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Platelet adhesion to collagen types I through VIII under conditions of
stasis and flow is mediated by GPIa/IIa (alpha 2 beta 1-integrin)
EU Saelman, HK Nieuwenhuis, KM Hese, PG de Groot, HF Heijnen, EH Sage, S Williams, L McKeown, HR Gralnick and JJ Sixma
Department of Haematology, University Hospital Utrecht, The Netherlands.
Platelet adhesion to fibrillar collagens (types I, II, III, and V) and
nonfibrillar collagens (types IV, VI, VII, and VIII) was investigated in
the presence of physiologic concentrations of divalent cations under
conditions of stasis and flow. Under static conditions, platelet adhesion
was observed to collagen types I through VII but not to type VIII. Under
flow conditions, platelet adhesion to collagen types I, II, III, and IV was
almost independent of shear rates above 300/s. Collagen type V was
nonadhesive. Platelet adhesion to collagen type VI was shear rate-dependent
and optimal at a rate of 300/s. Collagen types VII and VIII showed minor
reactivity and supported platelet adhesion only between shear rates 100 to
1,000/s. Monoclonal antibody (MoAb) 176D7, directed against platelet
membrane glycoprotein Ia (GPIa; very late antigen [VLA]-alpha 2 subunit),
completely inhibited platelet adhesion to all collagens tested, under
conditions of both stasis and flow. Platelet adhesion to collagen type III
at shear rate 1,600/s was only inhibited for 85%. The concentration of
antibody required for complete inhibition of platelet adhesion was
dependent on the shear rate and the reactivity of the collagen. An MoAb
directed against GPIIa (VLA-beta subunit) partially inhibited platelet
adhesion to collagen. These results show that GPIa-IIa is a major and
universal platelet receptor for eight unique types of collagen.
Volume 83,
Issue 5,
pp. 1244-1250,
03/01/1994
Copyright © 1994 by The American Society of Hematology
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