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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1997-6-5
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pubmed:abstractText |
The functional expression of homo-oligomeric alpha7 neuronal nicotinic and type 3 serotonin receptors is dependent on the activity of a cyclophilin. In this paper we demonstrate that the mechanism of cyclophilin action during functional homo-oligomeric receptor expression in Xenopus oocytes is distinct from the calcineurin-dependent immunosuppressive mechanism by showing that a nonimmunosuppressive analog of cyclosporin A (CsA), SDZ 211-811, reduces functional receptor expression to the same extent as CsA. The cytoplasmic subtype of cyclophilin, cyclophilin A (CyPA), appears to be required for functional receptor expression. This is because overexpression of CyPA and a CyPA mutant that is deficient in CsA binding activity reverses CsA-induced reduction in functional receptor expression. The mechanism of action of CyPA is likely to involve its prolyl isomerase activity because a mutant CyPA with a single amino acid substitution (arginine 55 to alanine) that is predicted to produce a 1000-fold attenuation in isomerase activity fails to reverse the cyclosporin A effect. Our data also suggest that CyPA does not form a stable complex with receptor subunits.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1338979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1357751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1379518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1714445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1715244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1731198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-1985948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2000394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2001362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2059621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2186809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2194066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2357375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2477715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2493138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-2664782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-3048413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-3277061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-3306408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-6395866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7507339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7513288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7514503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7533300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7603990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7693682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7822304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7884893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7913447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7929183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7957056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7969494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-7969495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144255-8317297
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nicotinic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin, 5-HT3,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5432-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9144255-Amino Acid Isomerases,
pubmed-meshheading:9144255-Animals,
pubmed-meshheading:9144255-Brain,
pubmed-meshheading:9144255-Carrier Proteins,
pubmed-meshheading:9144255-Cloning, Molecular,
pubmed-meshheading:9144255-Cyclosporine,
pubmed-meshheading:9144255-Female,
pubmed-meshheading:9144255-Gene Expression,
pubmed-meshheading:9144255-Kidney,
pubmed-meshheading:9144255-Membrane Potentials,
pubmed-meshheading:9144255-Mutagenesis, Site-Directed,
pubmed-meshheading:9144255-Oocytes,
pubmed-meshheading:9144255-PC12 Cells,
pubmed-meshheading:9144255-Peptidylprolyl Isomerase,
pubmed-meshheading:9144255-Polymerase Chain Reaction,
pubmed-meshheading:9144255-Rats,
pubmed-meshheading:9144255-Receptors, Nicotinic,
pubmed-meshheading:9144255-Receptors, Serotonin,
pubmed-meshheading:9144255-Receptors, Serotonin, 5-HT3,
pubmed-meshheading:9144255-Recombinant Fusion Proteins,
pubmed-meshheading:9144255-Xenopus laevis
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pubmed:year |
1997
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pubmed:articleTitle |
Peptidyl prolyl cis-trans isomerase activity of cyclophilin A in functional homo-oligomeric receptor expression.
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pubmed:affiliation |
Division of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA. shelekar@bcm.tmc.edu
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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