Linked Life Data

7744759

Source:http://linkedlifedata.com/resource/pubmed/id/7744759

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1995-6-15
pubmed:abstractText
The kinetic properties of sulfate transport mediated by the anion exchangers AE1 and AE2 have been examined. Microsomes isolated from HEK cells transiently overexpressing either protein were reconstituted in unilamellar, 200-600-nm diameter proteoliposomes. Transport mediated by the exchangers was monitored by loading the reconstituted proteoliposomes with the slowly transportable anion SO4(2-) using [35S]SO4(2-) as a tracer and performing [35S]SO4(2-)/SO4(2-) exchange. The following data suggest that AE1 and AE2 have been functionally reconstituted: (i) the rate of SO4(2-) transport in AE1 and AE2 containing proteoliposomes was 10-20 times higher than in proteoliposomes derived from control microsomes; (ii) the transport of SO4(2-) was strongly dependent on the presence of a trans anion; and (iii) the anion exchanger inhibitors, 4,4'-diisothiocyanostilbene-2,2'-disulfonate (DIDS) and 4,4'-dinitrostilbene-2,2'-di-sulfonate (DIDS) totally abolished SO4(2-) transport. furthermore, DIDS inhibits SO4(2-) transport only when occluded inside the vesicles, indicating a uniform, asymmetrical, inside-out orientation of the reconstituted exchangers. The Ki values of the stilbene disulfonate compound DNDS were 2.5 and 4 microM for AE1 and AE2, respectively, suggesting that the two exchangers possess similar high affinity sites for stilbene compounds. Both AE1 and AE2 showed the same steep pH dependence of sulfate transport, which was maximal at pH 5.5 and reduced to less than 10% (of the value at pH 5.5) at pH 8.5, suggesting that an acidic residue shared by AE1 and AE2 participates in the pH regulation of sulfate transport.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11251-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7744759-4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid, pubmed-meshheading:7744759-Animals, pubmed-meshheading:7744759-Antiporters, pubmed-meshheading:7744759-Binding Sites, pubmed-meshheading:7744759-Cell Line, pubmed-meshheading:7744759-Humans, pubmed-meshheading:7744759-Hydrogen-Ion Concentration, pubmed-meshheading:7744759-Kidney, pubmed-meshheading:7744759-Kinetics, pubmed-meshheading:7744759-Liposomes, pubmed-meshheading:7744759-Mice, pubmed-meshheading:7744759-Microscopy, Electron, pubmed-meshheading:7744759-Microsomes, pubmed-meshheading:7744759-Proteolipids, pubmed-meshheading:7744759-Radioisotope Dilution Technique, pubmed-meshheading:7744759-Recombinant Proteins, pubmed-meshheading:7744759-Stilbenes, pubmed-meshheading:7744759-Sulfates, pubmed-meshheading:7744759-Sulfur Radioisotopes, pubmed-meshheading:7744759-Transfection
pubmed:year
1995
pubmed:articleTitle
Sulfate transport mediated by the mammalian anion exchangers in reconstituted proteoliposomes.
pubmed:affiliation
Department of Biological Sciences, Stanford University, California 94305-5020, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't