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High-molecular-weight kininogen is exclusively membrane bound on
endothelial cells to influence activation of vascular endothelium
AA Hasan, DB Cines, JR Ngaiza, EA Jaffe and AH Schmaier
Department of Internal Medicine, University of Michigan, Ann Arbor
48109-0724, USA.
An important biologic function of high-molecular-weight kininogen (HK) is
to deliver bradykinin (BK) to its cellular receptors. Internalization and
degradation of HK may provide a mechanism by which endothelial cells
modulate the production of BK and control its activities. Therefore, we
investigated the binding and subsequent distribution of biotinylated-HK
(biotin-HK) associated with human umbilical vein endothelial cells (HUVEC).
HUVEC bound 3 to 4 times more HK and with greater avidity at 1 to 3 hours
at 37 degrees C than at 4 degrees C (Bmax = 1.0 +/- 0.02 x 10(7)
molecules/cell, kd = 7 +/- 3 nmol/L v Bmax = 2.6 +/- 0.2 x 10(6)
molecules/cell, kd = 46 +/- 8 nmol/L). However, there was no evidence that
the difference was caused by internalization of HK at the higher
temperature. First, the same amount of biotin-HK was associated with
nonpermeabilized and permeabilized HUVEC using buffers containing 20 to 50
mumol/L zinc ion in the absence or presence of 2 mmol/L calcium ion.
Second, binding of biotin-HK to HUVEC was approximately 92% reversible at 1
hour when the cells were maintained at both 37 degrees C and 4 degrees C.
Third, neither chloroquine nor primaquine altered the amount of biotin-HK
bound to HUVEC. Fourth, biotin-HK bound to HUVEC was almost completely
removed by pronase. Fifth, the nonpermeable dye, crystal violet, almost
completely quenched the fluorescence signal emitted by HUVEC-associated
fluorescein isothiocyanate (FITC) HK. Finally, the localization of
HUVEC-bound FITC-HK was restricted to the membrane as shown by laser
scanning confocal microscopy. The expression of HK binding sites had an
absolute requirement for metabolic energy, but was not dependent on new
protein synthesis. Membrane-bound HK contributed to the anticoagulant
nature of endothelial cells by blocking human alpha-thrombin binding and
its resultant induction of prostacyclin formation. These studies indicate
that HK is not internalized by HUVEC, but remains primarily on cell
surfaces to be accessible for BK liberation and to modulate the binding and
actions of alpha-thrombin.
Volume 85,
Issue 11,
pp. 3134-3143,
06/01/1995
Copyright © 1995 by The American Society of Hematology
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