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Am J Physiol Heart Circ Physiol 280: H1821-H1829, 2001;
0363-6135/01 $5.00
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Vol. 280, Issue 4, H1821-H1829, April 2001

Assembly and activation of HK-PK complex on endothelial cells results in bradykinin liberation and NO formation

Yongqiang Zhao1,*, Qianyao Qiu1,*, Fakhri Mahdi1,*, Zia Shariat-Madar1, Rasmus Røjkjær1, and Alvin H. Schmaier1,2

1 Division of Hematology and Oncology, Department of Internal Medicine and 2 Pathology, University of Michigan, Ann Arbor, Michigan 48109-5669

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 Zn2+. We examined the Zn2+ requirement for HK binding to and the consequences of PK activation on endothelial cells. Optimal HK binding (14 pmol/106 HUVEC) is seen with no added Zn2+ in HEPES-Tyrode buffer containing gelatin versus 16-32 µM added Zn2+ 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 × 107 sites/cell (means ± SD). PK is activated to kallikrein by an antipain-sensitive mechanism in the presence of HK and Zn2+ 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/106 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.

kininogen; prekallikrein; kallikrein; nitric oxide; zinc

* Y. Zhao, Q. Qiu, and F.Mahdi contributed equally to this work.




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