|
|
 Previous Article | Table of Contents | Next Article 
A murine monoclonal antibody that blocks fibrinogen binding to normal
platelets also inhibits fibrinogen interactions with chymotrypsin- treated
platelets
EI Peerschke and BS Coller
We recently described a monoclonal antibody, 10E5 , that completely blocks
adenosine diphosphate (ADP) induced fibrinogen binding to platelets and
aggregation induced by ADP, epinephrine, and thrombin. Multiple lines of
evidence indicate that 10E5 binds to platelet membrane glycoproteins IIb
and/or IIIa. Because it has been reported that platelets treated with
chymotrypsin aggregate when fibrinogen is added, we tested the effect of
10E5 antibody on chymotrypsin-induced fibrinogen binding and platelet
aggregation. Aspirin-treated human platelets were washed in modified
Tyrode's buffer (pH 7.5), incubated for 5 minutes at 22 degrees C with 300
micrograms/mL chymotrypsin, and washed again. The amount of 10E5 antibody
bound to these platelets (37,232 +/- 2,928 molecules/platelet; mean +/-
SEM, N=9) was similar to that bound to unstimulated control platelets
(36,910 +/- 2,669) and did not differ significantly from the amount of
antibody bound to ADP- treated platelets (P less than .01, N = 5). The
amount of 10E5 bound to chymotrypsin-treated platelets correlated directly
with the amount of fibrinogen bound to separate aliquots of the same
platelet samples (r = .876, P less than .001). The 10E5 antibody caused
virtually complete inhibition of both the binding of fibrinogen to
chymotrypsin-treated platelets and the aggregation induced by exogenous
fibrinogen. Immunoprecipitation studies of 125I-labeled
chymotrypsin-treated platelets revealed that the 10E5 antibody bound
proteins with molecular weights characteristic of glycoproteins IIb and
IIIa. These data suggest that the fibrinogen receptor on
chymotrypsin-treated platelets is identical to that on ADP-treated
platelets and that this receptor is either near to, or on, the glycoprotein
IIb/IIIa complex.
Volume 64,
Issue 1,
pp. 59-63,
07/01/1984
Copyright © 1984 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:
|
|
|
|
 
M. Jirouskova, J. K. Jaiswal, and B. S. Coller
Ligand density dramatically affects integrin {alpha}IIb{beta}3-mediated platelet signaling and spreading
Blood,
June 15, 2007;
109(12):
5260 - 5269.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Si-Tahar, D. Pidard, V. Balloy, M. Moniatte, N. Kieffer, A. Van Dorsselaer, and M. Chignard
Human Neutrophil Elastase Proteolytically Activates the Platelet Integrin alpha IIbbeta 3 through Cleavage of the Carboxyl Terminus of the alpha IIb Subunit Heavy Chain. INVOLVEMENT IN THE POTENTIATION OF PLATELET AGGREGATION
J. Biol. Chem.,
April 25, 1997;
272(17):
11636 - 11647.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M.H. Ginsberg, T.E. O'Toole, J.C. Loftus, and E.F. Plow
Ligand Binding to Integrins: Dynamic Regulation and Common Mechanisms
Cold Spring Harb Symp Quant Biol,
January 1, 1992;
57(0):
221 - 231.
[Abstract]
[PDF]
|
|
|
|
|
