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Six glutathione-containing inhibitors of the human NADP-linked 15-hydroxyprostaglandin dehydrogenase have been isolated from placental homogenates. Glutathione disulfide is one of these inhibitors. Although the structures of the other five have not been fully elucidated, all are disulfides. Studies with these compounds and with other mixed disulfides have shown that the glutathione mixed disulfides of beta-mercaptopyruvate, mercaptoacetate, and beta-mercaptolactate are more effective inhibitors of the enzyme than are the glutathione-containing mixed disulfides isolated from placental homogenates. beta-Mercaptolactate is particularly noteworthy because of its low Ki (0.13 microM). The results reported here suggest that the activity of the prostaglandin dehydrogenase may be influenced in vivo by various glutathione mixed disulfides.
H Chung, and
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E Williams-Ashman, and
J Jarabak
September 1987,
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H Chung, and
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August 1988,
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H Chung, and
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March 1972,
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H Chung, and
J Fried, and
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J Jarabak
June 1982,
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H Chung, and
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J Jarabak
August 1979,
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H Chung, and
J Fried, and
E Williams-Ashman, and
J Jarabak
March 1988,
Prostaglandins,
H Chung, and
J Fried, and
E Williams-Ashman, and
J Jarabak
March 1986,
Biochemical and biophysical research communications,
H Chung, and
J Fried, and
E Williams-Ashman, and
J Jarabak
November 1982,
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H Chung, and
J Fried, and
E Williams-Ashman, and
J Jarabak
June 1977,
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H Chung, and
J Fried, and
E Williams-Ashman, and
J Jarabak
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