Disease relevance of Cbr1

• In a buffer containing 1% albumin and 10 microM quinone, 9,10-phenanthrenequinone is reduced most rapidly by the carbonyl reductase, 2-methyl-1,4-naphthoquinone is reduced most rapidly by the rat enzyme, and 3,6-pyrenequinone is reduced most rapidly by the Clostridium enzyme [1].
• The protective role of 11 beta-hydroxysteroid dehydrogenase/carbonyl reductase against tobacco-smoke related lung cancer [2].

High impact information on Cbr1

• Characterization of ovarian carbonyl reductase gene expression during ovulation in the gonadotropin-primed immature Rat [3].
• Treatment of the animals with ovulation-blocking doses of epostane (an inhibitor of progesterone synthesis) or indomethacin (an inhibitor of prostanoid synthesis) did not reduce the expression of ovarian carbonyl reductase [3].
• The data suggest that the nitroreduction is catalyzed largely by a xanthine oxidase and partially by a diaphorase and 9-oxoreduction by a carbonyl reductase [4].
• Changes in rat ovarian carbonyl reductase activity and content during the estrous cycle, and localization [5].
• Changes and localization of ovarian carbonyl reductase during pseudopregnancy and pregnancy in rats [6].

Biological context of Cbr1

• Nevertheless, the temporal pattern of expression of carbonyl reductase after the induction of ovulation suggests that this enzyme activity is at least indirectly associated with the ovulatory process [3].
• The recombinant enzyme exhibited the same substrate specificity and susceptibility to inhibitors as the enzyme isolated from rat testis, and also closely resembled human carbonyl reductase [7].
• The sequence obtained demonstrated a high degree of homology with an internal amino acid sequence in human carbonyl reductase (EC 1.1.1.184) [8].
• These observations indicate that tissue distribution of 20beta-HSD is similar to that of carbonyl reductase in the human and rat [9].
• Since the severe cardiotoxicity of anthracyclines has been attributed to the intramyocardial formation of C-13 alcohol metabolites, the kinetics of cardiac metabolite formation and disposition as well as the effect of carbonyl reductase inhibitors are of specific interest [10].

Anatomical context of Cbr1

• Cloning and expression of carbonyl reductase from rat testis [7].
• A carbonyl-reductase-like enzyme is exclusively expressed in rat reproductive tissues and adrenal glands [7].
• Differential hormonal regulation of carbonyl reductase activities in liver and kidney microsomes of rat [11].
• 2. The treatment with TP had no effect on the CR activity in liver microsomes of the ovariectomized or hypophysectomized female rat [11].
• CR was primarily localized in interstitial gland cells and in theca interna cells but was not found in corpora lutea cells in the ovary during the estrous cycle [6].

Associations of Cbr1 with chemical compounds

• On the other hand, renal microsomal CR activities decreased by Tx and Hx were markedly increased by the treatment with TP [11].
• The changes in ovarian CR activity, i.e. the rapid decrease with progressing pseudopregnancy and pregnancy, correlated with the increase in progesterone and the decrease in LH [6].
• The reaction was strongly inhibited by quercitrin, a specific inhibitor of carbonyl reductase [12].
• Menadione (an inhibitor of aldehyde oxidase) and quercetin (an inhibitor of carbonyl reductase) did not show any effects [13].
• This study was designed to elucidate strain- and sex-related differences of carbonyl reductase activity in rat kidney by using the oral antidiabetic drug acetohexamide as substrate [14].

Other interactions of Cbr1

• Properties of carbonyl reductase activity of sepiapterin reductase, an enzyme involved in the biosynthesis of tetrahydrobiopterin [15].

Analytical, diagnostic and therapeutic context of Cbr1

• Northern blot analyses indicated a 14-fold increase in ovarian mRNA for carbonyl reductase, with expression reaching a peak at 8 h after hCG treatment and then declining to negligible levels during the next 16 h [3].
• 1. In the male rat, hepatic microsomal carbonyl reductase (CR) activity decreased by testectomy (Tx) was restored to the control level by the treatment with testosterone propionate (TP), even though the enzyme activity decreased by hypophysectomy (Hx) was not increased by the treatment with TP [11].
• Ovarian CR activity was measured by using two substrates that reflect the activity of the enzyme in rats, and the enzyme content was determined by western blot analysis [16].
• Carbonyl reductase activity and content in the rat ovary were measured at various stages of the estrous cycle, and the enzyme protein in the ovary was localized by immunohistochemistry [5].
• Both eCG and oFSH significantly increased the ovarian carbonyl reductase concentration 48 h after treatment compared with the saline-treated group, but the increase with eCG was approximately twice that with oFSH [17].

References