Source:http://linkedlifedata.com/resource/pubmed/id/15010017
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-3-10
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pubmed:databankReference | |
pubmed:abstractText |
The renin-angiotensin system (RAS) has become increasingly complex. New components have been identified, and additional roles for angiotensin peptides and their receptors are being uncovered. A functional (pro)renin receptor has been cloned that acts as (pro)renin cofactor on cell surface, enhancing the efficiency of angiotensinogen cleavage by (pro)renin and unmasking prorenin catalytic activity. Binding of (pro)renin to the receptor mediates (pro)renin cellular effects by activating mitogen-activating protein (MAP) kinases, extracellular signal-regulated kinases (ERK)1/2. Immunofluorescence studies have localized the receptor on mesangial and vascular smooth muscle cells in human heart and kidney. This suggests that the renin receptor might represent a means to capture (pro)renin from the circulation and to concentrate (pro)renin at the interface between smooth muscle and endothelial cells. In this article, we review the biochemical characteristics of this receptor and of other renin-binding proteins, and discuss their physiologic significance.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP6AP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Renin,
http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1522-6417
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-32
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15010017-Amino Acid Sequence,
pubmed-meshheading:15010017-Animals,
pubmed-meshheading:15010017-Glomerular Mesangium,
pubmed-meshheading:15010017-Humans,
pubmed-meshheading:15010017-Mitogen-Activated Protein Kinases,
pubmed-meshheading:15010017-Molecular Sequence Data,
pubmed-meshheading:15010017-Muscle, Smooth, Vascular,
pubmed-meshheading:15010017-Receptors, Cell Surface,
pubmed-meshheading:15010017-Renin,
pubmed-meshheading:15010017-Vacuolar Proton-Translocating ATPases
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pubmed:year |
2004
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pubmed:articleTitle |
Renin/prorenin-receptor biochemistry and functional significance.
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pubmed:affiliation |
INSERM U36, Collège de France, 11, place Marcelin Berthelot, 75005, Paris, France. genevieve.nguyen@college-de-france.fr
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pubmed:publicationType |
Journal Article,
Review
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