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cDNA cloning, expression and characterization of human prostaglandin F synthase 1
Author(s) -
Suzuki-Yamamoto Toshiko,
Nishizawa Mikio,
Fukui Motonari,
Okuda-Ashitaka Emiko,
Nakajima Tatsuya,
Ito Seiji,
Watanabe Kikuko
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01551-3
Subject(s) - cloning (programming) , complementary dna , molecular cloning , atp synthase , microbiology and biotechnology , prostaglandin , chemistry , biology , genetics , biochemistry , enzyme , gene , computer science , programming language
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.