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Platelet adhesion to laminin: role of Ca2+ and Mg2+ ions, shear rate, and
platelet membrane glycoproteins
G Hindriks, MJ Ijsseldijk, A Sonnenberg, JJ Sixma and PG de Groot
Department of Haematology, University Hospital Utrecht, The Netherlands.
The adhesion of platelets to purified laminin under flow conditions was
investigated. Adhesion to laminin was strongly dependent on the presence of
divalent cations. In the absence of cations platelet adhesion (8% coverage
in 5 minutes) was maximal at a shear rate of 100/s and no adhesion could be
detected at shear rates above 800/s. In the presence of 0.8 mmol/L Mg2+ and
2 mmol/L Ca2+ platelet adhesion reached its maximum (30% coverage) around
800/s. At 1,800/s platelets still adhered to purified laminin (coverage of
6%). Antibodies against the E8 domain of laminin and antibodies against the
alpha 6 and beta 1 chains of platelet membrane glycoprotein very late
activation antigen-6 (VLA-6), completely inhibited adhesion. No inhibition
was found with antibodies against glycoprotein IIb:IIIa, against the alpha
2 chain of VLA-2, and against the alpha 5 chain of VLA-5. Fibronectin and
von Willebrand factor were not involved in laminin-dependent adhesion.
Anti- VLA-6 partly inhibited platelet adhesion to the extracellular matrix
of endothelial cells at shear rates below 800/s. Preincubation of the
matrices with antilaminin E8 antibodies did not influence the adhesion.
These results show that purified laminin supports platelet adhesion and
that the presence of VLA-6 is important for platelet adhesion under flow
conditions. The protein in the matrix with which VLA-6 interacts is
currently unknown.
Volume 79,
Issue 4,
pp. 928-935,
02/15/1992
Copyright © 1992 by The American Society of Hematology
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