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)

The levels of several androgen responsive enzymes including beta-glucuronidase, alcohol dehydrogenase, D-amino acid oxidase and arginase, were compared in kidneys of normal and hypophysectomized female mice after treatment with testosterone. While hypophysectomy did not alter the basal level of glucuronidase, the androgen-mediated accumulation of kidney beta-glucuronidase was greatly decreased in hypophysectomized mice. Measurements of the rate of synthesis of glucuronidase showed that after androgen treatment the enzyme was synthesized in kidney of hypophysectomized mice at only 5% the normal rate. Glucuronidase activity in seven other organs was not appreciably affected by treatment with androgens or by hypophysectomy. Unlike the effect of hypophysectomy on kidney glucuronidase, there was no reduction in the accumulation of alcohol dehydrogenase or D-amino acid oxidase in kidney of hypophysectomized mice after androgen treatment. Hypophysectomy caused a large reduction in kidney arginase activity. However, subsequent administration of testosterone restored much of this activity. It is concluded that there are at least two mechanisms by which androgens increase enzyme activity in kidney. The normal increase in activity or rate of synthesis of beta-glucuronidase following androgen administration requires pituitary hormones and/or products of these hormones, while the increase in activity of enzymes like alcohol dehydrogenase and D-amino acid oxidase does not require pituitary hormones.
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PMID:Differential effect of hypophysectomy on the synthesis of beta-glucuronidase and other androgen-inducible enzymes in mouse kidney. 1 33

The approximate percentage of epithelium (Iepith) in a sample of human prostate tissue can be estimated by assaying the specific activity of epithelial marker enzymes, beta-glucuronidase or arginase. There is a good correlation between epithelial density and beta-glucuronidase activity per unit of tissue protein.
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PMID:Derivation and determination of a human prostatic epithelial index. 44 26

RMI 12,936 (7alpha-methyl-17beta-hydroxy-androst-5-en-one) was tested for androgenic activity in mouse kidney and for antiprogestational activity in guinea-pig uterus. RMI 12,936 stimulated an increase in kidney weight and in the activity of the androgen-responsive renal enzymes, beta-glucuronidase, alcohol dehydrogenase and arginase. RMI 12,936 was bound by the renal androgen receptor with a relative affinity approximately one-third that of testosterone. Although RMI 12,936 did not stimulate glycogen accumulation in guinea-pig endometrium in vivo, it was active in endometrial organ culture. When RMI 12,936 was combined with progesterone, glycogen accumulation in vitro was partly inhibited. RMI 12,936 was bound by the guinea-pig uterine progesterone receptor with a relative affinity of less than 1%. It is concluded that RMI 12,936 is an androgenic steroid with antifertility actions and in-vitro antiglycogenic activity.
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PMID:Androgenic effects of the antiprogestagen RMI 12,936. 63 20

To determine whether the activities of certain hydrolases (arylesterase, beta-glucuronidase, cathepsin L, plasminogen activators, arginase, glutaminase, asparaginase and adenosine deaminase) are changed during pregnancy, three groups of 15 apparently healthy women (aged 18-38 years) in their first, second and third trimester of pregnancy were compared to a control group formed of 15 non-pregnant women of similar ages. Enzyme and specific activities gradually increased from the first to the end of the third trimester of pregnancy for arylesterase and beta-glucuronidase, these increases being statistically significant (P < 0.01) in comparison to controls. However, as regards cathepsin L and plasminogen activators, the greatest increase was found in the second trimester. Arginase, glutaminase and asparaginase activities were very low and not distinguishable from the controls. In conclusion, differences in the activities of several hydrolases have been found in the sera of healthy pregnant women in comparison to controls.
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PMID:Variation in serum arylesterase, beta-glucuronidase, cathepsin L and plasminogen activators during pregnancy. 893 58

