Cellular source(s) of platelet-activating-factor acetylhydrolase activity in plasma

Koichiro Asano, Shinichiro Okamoto, Kouichi Fukunaga, Tetsuya Shiomi, Takehiko Mori, Makiko Iwata, Yasuo Ikeda, Kazuhiro Yamaguchi

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91 Citations (Scopus)


Platelet activating factor (PAF) is immediately degraded and inactivated in the bloodstream by plasma PAF acetylhydrolase (PAF-AH). Although plasma PAF-AH-like activity was secreted in vitro from various cell types such as macrophages and hepatocytes, the exact cellular source(s) of this enzyme activity in vivo remains unclear. There is a naturally-occurring missense mutation (V279F) in the plasma PAF-AH gene in the Japanese population which results in complete loss of the enzyme activity. We analyzed 52 Japanese who had received an allogeneic bone marrow transplant and maintained donor-derived hematopoiesis. Ten recipients had chimeric plasma PAF-AH genotypes between the donor-derived peripheral blood leukocytes and the recipient-derived epithelial cells of buccal mucosa. Multiple regression analysis demonstrated that PAF-AH activity in plasma depended on the donor's genotype (standardized regression coefficient = 0.68, P < 0.0001), but not on the recipient's genotype (p = 0.48). One recipient who was a V279F homozygote in leukocytes and wild type homozygote in buccal mucosa had undetectable PAF-AH activity in plasma. We conclude that most of the PAF-AH activity in human plasma originates from hematopoietic lineage cells.

Original languageEnglish
Pages (from-to)511-514
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 1999 Aug 2


  • Bone marrow transplantation
  • Hepatocytes
  • Macrophages

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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