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Lysophospholipase D/Autotaxin in Lysophospholipid Biology

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Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) are bioactive lysophospholipid mediators with a wide variety of biological actions. G-protein-coupled receptors for LPA and S1P have been identified, and physiological and pathological significances of the lysophospholipids and their receptors are under intensive investigation. Furthermore, specific agonists and antagonists for the receptors have been developed for clinical applications. However, mechanisms underlying their production have not yet been fully elucidated. Recently, autotaxin, an exo-phosphodiesterase implicated in tumor cell migration, has been discovered as lysophospholipase D that produces LPA and S1P from lysophosphatidylcholine and sphingosylphosphorylcholine, respectively. In this article, I reviewed the structure, expression, substrate specificity, enzymatic function, specific inhibitors and pathophysiological significances of lysophospholipase D/autotaxin.

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Keywords: Lysophospholipase D; autotoxin; lysophosphatidic acid; lysophosphatidylcholine; sphingosine 1-phosphate; sphingosylphosphorylcholine; tumor metastasis

Document Type: Research Article

Affiliations: Laboratory of Pharmacology,College of Pharmacy, Pusan National University, San 30, Jang-Jun-dong,Geum-Jung-gu, Busan 609-735, Republic of Korea.

Publication date: 2007-02-01

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  • Current Enzyme Inhibition aims to publish all the latest and outstanding developments in enzyme inhibition studies with regards to the mechanisms of inhibitory processes of enzymes, recognition of active sites, and the discovery of agonists and antagonists, leading to the design and development of new drugs of significant therapeutic value. Each issue contains a series of timely, in-depth reviews written by leaders in the field, covering a range of enzymes that can be exploited for drug development. Current Enzyme Inhibition is an essential journal for every pharmaceutical and medicinal chemist who wishes to have up-to-date knowledge about each and every development in the study of enzyme inhibition.
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