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cDNA cloning, expression and characterization of human prostaglandin F synthase11 The amino acid sequence of human PGFS and the amplified genomic DNA with PGFS-F4 and R5 were registered in the DDBJ under accession no. AB018580 and no. AB028065, respectively.

FEBS Letters
Wiley Blackwell (John Wiley & Sons)
Publication Date
DOI: 10.1016/s0014-5793(99)01551-3
  • Prostaglandin F Synthase
  • Human Lung
  • Aldo-Keto Reductase
  • Prostaglandin D2
  • 11β-Prostaglandin F2
  • Peripheral Blood Lymphocyte
  • Biology
  • Medicine


Abstract 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) D 2, PGH 2 and phenanthrenequinone (PQ), and the oxidation of 9α,11β-PGF 2 to PGD 2. The k cat/ K m values for PGD 2 and 9α,11β-PGF 2 were 21 000 and 1800 min −1 mM −1, respectively, indicating that the catalytic efficiency for PGD 2 and 9α,11β-PGF 2 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.

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