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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1 Pt 2
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pubmed:dateCreated |
1993-3-5
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pubmed:abstractText |
The relationship between Ca2+ and intracellular pH (pHi) was studied in the rabbit collecting duct from the inner stripe of the outer medulla (OMCDi). When bath Ca2+ was lowered [1 mM Ca2+ plus 2 mM ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA)] intracellular Ca2+ concentration ([Ca2+]i) decreased by 38.3 +/- 6.2% from 265 +/- 25 to 165 +/- 25 nm (n = 4). Lowering bath Ca2+ produced a biphasic response in pHi, transient acidification (from 6.93 +/- 0.06 to 6.80 +/- 0.06) followed by a return of pHi to levels slightly higher than control (pHi = 6.97 +/- 0.06). The acidification was not blocked by bath amiloride or 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) or lumen N-ethylmaleimide (NEM). However, bath amiloride significantly reduced the initial rate of pHi recovery after acidification (0.70 pH U/min in control vs. 0.39 pH U/min with amiloride). Lanthanum, a Ca2+ pump inhibitor, completely inhibited the acidification. Moreover, lowering bath temperature to 20 degrees C also inhibited the acidification. Acidification was blocked when the bath pH was raised to 8.0, whereas lowering bath Ca2+ markedly acidified cells when bath pH was lowered to 6.0 (delta pHi = 0.28 +/- 0.01). We also measured the transepithelial (Vt) and basolateral (Vbl) membrane voltages. Lowering bath Ca2+ depolarized Vt and Vbl by 12.7 +/- 4.9 and 6.0 +/- 2.0 mV, respectively. In summary, 1) lowering bath Ca2+ caused a biphasic response in pHi of OMCDi cells, and 2) the acidification phase is due to H+ influx associated with the Ca2+ pump.
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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/Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Lanthanum,
http://linkedlifedata.com/resource/pubmed/chemical/calcium-hydrogen antiporters
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
F88-93
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8381606-Animals,
pubmed-meshheading:8381606-Antiporters,
pubmed-meshheading:8381606-Calcium,
pubmed-meshheading:8381606-Calcium-Binding Proteins,
pubmed-meshheading:8381606-Calcium-Transporting ATPases,
pubmed-meshheading:8381606-Cation Transport Proteins,
pubmed-meshheading:8381606-Egtazic Acid,
pubmed-meshheading:8381606-Electrophysiology,
pubmed-meshheading:8381606-Female,
pubmed-meshheading:8381606-Hydrogen-Ion Concentration,
pubmed-meshheading:8381606-Intracellular Membranes,
pubmed-meshheading:8381606-Kidney Medulla,
pubmed-meshheading:8381606-Kidney Tubules, Collecting,
pubmed-meshheading:8381606-Lanthanum,
pubmed-meshheading:8381606-Rabbits,
pubmed-meshheading:8381606-Temperature
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pubmed:year |
1993
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pubmed:articleTitle |
Evidence for basolateral membrane Ca2+/H+ exchange in outer medullary collecting duct.
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pubmed:affiliation |
Department of Medicine, Vanderbilt University, Nashville, Tennessee.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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