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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2004;24:989.)
© 2004 American Heart Association, Inc.

Editorials

Fifty (or More) Ways to Leave Your Platelets (in a Thrombus)

Lawrence Brass

From the Hematology/Oncology Section, University of Pennsylvania Health System, Philadelphia, Penn.

Correspondence to Dr Lawrence F. Brass, University of Pennsylvania, Room 913, BRB-II, 415 Curie Blvd, Philadelphia, PA 19104. E-mail brass@mail.med.upenn.edu

An extract of the first 250 words of the full text is provided, because this article has no abstract.

With a nod to Paul Simon, there may be more ways to activate platelets than there were ways to leave your lover in his song from the 70’s—or at least it seems that way. Gas6 is a vitamin K–dependent, protein-S–related protein found in the -granules of resting platelets. Once platelet activation has occurred, Gas-6 appears in the fluid phase and on the platelet surface, where it presumably becomes bound after secretion. In this issue of Arteriosclerosis, Thrombosis, and Vascular Biology, Chen et al show that platelets express at least one of the known receptors for Gas-6, the receptor tyrosine kinase, Mer.¹ According to their observations, deletion of the gene encoding Mer in mice does not produce an overt bleeding phenotype or even prolong the bleeding time, but it does inhibit platelet aggregation, diminish the thrombotic response to vascular injury, and provide some protection against disseminated thrombosis.¹ These effects are less profound, but qualitatively similar to those reported several years ago by Angelillo-Scherrer et al in their studies on mice that lack Gas6,² and essentially similar to those they have subsequently reported in abstract form using mice that lack either Mer or two related receptors, Axl and Rse (also known as Sky).³

See page 1118

Gas6 is a 75-kDa protein with several distinct structural domains, starting with an N-terminal domain that includes -carboxylated glutamic acid (Gla) residues, a central domain with epidermal growth factor (EGF) repeats and two C-terminal G domains responsible for receptor binding and activation.^4,5 Gla residues are . . . [Full Text of this Article]

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