Archives of Medical Research
Volume 37, Issue 6 , Pages 696-699, August 2006

Catalytic Inactivation of Human Phospholipase D2 by a Naturally Occurring Gly901Asp Mutation

  • Yoshiji Yamada

      Affiliations

    • Department of Human Functional Genomics, Life Science Research Center, Mie University, Tsu, Japan
    • Corresponding Author InformationAddress reprint requests to: Yoshiji Yamada, MD, PhD, FAHA, Department of Human Functional Genomics, Life Science Research Center, Mie University, 1577 Kurima-machiya, Tsu, Mie 514-8507, Japan
  • ,
  • Yoshiko Banno

      Affiliations

    • Department of Cell Signaling, Gifu University Graduate School of Medicine, Gifu, Japan
  • ,
  • Hitoshi Yoshida

      Affiliations

    • Molecular Oncology Division, National Cancer Center Research Institute, Tokyo, Japan
  • ,
  • Ryosuke Kikuchi

      Affiliations

    • Nagoya University School of Health Sciences, Nagoya, Japan
  • ,
  • Yukihiro Akao

      Affiliations

    • Gifu International Institute of Biotechnology, Kakamigahara, Japan
  • ,
  • Takashi Murate

      Affiliations

    • Nagoya University School of Health Sciences, Nagoya, Japan
  • ,
  • Yoshinori Nozawa

      Affiliations

    • Gifu International Institute of Biotechnology, Kakamigahara, Japan

Received 1 September 2005; accepted 4 January 2006.

(ARCMED-D-05-00351)

Background

We previously showed that the 1814C→T (Thr577Ile) polymorphism of the human phospholipase D2 (PLD2) gene is associated with the prevalence of colorectal cancer, with the T allele representing a risk factor for this condition. However, we failed to detect a difference in PLD activity of cell lysates or membrane fractions between cells transfected with cDNAs encoding the Thr577 or Ile577 variants of PLD2. In the present study, we have examined the possible functional relevance of other naturally occurring polymorphisms (or mutations) of the human PLD2 gene that result in amino acid substitutions.

Methods

Human embryonic kidney cells were transfected with expression vectors for each PLD2 variant and assayed for enzyme activity in vitro and in vivo.

Results and Conclusions

The G→A (Gly901Asp) mutation of the human PLD2 gene was found to result in catalytic inactivation of the encoded protein.

Key Words: Phospholipase D2, Single nucleotide polymorphism, Mutation, Inactive mutant, Lipid metabolism

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PII: S0188-4409(06)00083-X

doi:10.1016/j.arcmed.2006.01.006

Archives of Medical Research
Volume 37, Issue 6 , Pages 696-699, August 2006