Characterization of multiple Chinese hamster carbonyl reductases

Terada, Tomoyuki; Sugihara, Y.; Nakamura, Kayo; Sato, Ryuichiro; Sakuma, Satoru; Fujimoto, Yohko; Fujita, Tadashi; Inazu, Norihisa; Maeda, Masatomo

doi:10.1016/s0009-2797(00)00240-4

Cited by 13 publications

(8 citation statements)

References 46 publications

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“…For CHCR2, metyrapone and steroids such as 5β-androstane-3,17-dione, 5α-androstane-3,17-dione, and 5α-androstane-17β-ol-3-one are better substrates (Terada et al, 2001). CHCR3 has relatively lower activity toward 4-nitrobenzaldehyde and pyridine-4-carboxaldehyde than CHCR1 and CHCR2.…”

Section: Chinese Hamster Carbonyl Reductases (Chcr 1-3) Terada Et Almentioning

confidence: 97%

Carbonyl Reductases and Pluripotent Hydroxysteroid Dehydrogenases of the Short-chain Dehydrogenase/reductase Superfamily

Hoffmann¹,

Maser²

2007

Drug Metabolism Reviews

200

124

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Carbonyl reduction of aldehydes, ketones, and quinones to their corresponding hydroxy derivatives plays an important role in the phase I metabolism of many endogenous (biogenic aldehydes, steroids, prostaglandins, reactive lipid peroxidation products) and xenobiotic (pharmacologic drugs, carcinogens, toxicants) compounds. Carbonyl-reducing enzymes are grouped into two large protein superfamilies: the aldo-keto reductases (AKR) and the short-chain dehydrogenases/reductases (SDR). Whereas aldehyde reductase and aldose reductase are AKRs, several forms of carbonyl reductase belong to the SDRs. In addition, there exist a variety of pluripotent hydroxysteroid dehydrogenases (HSDs) of both superfamilies that specifically catalyze the oxidoreduction at different positions of the steroid nucleus and also catalyze, rather nonspecifically, the reductive metabolism of a great number of nonsteroidal carbonyl compounds. The present review summarizes recent findings on carbonyl reductases and pluripotent HSDs of the SDR protein superfamily.

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Section: Chinese Hamster Carbonyl Reductases (Chcr 1-3) Terada Et Almentioning

confidence: 97%

Carbonyl Reductases and Pluripotent Hydroxysteroid Dehydrogenases of the Short-chain Dehydrogenase/reductase Superfamily

Hoffmann¹,

Maser²

2007

Drug Metabolism Reviews

200

124

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“…PGF 2α can be produced directly from PGH 2 by aldo-keto reductase family 1 members B1 and C3 (AKR1B1 and AKR1C3). Alternatively, it can be synthesized via PGE 2 by the action of the enzymes carbonyl reductase 1 (CBR1), AKR1C1 and AKR1C2 ( Terada et al ., 2001 ; Dozier et al ., 2008 ) or by reduction of PGD 2 by AKR1C3. Prostanoids such as PGI 2 and TXA 2 are deactivated spontaneously before they are exported into the circulation as inactive metabolites.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive expression analysis of prostanoid enzymes and receptors in the human endometrium across the menstrual cycle

Catalano

Wilson

Boddy

et al. 2010

Molecular Human Reproduction

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Prostanoids are well-described primary mediators of inflammatory processes and are essential for the normal physiological function of the female reproductive system. The aim of this study was to determine the temporal expression of the prostanoid biosynthetic enzymes (PTGS1, PTGS2, PTGES, PTGES2, PTGES3, AKR1B1, AKR1C3, CBR1, HPGDS, PTGDS, PTGIS, TBXAS1 and HPGD) and the prostanoid receptors (PTGER1, PTGER2, PTGER3, PTGER4, PTGFR, PTGDR, GPR44, PTGIR and TBXA2R) in the human endometrium throughout the menstrual cycle. The analysis identified PTGFR to have a distinct expression profile compared with other components of the prostanoid system, as expression is maximal during the proliferative phase. Immunohistochemical analysis for PTGER1 suggests a dual function for this receptor depending on its temporal (proliferative versus secretory) and spatial (nuclear versus cell membrane) expression. The expression profiles of the PGF2α synthases identified AKR1B1 and CBR1 as the likely regulators of PGF2α production during the menstrual phase. Immunohistochemical analysis for AKR1B1, CBR1 and AKR1C3 suggest expression to be in the glandular epithelium and vasculature. This study represents the first comprehensive analysis of the components of prostanoid biosynthetic and signalling pathway in the human endometrium. The expression profiles described have the potential to identify specific prostanoid components that may be dysregulated in inflammatory-associated disorders of the endometrium.

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“…The functional inactivation of PGs occurs when the 15-hydroxyl group is oxidized to a 15-keto group by . In addition, carbonyl reductase 1 (CBR1) can also inactivate PGE2 by converting it into PGF2a (23). It has been shown that progesterone can increase 15-PGDH activity in pregnant rat uterus and decrease PGF2a production to maintain uterine quiescence (24).…”

mentioning

confidence: 99%

Differential expression and regulation of prostaglandin transporter and metabolic enzymes in mouse uterus during blastocyst implantation

Gao

Wei

Diao

et al. 2007

Fertility and Sterility

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Characterization of multiple Chinese hamster carbonyl reductases

Cited by 13 publications

References 46 publications

Carbonyl Reductases and Pluripotent Hydroxysteroid Dehydrogenases of the Short-chain Dehydrogenase/reductase Superfamily

Carbonyl Reductases and Pluripotent Hydroxysteroid Dehydrogenases of the Short-chain Dehydrogenase/reductase Superfamily

Comprehensive expression analysis of prostanoid enzymes and receptors in the human endometrium across the menstrual cycle

Differential expression and regulation of prostaglandin transporter and metabolic enzymes in mouse uterus during blastocyst implantation

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