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Thromb Haemost 1990; 64(01): 069-073
DOI: 10.1055/s-0038-1647255
Original Article
Schattauer GmbH Stuttgart

Dffierent Effects of Human Neutrophil Elastase on Platelet Glycoproteins IIb and IIIa of Resting and Stimulated Platelets[*]

K Bykowska
Laboratory of Blood Coagulation and Haemostasis, Institute of Haematology, Warsaw
,
Z Pawlowska
1   The Department of Biophysics, Medical School, Lodz, Foland
,
C Cierniewski
1   The Department of Biophysics, Medical School, Lodz, Foland
,
S Lopaciuk
Laboratory of Blood Coagulation and Haemostasis, Institute of Haematology, Warsaw
,
M Kopeć
Laboratory of Blood Coagulation and Haemostasis, Institute of Haematology, Warsaw
› Author Affiliations
Further Information

Publication History

Received 04 July 1989

Accepted after revision 29 December 1989

Publication Date:
04 September 2018 (online)

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Summary

The effect of human neutrophil elastase (HNE) on the structure and receptor activity of platelet glycoprotein IIb/IIIa complex was studied. Resting platelets, which bound only traces of 125I-fibrinogen in the absence of ADR were found to be barely susceptible to HNE. As shown by immunoblotting experiments, treatment of such platelets with HNE (14 μg/ml) did not provoke a detectable cleavage of GPIIb but resulted in a partial digestion of GPIIIa and appearance of 110 kDa fragment. Such proteolytic modification of the GPIIb/IIIa complex was accompanied by a slight increase in the binding of fibrinogen to blood platelets in the absence of ADP. Treatment of partially activated platelets (spontaneous activation during washing procedure) with HNE caused a progressive loss of GPIIb and degradation of GPIIIa to 110 kDa and 60 kDa fragments. These spontaneously stimulated platelets had initially a high number of fibrinogen binding sites exposed, corresponding to approximately 50% of receptor capacity observed in platelets activated by the optimal concentration of ADP. Digestion of GPIIb/IIIa by HNE of such platelets markedly increased the exposure of fibrinogen receptors. Thus, the stimulation of platelets increases significantly the susceptibility of the GPIIb/IIIa complex to proteolysis by HNE. However, such modification of the GPIIb/IIIa does not destroy its function as a receptor for fibrinogen either on the resting or activated platelets.

Dedicated to Professor M. Verstraete on the occasion of his 65th birthday.


 

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