rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1994-2-22
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pubmed:databankReference |
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pubmed:abstractText |
We have cloned a protein from bovine brain, brain-derived voltage-dependent anion channel 1 (BR1-VDAC), that is identical to a recently sequenced plasmalemmal-bound porin from human lymphocytes. mRNA hybridization indicates that BR1-VDAC is widely distributed throughout nervous and nonnervous tissues. In situ localization substantiated that the BR1-VDAC is associated with the plasmalemma of astrocytes. A monoclonal antibody that recognizes the N terminus of the BR1-VDAC protein completely blocks an astrocytic high-conductance anion channel that has electrophysiological similarities with the mitochondrial VDAC. Since the high-conductance anion channel in astrocytes has been shown to respond to hypoosmotic solutions, its molecular identification provides the basis for a better understanding of volume regulation in brain tissue.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1011248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1281637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1373732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1380503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-14116659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1659831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1707632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1718414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-1724155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2282496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2433415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2441828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2471080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2476912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2559744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2581224,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-2823172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-450112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-6097869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-6311302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7507248-8420959
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
499-503
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:7507248-Animals,
pubmed-meshheading:7507248-Antibodies, Monoclonal,
pubmed-meshheading:7507248-Astrocytes,
pubmed-meshheading:7507248-Base Sequence,
pubmed-meshheading:7507248-Binding, Competitive,
pubmed-meshheading:7507248-Cattle,
pubmed-meshheading:7507248-Cell Membrane,
pubmed-meshheading:7507248-Cells, Cultured,
pubmed-meshheading:7507248-Cloning, Molecular,
pubmed-meshheading:7507248-DNA, Complementary,
pubmed-meshheading:7507248-Humans,
pubmed-meshheading:7507248-Immunohistochemistry,
pubmed-meshheading:7507248-Ion Channels,
pubmed-meshheading:7507248-Membrane Proteins,
pubmed-meshheading:7507248-Molecular Sequence Data,
pubmed-meshheading:7507248-Porins,
pubmed-meshheading:7507248-Rats,
pubmed-meshheading:7507248-Voltage-Dependent Anion Channel 1,
pubmed-meshheading:7507248-Voltage-Dependent Anion Channels
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pubmed:year |
1994
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pubmed:articleTitle |
Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.
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pubmed:affiliation |
Institute of Anatomy, University of Regensburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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