Linked Life Data

8853415

Source:http://linkedlifedata.com/resource/pubmed/id/8853415

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3 Pt 2
pubmed:dateCreated
1996-12-5
pubmed:abstractText
The human ATP1AL1 gene encodes a protein expressed in brain, kidney, and skin and that is highly homologous to the recently cloned nongastric isoforms of H-K-adenosinetriphosphatase H-K-ATPase). We have generated polyclonal antibodies against the protein encoded by ATP1AL1 and used them to monitor the protein's expression and distribution in transfection studies. The protein was retained in the endplasmic reticulum when it was transiently expressed alone in COS cells. In COS cells cotransfected with ATP1AL1 plus gastric H-K-ATPase beta-subunit cDNAs (ATP1AL1-gH-K beta), both proteins reached the surface. Stably transfected lines of HEK 293 cells expressing both of these proteins demonstrate a 86Rb+ uptake activity sensitive to both 2-methyl,8-(phenylmeoxy)imidazo(1,2-a)pyridine 3-acetonitrile (SCH-28080) and ouabain (inhibitory constants of approximately 131 and 42 microM, respectively). Outward proton fluxes were measured in the same cells as the spontaneous intracellular pH (pHi) recovery in Cells loaded with a pH-sensitive dye [2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein] and subjected to acid loading through an NH4Cl pulse. The cells expressing both the ATP1AL1-encoded protein and the gastric H-K-ATPase beta-subunit possess a net acid extrusion activity that can be inhibited by 1 mM ouabain. Comparison of the 86Rb+ influx and proton efflux, however, does not support equal H+/Rb+ exchange mediated by this pump under the conditions of pHi-monitoring experiments. Moreover, whereas the acid extrusion activity mediated by the pump shows a marked pH dependence, the 86Rb+ uptake activity present in the cells expressing the ATP1AL1-gH-K beta complex cannot be stimulated by acute lowering of pHi. These data suggest that the ATP1AL1-encoded protein is the catalytic alpha-subunit of a human K(+)-dependent ATPase. The possible implications of the discrepancy between 86Rb+ uptake and pHi monitoring data are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
F539-51
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8853415-Acids, pubmed-meshheading:8853415-Adenosine Triphosphatases, pubmed-meshheading:8853415-Animals, pubmed-meshheading:8853415-Antibodies, pubmed-meshheading:8853415-Antibody Specificity, pubmed-meshheading:8853415-COS Cells, pubmed-meshheading:8853415-Cation Transport Proteins, pubmed-meshheading:8853415-Cell Line, pubmed-meshheading:8853415-Chemical Phenomena, pubmed-meshheading:8853415-Chemistry, pubmed-meshheading:8853415-DNA, Complementary, pubmed-meshheading:8853415-Fibroblasts, pubmed-meshheading:8853415-H(+)-K(+)-Exchanging ATPase, pubmed-meshheading:8853415-Humans, pubmed-meshheading:8853415-Immunologic Techniques, pubmed-meshheading:8853415-Isoenzymes, pubmed-meshheading:8853415-Mathematics, pubmed-meshheading:8853415-Rats, pubmed-meshheading:8853415-Rubidium, pubmed-meshheading:8853415-Stomach
pubmed:year
1996
pubmed:articleTitle
Functional expression of the cDNA encoded by the human ATP1AL1 gene.
pubmed:affiliation
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't