TAILIEUCHUNG - Báo cáo Y học: Immunohistochemical localization of guinea-pig leukotriene B4 12-hydroxydehydrogenase/15-ketoprostaglandin 13-reductase

The Department of Biochemistry and Molecular Biology, 2CREST of Japan Science and Technology Corporation; 3The Department of Nephrology and Endocrinology, Faculty of Medicine, The University of Tokyo, Japan We have cloned cDNA for leukotriene B4 12-hydroxydehydrogenase (LTB 4 12-HD)/15-ketoprostaglandin 13-reductase (PGR) from guinea-pig liver. LTB4 12-HD catalyzes the conversion of LTB4 into 12-keto-LTB4 in the presence of NADP1, and plays an important role in inactivating LTB4. The cDNA contained an ORF of 987 bp that encodes a protein of 329 amino-acid residues with a 78% identity with porcine LTB4 12-HD. The amino acids in the putative NAD1/NADP1 binding domain are well. | Eur. J. Biochem. 268 6105-6113 2001 FEBS 2001 Immunohistochemical localization of guinea-pig leukotriene B4 12-hydroxydehydrogenase 15-ketoprostaglandin 13-reductase Toshiko Yamamoto1 Takehiko Yokomizo1 2 Akihide Nakao3 Takashi Izumi1 2 and Takao Shimizu1 2 1The Department of Biochemistry and Molecular Biology 2CREST of Japan Science and Technology Corporation 3The Department of Nephrology and Endocrinology Faculty of Medicine The University of Tokyo Japan We have cloned cDNA for leukotriene B4 12-hydroxy-dehydrogenase LTB4 12-HD 15-ketoprostaglandin 13-reductase PGR from guinea-pig liver. LTB4 12-HD catalyzes the conversion of LTB4 into 12-keto-LTB4 in the presence of NADP and plays an important role in inactivating LTB4. The cDNA contained an ORF of 987 bp that encodes a protein of 329 amino-acid residues with a 78 identity with porcine LTB4 12-HD. The amino acids in the putative NAD NADP binding domain are well conserved among the pig guinea-pig human rat and rabbit enzymes. The guinea-pig LTB4 12-HD gpLTB4 12-HD was expressed as a glutathione S-transferase GST fusion protein in Escherichia coli which exhibited similar enzyme activities to porcine LTB4 12-HD. We examined the 15-ketoprostaglandin 13-reductase PGR activity of recombinant gpLTB4 12-HD and confirmed that the Kcat of the PGR activity is higher than that of LTB4 12-HD activity by 200-fold. Northern and Western blot analyses revealed that gpLTB4 12-HD PGR is widely expressed in guinea-pig tissues such as liver kidney small intestine spleen and stomach. We carried out immunohistochemical analyses of this enzyme in various guinea-pig tissues. Epithelial cells of calyx and collecting tubules in kidney epithelial cells of airway alveoli epithelial cells in small intestine and stomach and hepatocytes were found to express the enzyme. These findings will lead to the identification of the unrevealed roles of PGs and LTs in these tissues. Keywords leukotriene B4 12-hydroxydehydrogenase leukotriene B4 cDNA .

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