Identification and biochemical characterization of a novel autotaxin isoform, ATXδ, with a four-amino acid deletion

Takafumi Hashimoto, Shinichi Okudaira, Koji Igarashi, Kotaro Hama, Yutaka Yatomi, Junken Aoki

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

Autotaxin (ATX) is lysophospholipase D, which converts lysophospholipids such as lysophosphatidylcholine (LPC) to lysophosphatidic acid (LPA), a bioactive lipid mediator with multiple biological roles. ATX is present in high concentrations in various biological fluids and is responsible for LPA production in these fluids. The plasma ATX level is altered in some patho-physiological conditions. Three splicing isoforms of ATX have been reported so far (ATXα, β and γ). In this study, we identified and characterized ATXδ, a novel alternative splice variant of ATX, which has a four-amino acid deletion in the L2 linker region of ATXβ. ATXδ was found to be the second major isoform following ATXβ and fully active. ATXβ and ATXδ showed similar divalent cation sensitivity and cell motility-stimulating activity. ATXβ and ATXδ are present in wide range of organism from fish to mammals. Among them, only ATXδ was found in Gallus gallus and Xenopus laevis, suggesting the indispensable role of the isoform. ATXδ was expressed in various human tissues with different expression patterns from that of ATXβ. These results show that ATXδ is a second major ATX isoform sharing similar biochemical characters with the major isoform, ATXβ, and is a potential biomarker.

Original languageEnglish
Pages (from-to)89-97
Number of pages9
JournalJournal of biochemistry
Volume151
Issue number1
DOIs
Publication statusPublished - 2012 Jan

Keywords

  • alternative splicing
  • autotoxin
  • lysophosphatidic acid
  • lysophosphatidylcholine
  • lysophospholipase D

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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