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. Oestrone is rapidly taken up by isolated perfused rat liver (t 1/2 less than 2 min) to yield at least 10 metabolites excreted in the bile; peak concentration occurs after about 20 min. 2. Sulphated metabolites of oestrone appear in the perfusate, reaching peak concentration at about 10 min, and then slowly disappear. 3. Sulphated metabolites of oestrone accumulate in the liver during the first 10 min. They are partly converted to sulphoglucuronides (steroid 3-sulphates conjugated with glucuronic acid in the D ring) and partly hydrolysed to be reconjugated as glucuronides. 4. The major biliary metabolites of oestrone in isolated perfused rat liver are glucuronides and sulphoglucuronides, but free steroids, sulphates and polar metabolites are also so excreted. 5. The isolated perfused guinea pig liver also rapidly takes up oestrone (t 1/2 less than 2 min) but, in contrast to the rat, a single glucuronide is the only quantitatively important metabolite in the bile: it is also extensively secreted into the perfusate where it reaches peak concentration at about 10 min. 6. In perfused guinea pig liver, oestrone does not form sulphoglucuronides, and sulphates are only minor metabolites; this is not due to lack of the appropriate sulphotransferase because oestradiol 17 beta-(beta-D-glucuronide) is extensively sulphated in this system. 7. Oestradiol 17 beta-(beta-D-glucuronide) is not cholestatic in the isolated perfused guinea pig liver although it is in rat liver. 8. There is a similar species difference in the metabolism of dehydroepiandrosterone in the two species: the rat forms sulphoglucuronides, the guinea pig does not. 9. The perfused rat liver extensively hydroxylates, presumably on the D ring, 17-deoxyoestrone and 17-deoxydehydroepiandrosterone. 10. The inability of perfused guinea pig liver to form sulphoglucuronides from oestrone or dehydroepiandrosterone is probably due to its restricted ability to hydroxylate the D ring of steroids. 11. Both rat and guinea pig biles contain beta-glucuronidase, about 80 and 230 sigma units/ml, respectively.
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PMID:The metabolism of oestrone and some other steroids in isolated perfused rat and guinea pig livers. 296 41

Daily urine samples were collected from 5 female golden lion tamarins (Leontopithecus rosalia) over a period of 3 or more months, and urinary oestrogen concentrations were determined by radioimmunoassay. Four females exhibited regular patterns of oestrogen excretion, with a peak-to-peak periodicity of 19.6 +/- 1.4 days. Levels of oestrogen excretion tended to vary between, but not within, individual females. Post-partum oestrogen patterns included periods of clear oestrogen cyclicity before conception, with dramatic elevations in oestrogen excretion following conception. Oestrone was the predominant urinary oestrogen excreted by female lion tamarins. Enzyme hydrolysis with Helix pomatia beta-glucuronidase/sulphatase was an efficient method of liberating conjugated oestrogens in tamarin urine. Urinary oestrogen determinations can provide useful information about reproductive status in female lion tamarins.
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PMID:Patterns of urinary oestrogen excretion in female golden lion tamarins (Leontopithecus rosalia). 393 66

The metabolism of endogenous estrogens, estradiol and estrone, and the irreversible binding of estrogens to cellular macromolecules have been examined and compared in subcellular microsomal and in intact hepatocyte preparations. In studies with rat liver microsomal preparations containing estradiol, an NADPH-generating system, and denatured DNA, the irreversible binding of radiolabeled steroid metabolite(s) to the microsomal proteins was 3.26 nmoles/mg protein in 1 hr (S.D. 0.39; 7.9% of total steroid) while binding to DNA was found to be 0.288 nmole/mg DNA/mg protein (S.D. 0.025; 0.39% of total steroid). No significant difference was observed between microsomal preparations from untreated, phenobarbital-treated or 3-methylcholanthrene-treated rats. Irreversible binding to proteins was also demonstrated in the intact hepatocyte cell incubations. After 2-hr incubations of estradiol with hepatocytes, 5.9% (S.D. 1.4%) of the steroid(s) was irreversibly associated with cellular proteins (approximately 1.43 pmoles/mg/min). Analysis of the organic-soluble metabolites demonstrated the presence of the catechol estrogens and their metabolites, 2-hydroxyestradiol, 2-hydroxyestrone, 2-methoxyestradiol, and 2-methoxyestrone. Estrone and estriol were also identified. The aqueous-soluble materials isolated from hepatocyte incubations contained glucuronide, sulfate, and apparent thioether conjugates, as determined by liberation from estrogen metabolites by treatment with beta-glucuronidase, sulfatase, and Raney nickel. Thus, extensive primary and secondary metabolism of estrogens occurs in intact hepatocyte incubations. Furthermore, irreversible binding of estrogens to cellular proteins occurs in these intact cells having demonstrated conjugative pathways of metabolism.
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PMID:Estrogen metabolism in rat liver microsomal and isolated hepatocyte preparations--I. Metabolite formation and irreversible binding to cellular macromolecules. 650 37

To understand the means whereby a charged, estrogen conjugate may be transferred across guinea pig amnion and chorion, the permeability to [3H]estrone-[14C]glucuronide was examined at 45 days and near term. No evidence of deconjugation was obtained in either early or late amnion, despite significantly greater transfer near term. Early amnion was virtually impermeable, regardless of ATP depletion. In contrast, early chorion transferred estrone-glucuronide without any requirement for deconjugation or ATP. No effect of tissue orientation was observed in amnion; whereas, incubations from maternal to fetal side of late chorion exhibited beta-glucuronidase activity. Inhibition of the latter demonstrated that hydrolysis was concomitant with but not required for transport. [3H]Estrone produced by deconjugation was enzymatically reduced after pubic symphysis relaxation, although beta-glucuronidase activity began prior to this stage. Transport across late fetal membranes was not saturable and chorion incubations from maternal to fetal side demonstrated a lower transport capacity. In either tissue orientation, late chorion displayed a lower rate of transfer than amnion. These results indicate that fetal membranes possess distinct abilities for transferring intact estrone-glucuronide, depending on stage of development and tissue orientation. The passive nature of transport and its dependence on structural characteristics is consistent with possible regulation of tight junctions.
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PMID:Beta-glucuronidase is not required for transfer of [3H]-estrone-[14C]glucuronide across guinea pig fetal membranes. 971 13