | pubmed:affiliation | Department of Medicine, Johns Hopkins University, School of Medicine, Baltimore, MD 21205. | lld:pubmed |
pubmed-article:8415663 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8415663 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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