Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The effects of oestrogens, testosterone, progesterone and medroxyprogesterone acetate (MPA) on the rate of N-demethylation of ethylmorphine (EM) to norethylmorphine (NEM) were studied in human adult liver microsomes. 2. N-Demethylase activity was found to be inhibited by progesterone and MPA to a similar extent while oestrogens and testosterone had no or negligible effects. 3. These findings prompted us to measure the N-demethylation of EM in relation to serum progesterone concentration in vivo in three groups of volunteers with large physiological differences in their endogenous levels of progesterone, i.e. i) pregnant women, ii) non-pregnant ovulating women and iii) men. 4. The metabolic ratio (MRP) of EM to NEM in plasma 60 min after dosage and the corresponding ratio in urine sampled for 6 h (MRU,1), measured on two occasions 14 days apart were used to reflect intraindividual variation in the rate of N-demethylation. 5. The average difference in MRP and MRU,1 between the two occasions was similar in all groups. However, the variability in MRP between individuals within a group was significantly higher in ovulating women than in men, but this had no relation to the serum concentrations of progesterone or oestradiol. 6. The cumulative 12 h urinary excretion of EM, NEM and morphine (MO) after hydrolysis with beta-glucuronidase was about 46%. There was no difference in the metabolic ratio of EM to NEM and its conjugate(s) in the urine between the luteal and the follicular phases. Our findings suggest that the menstrual cycle does not influence the rate of N-demethylation of EM.
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PMID:N-demethylation of ethylmorphine in pregnant and non-pregnant women and in men: an evaluation of the effects of sex steroids. 138 49

Mouse L cells deficient in expression of the murine cation-independent mannose 6-phosphate receptor/insulin-like growth factor II receptor (CI-MPR/IGF-IIR) were stably transfected with a plasmid containing the cDNA for the human receptor. Transfected cells expressed high levels of the human receptor which functioned in the transport of lysosomal enzymes and was capable of binding 125I-IGF-II, both at the cell surface and intracellularly. Cell surface binding of 125I-IGF-II by the receptor could be inhibited by pretreatment of cells with antibodies to the receptor or by coincubation with the lysosomal enzyme, beta-glucuronidase. Expression of the receptor conferred on transfected cells the ability to internalize and degrade 125I-IGF-II. Cells transfected with the parental vector and those expressing the human CI-MRP/IGF-IIR were found to express an atypical binding site for IGF-II that was distinct from the CI-MPR/IGF-IIR and the type I IGF-receptor. The availability of two cell lines, one of which overexpresses the human CI-MPR/IGF-IIR and one deficient in expression of the murine receptor, may help in the analysis of the role of the receptor in mediating the biological effects of IGF-II. They should also be useful in examining the significance of binding of ligands, such as transforming growth factor-beta 1 precursor and proliferin to this receptor.
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PMID:Binding of insulin-like growth factor II (IGF-II) by human cation-independent mannose 6-phosphate receptor/IGF-II receptor expressed in receptor-deficient mouse L cells. 196 41