Correction for Arterioscler Thromb Vasc Biol 23 (5) a-1-a-83.

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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2003;23:1479.)
© 2003 American Heart Association, Inc.

Correction

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

Below are four abstracts from the 4th Annual Conference on Arteriosclerosis, Thrombosis, and Vascular Biology (2003;23:a-1–a-83). Abstracts 22 and P150 have corrected author lines. Abstracts P59 and P66 were originally withdrawn but later accepted for publication.

22

Lipid Phosphate Phosphatase 1 Regulates Lysophosphatidic Acid Signaling in Platelets

Susan S Smyth, Yury Sigal, Zehra Pamuklar, UNC-Chapel Hill, Chapel Hill, NC; Yong Xu, Univeristy of Utah, Salt Lake City, UT; Glenn Prestwich, The Univeristy of Utah, salt Lake City, UT; Andrew J Morris, UNC-Chapel Hill, Chapel Hill, NC

Lysophosphatidic acid (LPA) is the prototypic member of a class of receptor active lysopholipid mediators that exert their effects by binding to the Edg family of G-protein-coupled cell surface receptors. LPA stimulates platelets, leukocytes, endothelial cells, and smooth muscle cells and may be a key mediator of both inflammatory and thrombotic responses. Several mechanism(s) for LPA production have been reported, however, little is known about the enzymes and pathways responsible for LPA inactivation. The dephosphorylated products of LPA are receptor-inactive and, therefore, degradation of LPA by cell surface lipid phosphate phosphatases (LPPs) could provide an important mechanism to modulate cellular responses to LPA. We report that human platelets contain both soluble and membrane-associated LPP activities. Intact platelets and platelet-derived microparticles catalyze the rapid dephosphorylation of LPA and, to a lesser extent, the related lipid spingoshine-1-phosphate. RNA and immunological analysis indicate that LPP1 is the predominant species in human platelets. This novel enzyme is a member of a recently identified class of hexa-helical integral membrane . . . [Full Text of this Article]