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

Y Zhao1, Q Qiu, F Mahdi

  • 1Division of Hematology and Oncology, Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-5669, USA.

American Journal of Physiology. Heart and Circulatory Physiology
|March 15, 2001
PubMed
Summary
This summary is machine-generated.

Prekallikrein (PK) activation on endothelial cells releases bradykinin, a process influenced by high-molecular-weight kininogen (HK) and zinc. This bradykinin then stimulates nitric oxide formation, modulating endothelial cell functions.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Prekallikrein (PK) activation on endothelial cells is thought to release bradykinin.
  • This activation requires cell-bound high-molecular-weight kininogen (HK) and zinc ions (Zn2+).

Purpose of the Study:

  • To investigate the Zn2+ requirement for HK binding to endothelial cells.
  • To understand the consequences of PK activation on endothelial cells.

Main Methods:

  • Quantified HK binding to HUVEC under varying Zn2+ conditions.
  • Measured bradykinin liberation and nitric oxide formation following PK activation.
  • Utilized various endothelial and smooth muscle cell types.

Main Results:

  • Optimal HK binding occurred without added Zn2+ when gelatin was present.
  • PK activation to kallikrein occurred in the presence of HK and Zn2+ across multiple cell types.
  • Bradykinin was liberated from cell-bound HK and stimulated nitric oxide production via the B2 receptor.

Conclusions:

  • Endothelial cell-associated PK activation, dependent on HK and Zn2+, liberates bradykinin.
  • Liberated bradykinin modulates endothelial cell physiological activities, including nitric oxide synthesis.
  • This pathway highlights a mechanism by which endothelial cells regulate their function.