Comparison of substrate specificities of the human placental NAD- and NADP-linked 15-hydroxyprostaglandin dehydrogenases

Prostaglandins
J Jarabak, J Fried

Abstract

A study of the relative activity of the purified placental NAD- and NADP-linked 15-hydroxyprostaglandin dehydrogenases with various prostaglandins and thromboxane B2 (TxB2) suggests that most, if not all, oxidation in the placenta of the 15-hydroxyl group of prostaglandins of the A, E, and F series as well as PGI2 (prostacyclin) and 6-keto PGF1 alpha is catalyzed by the NAD-linked enzyme. Prostaglandin B1 is an excellent substrate for the NADP-linked enzyme. Despite the conformational similarities between PGB1 and PGI2, the latter molecule is a poor substrate for the NADP-linked enzyme. Thromboxane B2 is not oxidized by the NAD-linked enzyme and is oxidized slowly by the NADP-linked enzyme.

References

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Citations

May 1, 1981·Prostaglandins·J M Korff, J Jarabak
Oct 1, 1995·Journal of Lipid Mediators and Cell Signalling·Charles Mark Ensor, H H Tai
Sep 1, 1989·Prostaglandins, Leukotrienes, and Essential Fatty Acids·S ItoO Hayaishi
Nov 16, 2002·Prostaglandins & Other Lipid Mediators·Hsin-Hsiung TaiFengxiang Yan
Sep 18, 2007·Molecular Endocrinology·Jeffrey D RoizenLouis J Muglia
Mar 15, 2012·World Journal of Gastroenterology : WJG·Li-Hong LouKai Wu
Mar 4, 2006·Reproduction : the Official Journal of the Society for the Study of Fertility·Marianne ParentMichel A Fortier
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Related Concepts

Hydroxyprostaglandin Dehydrogenases
NADH
NADP
Oxidation-Reduction
Placenta
Prostaglandins
Substrate Specificity
Thromboxane B2

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