rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2001-3-15
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pubmed:abstractText |
Prekallikrein (PK) activation on human umbilical endothelial cells (HUVEC) presumably leads to bradykinin liberation. On HUVEC, PK activation requires the presence of cell-bound high-molecular-weight kininogen (HK) and Zn(2+). We examined the Zn(2+) requirement for HK binding to and the consequences of PK activation on endothelial cells. Optimal HK binding (14 pmol/10(6) HUVEC) is seen with no added Zn(2+) in HEPES-Tyrode buffer containing gelatin versus 16--32 microM added Zn(2+) in the same buffer containing bovine serum albumin. The affinity and number of HK binding sites on HUVEC are a dissociation constant of 9.6 +/- 1.8 nM and a maximal binding of 1.08 +/- 0.26 x 10(7) sites/cell (means +/- SD). PK is activated to kallikrein by an antipain-sensitive mechanism in the presence of HK and Zn(2+) on HUVEC, human microvascular endothelial cells, umbilical artery smooth muscle cells, and bovine pulmonary artery endothelial cells. Simultaneous with kallikrein formation, bradykinin (5.0 or 10.3 pmol/10(6) HUVEC in the absence or presence of lisinopril, respectively) is liberated from cell-bound HK. Liberated bradykinin stimulates the endothelial cell bradykinin B2 receptor to form nitric oxide. Assembly and activation of PK on endothelial cells modulates their physiological activities.
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pubmed:grant |
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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/Antipain,
http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Kallikreins,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogen, High-Molecular-Weight,
http://linkedlifedata.com/resource/pubmed/chemical/Lisinopril,
http://linkedlifedata.com/resource/pubmed/chemical/NG-Nitroarginine Methyl Ester,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Prekallikrein,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/omega-N-Methylarginine
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0363-6135
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
H1821-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11247797-Animals,
pubmed-meshheading:11247797-Antipain,
pubmed-meshheading:11247797-Binding Sites,
pubmed-meshheading:11247797-Biotinylation,
pubmed-meshheading:11247797-Bradykinin,
pubmed-meshheading:11247797-Cattle,
pubmed-meshheading:11247797-Cells, Cultured,
pubmed-meshheading:11247797-Endothelium, Vascular,
pubmed-meshheading:11247797-Enzyme Activation,
pubmed-meshheading:11247797-Humans,
pubmed-meshheading:11247797-Kallikreins,
pubmed-meshheading:11247797-Kinetics,
pubmed-meshheading:11247797-Kininogen, High-Molecular-Weight,
pubmed-meshheading:11247797-Lisinopril,
pubmed-meshheading:11247797-Microcirculation,
pubmed-meshheading:11247797-NG-Nitroarginine Methyl Ester,
pubmed-meshheading:11247797-Nitric Oxide,
pubmed-meshheading:11247797-Prekallikrein,
pubmed-meshheading:11247797-Pulmonary Artery,
pubmed-meshheading:11247797-Receptors, Bradykinin,
pubmed-meshheading:11247797-Serum Albumin, Bovine,
pubmed-meshheading:11247797-Umbilical Arteries,
pubmed-meshheading:11247797-Umbilical Veins,
pubmed-meshheading:11247797-Zinc,
pubmed-meshheading:11247797-omega-N-Methylarginine
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pubmed:year |
2001
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pubmed:articleTitle |
Assembly and activation of HK-PK complex on endothelial cells results in bradykinin liberation and NO formation.
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pubmed:affiliation |
Division of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-5669, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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