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 Blood, 15 January 2006, Vol. 107, No. 2, pp. 423-430.
Prepublished online as a Blood First Edition Paper on September 29, 2005; DOI 10.1182/blood-2005-04-1425.

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PLENARY PAPERS

C1qTNF–related protein-1 (CTRP-1): a vascular wall protein that inhibits collagen-induced platelet aggregation by blocking VWF binding to collagen

Gerald Lasser, Prasenjit Guchhait, Jeff L. Ellsworth, Paul Sheppard, Ken Lewis, Paul Bishop, Miguel A. Cruz, Jose A. Lopez, and Joachim Fruebis

From ZymoGenetics, Cardiovascular Biology, Seattle, WA; and Baylor College of Medicine, Houston, TX.

CTRP-1 is a novel member of the C1qTNF–related protein family containing family characteristic collagen and TNF-like domains and shows marked expression in vascular wall tissue. We observed that recombinant human CTRP-1 specifically bound to fibrillar collagen and blocked collagen-induced platelet aggregation. CTRP-1 completely or partially prevented VWF and GPVI-Fc4 binding to collagen, respectively. However, GPVI-Fc4 failed to compete for the binding of CTRP-1 to collagen. CTRP-1 had no effects on {alpha}2{beta}1 integrin I–domain binding to collagen. Using whole human blood under flow at low and high shear rates, CTRP-1 prevented platelets from accumulating on a collagen-coated surface but had no effects on "platelet-rolling" on a surface coated with VWF. These data suggest that CTRP-1 prevents collagen-induced platelet aggregation by specific blockade of VWF binding to collagen. By using the Folts vascular injury model in nonhuman primates (Macaca fascicularis), we were able to demonstrate that CTRP-1 can prevent platelet thrombosis in vivo. This effect was achieved in the absence of changes in activated-clotting time (ACT) and template cut bleeding times, suggesting that CTRP-1 has promising antiplatelet thrombotic activity and most likely acts by pacifying the thrombogenic site of vascular injury.


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Platelet-collagen interaction: a new modulator
Alastair W. Poole
Blood 2006 107: 415a-416. [Full Text] [PDF]



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