Immunohistochemical localization of guinea‐pig leukotriene B4 12‐hydroxydehydrogenase/15‐ketoprostaglandin 13‐reductase
作者： Toshiko Yamamoto , Takehiko Yokomizo , Akihide Nakao , Takashi Izumi , Takao Shimizu
DOI: 10.1046/J.0014-2956.2001.02462.X
关键词:
摘要: We have cloned cDNA for leukotriene B4 12-hydroxydehydrogenase (LTB4 12-HD)/15-ketoprostaglandin 13-reductase (PGR) from guinea-pig liver. LTB4 12-HD catalyzes the conversion of into 12-keto-LTB4 in presence NADP+, and plays an important role inactivating LTB4. The contained ORF 987 bp that encodes a protein 329 amino-acid residues with 78% identity porcine 12-HD. amino acids putative NAD+/NADP+ binding domain are well conserved among pig, guinea-pig, human, rat, rabbit enzymes. (gpLTB4 12-HD) was expressed as glutathione S-transferase (GST) fusion Escherichia coli, which exhibited similar enzyme activities to examined 15-ketoprostaglandin activity recombinant gpLTB4 12-HD, confirmed Kcat PGR is higher than by 200-fold. Northern Western blot analyses revealed 12-HD/PGR widely tissues such liver, kidney, small intestine, spleen, stomach. carried out immunohistochemical this various tissues. Epithelial cells calyx collecting tubules epithelial airway, alveoli, intestine stomach, hepatocytes were found express enzyme. These findings will lead identification unrevealed roles PGs LTs these
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