|
|
 Previous Article | Table of Contents | Next Article 
Regulation of glycoprotein IIB/IIIA exposure on platelets stimulated with
alpha-thrombin
G van Willigen and JW Akkerman
Department of Hematology, University Hospital Utrecht, The Netherlands.
Previous studies have shown that binding sites for fibrinogen on platelets
stimulated with platelet-activating factor (PAF), adenosine diphosphate or
epinephrine rapidly close in the absence of fibrinogen. In the present
study we investigated whether alpha-thrombin induced similar changes in the
glycoprotein (GP) IIB/IIIA-complex. Whereas 80% of binding sites exposed by
PAF closed within 30 minutes (22 degrees C), alpha-thrombin (0.1 U/mL)
triggered long-lasting exposure of binding sites for [125I]-fibrinogen and
[125I]-fibronectin. Even removal of alpha-thrombin with an excess of
hirudin failed to close the binding sites. Similar to PAF,
alpha-thrombin-exposed sites rapidly closed after addition of the protein
kinase C inhibitor staurosporine (1 mumol/L) or dibutyryl cyclic adenosine
monophosphate (250 mumol/L). In contrast, prostacyclin (PGI2, 10 ng/mL),
which induced rapid closure of binding sites in platelets stimulated with
PAF, failed to close the sites in alpha-thrombin-treated platelets. Removal
of alpha-thrombin from the platelets restored the PGI2-sensitivity. These
data indicate that a short interaction between alpha-thrombin and platelets
triggers long-lasting exposure of GPIIB/IIIA. Furthermore, as long as
alpha- thrombin remains bound to the platelets, agonists that activate the
PGI2-receptor are unable to close GPIIB/IIIA.
Volume 79,
Issue 1,
pp. 82-90,
01/01/1992
Copyright © 1992 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:
|
|
|
|
 
S. Gundewar, J. W. Calvert, J. W. Elrod, and D. J. Lefer
Cytoprotective effects of N,N,N-trimethylsphingosine during ischemia- reperfusion injury are lost in the setting of obesity and diabetes
Am J Physiol Heart Circ Physiol,
October 1, 2007;
293(4):
H2462 - H2471.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. W. Galt, S. Lindemann, L. Allen, D. J. Medd, J. M. Falk, T. M. McIntyre, S. M. Prescott, L. W. Kraiss, G. A. Zimmerman, and A. S. Weyrich
Outside-In Signals Delivered by Matrix Metalloproteinase-1 Regulate Platelet Function
Circ. Res.,
May 31, 2002;
90(10):
1093 - 1099.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
I. Hers, J. Donath, P. E. M. H. Litjens, G. van Willigen, and J.-W. N. Akkerman
Inhibition of Platelet Integrin {alpha}IIb{beta}3 by Peptides That Interfere With Protein Kinases and the {beta}3 Tail
Arterioscler Thromb Vasc Biol,
June 1, 2000;
20(6):
1651 - 1660.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Nakamura, J.-i. Kambayashi, M. Okuma, and N. N. Tandon
Activation of the GP IIb-IIIa Complex Induced by Platelet Adhesion to Collagen Is Mediated by Both {alpha}2{beta}1 Integrin and GP VI
J. Biol. Chem.,
April 23, 1999;
274(17):
11897 - 11903.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Shiraga, Y. Tomiyama, S. Honda, H. Suzuki, S. Kosugi, S. Tadokoro, Y. Kanakura, K. Tanoue, Y. Kurata, and Y. Matsuzawa
Involvement of Na+/Ca2+ Exchanger in Inside-Out Signaling Through the Platelet Integrin alpha IIbbeta 3
Blood,
November 15, 1998;
92(10):
3710 - 3720.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Lassila, K. Lindstedt, and P. T. Kovanen
Native Macromolecular Heparin Proteoglycans Exocytosed From Stimulated Rat Serosal Mast Cells Strongly Inhibit Platelet-Collagen Interactions
Arterioscler Thromb Vasc Biol,
December 1, 1997;
17(12):
3578 - 3587.
[Abstract]
[Full Text]
|
|
|
|
|
