Antibodies against rabbit ω-hydroxylases of prostaglandins and fatty acids cross-react with leukotriene B4 ω-hydroxylase in human neutrophils (cytochrome P-450(LTBω))

Hideki Sumimoto, Y. Kikuta, E. Kusunose, M. Kusunose, S. Minakami

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Leukotriene B4 (LTB4) ω-hydroxylase activity in human neutrophil microsomes was significantly inhibited by antisera against three rabbit ω-hydroxylase P-450s, lung prostaglandin ω-hydroxylase (P-450p-2), small intestine prostaglandin A ω-hydroxylase (P-450ia), and kidney fatty acid ω-hydroxylase (P-450kd). In contrast, the activity is not affected by antibodies raised against the phenobarbital-inducible forms of P-450s from both rabbits and rats. These findings suggest that the LTB4 ω-hydroxylase (P-450LTBω) is structurally related to a group of rabbit ω-hydroxylase P-450s. The antiserum raised against P-450p-2 also inhibited the NADPH-dependent oxidation of 20-hydroxy LTB4 to 20-oxo LTB4 and 20-carboxy LTB4 by the microsomes, supporting that P-450LTBω is able to catalyze the subsequent oxidation of 20-hydroxy LTB4 as well as the ω-hydroxylation of LTB4.

Original languageEnglish
Pages (from-to)381-387
Number of pages7
JournalBiochemistry International
Volume20
Issue number2
Publication statusPublished - 1990

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Leukotriene B4
Mixed Function Oxygenases
Cytochrome P-450 Enzyme System
Prostaglandins
Neutrophils
Fatty Acids
Rabbits
Antibodies
Microsomes
Immune Sera
Prostaglandins A
Oxidation
Hydroxylation
Phenobarbital
NADP
Human Activities
Small Intestine
Rats
Kidney
Lung

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Antibodies against rabbit ω-hydroxylases of prostaglandins and fatty acids cross-react with leukotriene B4 ω-hydroxylase in human neutrophils (cytochrome P-450(LTBω)). / Sumimoto, Hideki; Kikuta, Y.; Kusunose, E.; Kusunose, M.; Minakami, S.

In: Biochemistry International, Vol. 20, No. 2, 1990, p. 381-387.

Research output: Contribution to journalArticle

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abstract = "Leukotriene B4 (LTB4) ω-hydroxylase activity in human neutrophil microsomes was significantly inhibited by antisera against three rabbit ω-hydroxylase P-450s, lung prostaglandin ω-hydroxylase (P-450p-2), small intestine prostaglandin A ω-hydroxylase (P-450ia), and kidney fatty acid ω-hydroxylase (P-450kd). In contrast, the activity is not affected by antibodies raised against the phenobarbital-inducible forms of P-450s from both rabbits and rats. These findings suggest that the LTB4 ω-hydroxylase (P-450LTBω) is structurally related to a group of rabbit ω-hydroxylase P-450s. The antiserum raised against P-450p-2 also inhibited the NADPH-dependent oxidation of 20-hydroxy LTB4 to 20-oxo LTB4 and 20-carboxy LTB4 by the microsomes, supporting that P-450LTBω is able to catalyze the subsequent oxidation of 20-hydroxy LTB4 as well as the ω-hydroxylation of LTB4.",
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AU - Minakami, S.

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N2 - Leukotriene B4 (LTB4) ω-hydroxylase activity in human neutrophil microsomes was significantly inhibited by antisera against three rabbit ω-hydroxylase P-450s, lung prostaglandin ω-hydroxylase (P-450p-2), small intestine prostaglandin A ω-hydroxylase (P-450ia), and kidney fatty acid ω-hydroxylase (P-450kd). In contrast, the activity is not affected by antibodies raised against the phenobarbital-inducible forms of P-450s from both rabbits and rats. These findings suggest that the LTB4 ω-hydroxylase (P-450LTBω) is structurally related to a group of rabbit ω-hydroxylase P-450s. The antiserum raised against P-450p-2 also inhibited the NADPH-dependent oxidation of 20-hydroxy LTB4 to 20-oxo LTB4 and 20-carboxy LTB4 by the microsomes, supporting that P-450LTBω is able to catalyze the subsequent oxidation of 20-hydroxy LTB4 as well as the ω-hydroxylation of LTB4.

AB - Leukotriene B4 (LTB4) ω-hydroxylase activity in human neutrophil microsomes was significantly inhibited by antisera against three rabbit ω-hydroxylase P-450s, lung prostaglandin ω-hydroxylase (P-450p-2), small intestine prostaglandin A ω-hydroxylase (P-450ia), and kidney fatty acid ω-hydroxylase (P-450kd). In contrast, the activity is not affected by antibodies raised against the phenobarbital-inducible forms of P-450s from both rabbits and rats. These findings suggest that the LTB4 ω-hydroxylase (P-450LTBω) is structurally related to a group of rabbit ω-hydroxylase P-450s. The antiserum raised against P-450p-2 also inhibited the NADPH-dependent oxidation of 20-hydroxy LTB4 to 20-oxo LTB4 and 20-carboxy LTB4 by the microsomes, supporting that P-450LTBω is able to catalyze the subsequent oxidation of 20-hydroxy LTB4 as well as the ω-hydroxylation of LTB4.

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