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1
* Hematology-Oncology Division and
Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA;
Department of Physiology, Center for Vascular Biology, University of Connecticut School of Medicine, Farmington, Connecticut, USA;
§ New York Medical College, Valhalla, New York, USA;
¶ D.E. Shaw & Co., Inc., New York, New York and Attenuon L.L.C, San Diego, California, USA;
Department of Chemotherapeutics, Pharmaceutical Product Division, Abbott Laboratories, Abbott Park, Illinois, USA; and
Center for Neurovirology and Neurooncology, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania, USA
1Correspondence: Hematology-Oncology Division, BRB 3, Case Western Reserve University, School of Medicine, 10900 Euclid Ave., Cleveland, OH 44106-4937, USA. E-mail: kxm71{at}po.cwru.edu
We previously reported that the binding of two-chain high molecular
weight kininogen (HKa) to endothelial cells may occur through
interactions with endothelial urokinase receptors. Since the binding of
urokinase to urokinase receptors activates signaling responses and may
stimulate mitogenesis, we assessed the effect of HKa binding on
endothelial cell proliferation. Unexpectedly, HKa inhibited
proliferation in response to several growth factors, with 50%
inhibition caused by 
10 nM HKa. This activity was Zn2+
dependent and not shared by either single-chain high molecular weight
kininogen (HK) or low molecular weight kininogen. HKa selectively
inhibited the proliferation of human umbilical vein and dermal
microvascular endothelial cells, but did not affect that of umbilical
vein or human aortic smooth muscle cells, trophoblasts,
fibroblasts, or carcinoma cells. Inhibition of endothelial
proliferation by HKa was associated with endothelial cell apoptosis and
unaffected by antibodies that block the binding of HK or HKa to any of
their known endothelial receptors. Recombinant HK domain 5 displayed
activity similar to that of HKa. In vivo, HKa inhibited
neovascularization of subcutaneously implanted Matrigel plugs, as well
as rat corneal angiogenesis. These results demonstrate that HKa is a
novel inhibitor of angiogenesis, whose activity is dependent on the
unique conformation of the two-chain molecule.—Zhang, J.-C., Claffey,
K., Sakthivel, R., Darzynkiewicz, Z., Shaw, D. E., Leal, J., Wang,
Y.-C., Lu, F. M., McCrae, K. R. Two-chain high molecular
weight kininogen induces endothelial cell apoptosis and inhibits
angiogenesis: partial activity within domain 5.
Key Words: angiogenesis • coagulation • neovascularization • tumor • endothelium
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