Linked Life Data

11247797

Source:http://linkedlifedata.com/resource/pubmed/id/11247797

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pubmed-article:11247797pubmed:abstractTextPrekallikrein (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.lld:pubmed
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pubmed-article:11247797pubmed:year2001lld:pubmed
pubmed-article:11247797pubmed:articleTitleAssembly and activation of HK-PK complex on endothelial cells results in bradykinin liberation and NO formation.lld:pubmed
pubmed-article:11247797pubmed:affiliationDivision of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-5669, USA.lld:pubmed
pubmed-article:11247797pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11247797pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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