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The Journal of Immunology, Vol 144, Issue 1 221-225, Copyright © 1990 by American Association of Immunologists

ARTICLES

Modulation of platelet responses to collagen by Clq receptors

EI Peerschke and B Ghebrehiwet
Department of Pathology, Suny, Stony Brook 11794.

We recently described specific binding sites for Clq on human blood platelets that cross-react with antibodies against Clq receptors (ClqR) on lymphoblastoid cells. Inasmuch as Clq inhibits collagen-induced platelet aggregation, we compared the effects of ClqR occupancy by purified Clq, monoclonal (IIl/B5) and polyclonal anti-ClqR antibodies on collagen-induced platelet adhesion, release, and aggregation. Washed platelets in buffered Tyrode's solution containing 2 mM magnesium were preincubated (30 min, 22 degrees C) with antibodies, Clq, or appropriate control buffers and antiserum. Platelet aggregation and release measurements were made using 14C-serotonin-labeled platelets stimulated with type I collagen. Adhesion assays were performed in the presence of magnesium under static conditions at 22 degrees C with 51Cr- labeled platelets and collagen-coated microtiter wells. Concentrations of IIl/B5, polyclonal anti-Clq R antiserum, or Clq causing 82 to 92% (n = 7) inhibition of collagen-induced release and 67 to 98% inhibition of aggregation, failed to inhibit magnesium-dependent platelet adhesion to collagen. Inasmuch as divalent cation-independent platelet-collagen interactions have also been described, further studies were performed to compare the divalent cation requirement of ClqR occupancy by Clq and inhibition of platelet-collagen interactions. Whereas, Clq binding to platelets was divalent cation independent, neither Clq nor anti-ClqR antibodies prevented platelet adhesion to collagen in the presence of EDTA. These data suggest that under defined in vitro conditions, ClqR modulate collagen-induced platelet aggregation and secretion, but not platelet adhesion.


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C. A. Ogden, A. deCathelineau, P. R. Hoffmann, D. Bratton, B. Ghebrehiwet, V. A. Fadok, and P. M. Henson
C1q and Mannose Binding Lectin Engagement of Cell Surface Calreticulin and CD91 Initiates Macropinocytosis and Uptake of Apoptotic Cells
J. Exp. Med., September 17, 2001; 194(6): 781 - 796.
[Abstract] [Full Text] [PDF]


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