Identification of Human Plasma Lysophospholipase D, a Lysophosphatidic Acid-producing Enzyme, as Autotaxin, a Multifunctional Phosphodiesterase*
By A. Tokumura, E. Majima, Yuko Kariya, Kyoko Tominaga, K. Kogure, K. Yasuda, K. Fukuzawa. Journal of Biological Chemistry, 2002
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We purified human plasma lysophospholipase D that produces physiologically active lysophosphatidic acid and showed that it is a soluble form of autotaxin, an ecto-nucleotide pyrophosphatase/phosphodiesterase, originally found as a tumor cell motility-stimulating factor. Its lower K m value for a lysophosphatidylcholine than that for a synthetic substrate of nucleotide suggests that lysophosphatidylcholine is a more likely physiological substrate for autotaxin and that its predicted physiological and pathophysiological functions could be mediated by its activity to produce lysophosphate acid, an intercellular mediator. Recombinant autotaxin was found to have lysophospholipase D activity; its substrate specificity and metal ion requirement were the same as those of the purified plasma enzyme. The activity of lysophospholipase D for exogenous lysophosphatidylcholine in human serum was found to increase in normal pregnant women at the third trimester of pregnancy and to a higher extent in patients in threatened preterm delivery, suggesting its roles in induction of parturition.
Subfields: Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/f0a49c5ae72073e7aefceb2797b1e1e562bee050
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Citations in the corpus
- Hooked on fat: the role of lipid synthesis in cancer metabolism and tumour development (2013, background): “LPA, which can also be produced by the extracellular lysophospholipase autotaxin (Tokumura et al., 2002), activates cell proliferation, migration and survival through binding to G-protein-coupled receptors (Mills and Moolenaar, 2003). dmm.biologists.org1356 The role of lipid synthesis in…”
- International Union of Pharmacology LVIII: Update on the P2Y G Protein-Coupled Nucleotide Receptors: From Molecular Mechanisms and Pathophysiology to Therapy (2006, background): “…substrate selectivity for E-NPP2 has been expanded with the observation that this enzyme, but not E-NPP1 or E-NPP3, hydrolyzes lysophosphatidylcholine into lysophosphatidic acid, linking the activity of the enzyme with tumor cell growth and motility (Tokumura et al., 2002; Umezu-Goto et al., 2002).”