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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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Submitted April 11, 2005
Accepted August 26, 2005

C1q-TNF 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 Ellsworth, Paul Sheppard, Ken Lewis, Paul Bishop, Miguel A Cruz, Jose A Lopez, and Joachim Fruebis*

Cardiovascular Biology, ZymoGenetics, Seattle, WA, USA
Baylor College of Medicine, Houston, TX, USA

* Corresponding author; email: jofr{at}zgi.com.

CTRP-1 is a novel member of the C1q-TNF 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 non-human 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 CTRP-1 has promising anti-platelet thrombotic activity and most likely acts by pacifying the thrombogenic site of vascular injury.


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