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 Blood, 11 June 2009, Vol. 113, No. 24, pp. 6051-6060.
Prepublished online as a Blood First Edition Paper on February 13, 2009; DOI 10.1182/blood-2008-07-170571.

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PLENARY PAPER

C-terminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occlusion and cerebral stroke

Zongdong Li1, Michael A. Nardi2, Yong-Sheng Li3, Wei Zhang1, Ruimin Pan1, Suying Dang1, Herman Yee4, David Quartermain3, Saran Jonas3, and Simon Karpatkin1

Departments of 1 Medicine, 2 Pediatrics, 3 Neurology, and 4 Pathology, New York University School of Medicine, NY

Anti-platelet integrin GPIIIa49-66 antibody (Ab) induces complement-independent platelet oxidative fragmentation and death by generation of platelet peroxide following NADPH oxidase activation. A C-terminal 385–amino acid fragment of ADAMTS-18 (a disintegrin metalloproteinase with thrombospondin motifs produced in endothelial cells) induces oxidative platelet fragmentation in an identical kinetic fashion as anti–GPIIIa49-66 Ab. Endothelial cell ADAMTS-18 secretion is enhanced by thrombin and activated by thrombin cleavage to fragment platelets. Platelet aggregates produced ex vivo with ADP or collagen and fibrinogen are destroyed by the C-terminal ADAMTS-18 fragment. Anti–ADAMTS-18 Ab shortens the tail vein bleeding time. The C-terminal fragment protects against FeCI3-induced carotid artery thrombosis as well as cerebral infarction in a postischemic stroke model. Thus, a new mechanism is proposed for platelet thrombus clearance, via platelet oxidative fragmentation induced by thrombin cleavage of ADAMTS-18.


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