MISC

1999年12月3日

cDNA cloning, expression and characterization of human prostaglandin F synthase

FEBS Letters
  • Toshiko Suzuki-Yamamoto
  • ,
  • Mikio Nishizawa
  • ,
  • Motonari Fukui
  • ,
  • Emiko Okuda-Ashitaka
  • ,
  • Tatsuya Nakajima
  • ,
  • Seiji Ito
  • ,
  • Kikuko Watanabe

462
3
開始ページ
335
終了ページ
340
記述言語
英語
掲載種別
DOI
10.1016/S0014-5793(99)01551-3

A cDNA clone of prostaglandin F synthase (PGFS) was isolated from human lung by using cDNA of bovine lung-type PGFS as a probe and its protein expressed in Escherichia coli was purified to apparent homogeneity. The human PGFS catalyzed the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9α,11β-PGF2 to PGD2. The k(cat)/K(m) values for PGD2 and 9α,11β-PGF2 were 21 000 and 1800 min-1 mM-1, respectively, indicating that the catalytic efficiency for PGD2 and 9α,11β-PGF2 was the highest among the various substrates, except for PQ. The PGFS activity in the cytosol of human lung was completely absorbed with anti-human PGFS antiserum. Moreover, mRNA of PGFS was expressed in peripheral blood lymphocytes and the expression in lymphocytes was markedly suppressed by the T cell mitogen concanavalin A. These results support the notion that human PGFS plays an important role in the pathogenesis of allergic diseases such as asthma. Copyright (C) 1999 Federation of European Biochemical Societies.

リンク情報
DOI
https://doi.org/10.1016/S0014-5793(99)01551-3
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/10622721

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