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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-1-23
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pubmed:abstractText |
1. The high efficacy of ACE inhibitors to potentiate the actions of kinins might be explained by a hypothetical compartment in which B(2)-receptors are colocalized with kinin degrading enzymes. To demonstrate the functional consequence of such a compartment we compared the myocardial uptake and the persistence of action of bradykinin under the influence of kininase inhibitors. 2. Bradykinin-induced vasodilation and uptake of tritiated bradykinin were studied in perfused rat hearts during inhibition of ACE and aminopeptidase P. B(2)-receptors were localized by immuno-gold labelling and electron-microscopy. 3. The EC(50) of bradykinin-induced vasodilation (5.1+/-0.8 nM) was shifted to 14 fold lower concentrations during inhibition of both kininases. The maximum persistence of vasodilation after termination of bradykinin application (half-life 112+/-20 s) was increased by kininase inhibitors to 398+/-130 s. This prolongation was reversed when B(2)-receptors were blocked simultaneously with the termination of bradykinin infusion. 4. Tritiated bradykinin (perfused for 1 min) was partially (1.7+/-0.24%) retained by the myocardium and consecutively released with a half-life of 70+/-9 s. Kinin uptake was increased during kininase inhibition (7.7+/-2.6%), and was normalized by HOE 140 (2.0+/-0.34%), or when a tritiated B(2)-receptor antagonist (NPC 17731) was used as label. 5. B(2)-receptors were localized in plasmalemmal and cytosolic vesicles of capillary endothelium. 6. Bradykinin is locally incorporated and can associate with B(2)-receptors repeatedly when kinin breakdown is inhibited. This is the kinetic and functional consequence of a colocalization of kininases and B(2)-receptors in a compartment constituted by endothelial membrane vesicles.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-10209009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-10514427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-10642271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-10748135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-10856284,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12540521-9727019
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0007-1188
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
138
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
310-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12540521-Aminopeptidases,
pubmed-meshheading:12540521-Animals,
pubmed-meshheading:12540521-Bradykinin,
pubmed-meshheading:12540521-Enzyme Inhibitors,
pubmed-meshheading:12540521-Male,
pubmed-meshheading:12540521-Myocardium,
pubmed-meshheading:12540521-Peptidyl-Dipeptidase A,
pubmed-meshheading:12540521-Rats,
pubmed-meshheading:12540521-Rats, Wistar,
pubmed-meshheading:12540521-Receptor, Bradykinin B2,
pubmed-meshheading:12540521-Receptors, Bradykinin
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pubmed:year |
2003
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pubmed:articleTitle |
Inhibition of kinin breakdown prolongs retention and action of bradykinin in a myocardial B2 receptor compartment.
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pubmed:affiliation |
Institute of experimental and clinical Pharmacology and Toxicology, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany. dendorfe@medinf.mu-luebeck.de
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pubmed:publicationType |
Journal Article
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