|
|
 Previous Article | Table of Contents | Next Article 
Heparin binds to human monocytes and modulates their procoagulant
activities and secretory phenotypes. Effects of histidine-rich glycoprotein
L Leung, K Saigo and D Grant
Department of Medicine, Stanford University School of Medicine, CA 94305.
The binding of heparin to human monocytes and the monocytoid cell line U937
was characterized. Heparin binding was rapid, specific, saturable, and
reversible. There was a single class of heparin binding sites, with an
apparent dissociation constant of 0.19 mumol/L and 1.9 x 10(6) sites per
cell. The binding was not dependent on the anticoagulant property of
heparin. Analysis of surface-iodinated cell lysates by heparin affinity
chromatography revealed a major 120 Kd cell surface heparin- binding
protein. Histidine-rich glycoprotein, a potent heparin antagonist found in
human plasma and platelets, decreased the affinity of heparin for cell
binding. Cell surface bound heparin was functionally active and markedly
accelerated the inactivation of thrombin by antithrombin III. Heparin
induced the release of two monocyte secretory proteins of 160 and 17 Kd.
Our study supports the thesis that heparin and related glycosaminoglycans
interact with monocytes and macrophages, as well as endothelial cells and
smooth muscle cells, and play an important and complex role in blood vessel
wall biology.
Volume 73,
Issue 1,
pp. 177-184,
01/01/1989
Copyright © 1989 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
A.-K. Olsson, H. Larsson, J. Dixelius, I. Johansson, C. Lee, C. Oellig, I. Bjork, and L. Claesson-Welsh
A Fragment of Histidine-Rich Glycoprotein Is a Potent Inhibitor of Tumor Vascularization
Cancer Res.,
January 15, 2004;
64(2):
599 - 605.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. A. Gebska, I. Titley, H. F. Paterson, R. M. Morilla, D. C. Davies, A. M. Gruszka-Westwood, V. V. Kakkar, S. Eccles, and M. F. Scully
High-affinity binding sites for heparin generated on leukocytes during apoptosis arise from nuclear structures segregated during cell death
Blood,
March 15, 2002;
99(6):
2221 - 2227.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. A. Kluszynski, C. Kim, and W. P. Faulk
Zinc as a Cofactor for Heparin Neutralization by Histidine-rich Glycoprotein
J. Biol. Chem.,
May 23, 1997;
272(21):
13541 - 13547.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T Schaefer, M Roux, H. Stuhlsatz, R Herken, B Coulomb, T Krieg, and H Smola
Glycosaminoglycans modulate cell-matrix interactions of human fibroblasts and endothelial cells in vitro
J. Cell Sci.,
January 2, 1996;
109(2):
479 - 488.
[Abstract]
[PDF]
|
|
|
|
|