THE COMPOSITION OF ISOLATED NUCLEI AND CELL PREPARATIONS FROM TISSUES OF CALF, BEEF, HORSE, AND FOWL WAS STUDIED WITH RESPECT TO THE FOLLOWING COMPONENTS: 1. Liver and kidney arginase, catalase, and uricase; pancreatic lipase and amylase; cardiac muscle myoglobin; erythrocyte hemoglobin; intestinal alkaline phospharase. These are referred to as "special" components in view of their characteristically restricted distribution reflecting the differentiated nature of the tissues in question. 2. Esterase, beta-glucuronidase, alkaline and nucleotide phosphatases, adenosine deaminase, guanase, and nucleoside phosphorylase. These are enzymes of general distribution. The differences in nuclear composition noted with respect to the "special" components, together with the broad variability in nuclear activity found for enzymes of general distribution, led to the conclusion that nuclei are differentiated structures. The following distribution was observed: 1. "Special" components: Hemoglobin was found to be present in fowl and goose erythrocyte nuclei, but myoglobin was entirely absent from heart muscle nuclei; of the special enzymes listed, only catalase and arginase appeared to be concentrated in some of the nuclei. There was no significant nuclear concentration of lipase, amylase, uricase, or alkaline phosphatase. No simple relationship was found between the concentration of a special enzyme in a tissue and its activity in the corresponding nuclei. For example, arginase activity, which is high in mammalian liver and in fowl kidney, was found in liver, not kidney, nuclei. Similarly, catalase activity was demonstrated only in mammalian liver nuclei, although, in mammals, both liver and kidney are rich sources of this enzyme. 2. Enzymes of general distribution fell into three classes: (a) Those present in low concentrations, if at all, in the nuclei-alkaline phosphatase, the nucleotide phosphatases) and beta-glucuronidase. (b) Those present in nuclei in varying concentrations-esterase. (c) Those present in high proportions in most nuclei-adenosine deaminase, nucleoside phosphorylase, and guanase. The exceptionally low nuclear activity of intestinal mucosa with respect to these enzymes was discussed in relation to physiological considerations. The response of nuclei to changes in physiological state was demonstrated by experiments on starvation. The outstanding aspect of this response was a change in nuclear enzymatic activity opposing that observed in the cytoplasm. A comparison of fetal and adult mucosa cells led to the following tentative interpretation of the observed intracellular enzyme distribution: In cells tending to moribundity, as in those subjected to starvation, relative nuclear enzymatic activity falls. The occurrence of special enzymes in nuclei was considered in terms of differentiation, and the high nuclear concentration of the nucleoside-specific enzymes was interpreted in terms of general nuclear metabolic activity.
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PMID:Some enzymes of isolated nuclei. 1489 35

The detailed expression patterns of transcripts of two Arabidopsis arginase genes, ARGAH1 and ARGAH2, have not been previously described, and phylogenetic analysis suggests that they diverged independently of duplication events in other lineages. Therefore, we used beta-glucuronidase reporter fusions and quantitative reverse-transcriptase PCR to analyze tissue-specific expression of ARGAH1 and ARGAH2 during Arabidopsis development, and in response to the availability of nutrients and exposure to methyl jasmonate (MeJA). We demonstrated tissue-specific transcript expression and enzyme activity in pollen for ARGAH1, but not ARGAH2. Conversely, we demonstrated MeJA-inducibility of ARGAH2, but not ARGAH1. In addition, we used microarrays to identify genes for which transcript abundance following MeJA treatment differed in wild type and ARGAH2 mutants. These ARGAH2 and MeJA responsive genes included a putative pathogenesis-related protein pathogenesis response-1 (At2g14610), and a gene of unknown function (At5g03090). Interestingly, these genes had opposite responses to the loss of ARGAH2, suggesting multiple downstream effects of arginase activity, following MeJA treatment. These results, and the variety and complexity of expression patterns of ARGAH1 and ARGAH2 transcript expression and their related reporter gene fusions that we observed point to multiple functions of arginase genes in Arabidopsis, some of which have resulted through a sub-functionalization not shared by all angiosperms.
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PMID:Analysis of Arabidopsis arginase gene transcription patterns indicates specific biological functions for recently diverged paralogs. 1842 91

Mutation of either arginase structural gene (ARGAH1 or ARGAH2 encoding arginine [Arg] amidohydrolase-1 and -2, respectively) resulted in increased formation of lateral and adventitious roots in Arabidopsis (Arabidopsis thaliana) seedlings and increased nitric oxide (NO) accumulation and efflux, detected by the fluorogenic traps 3-amino,4-aminomethyl-2',7'-difluorofluorescein diacetate and diamino-rhodamine-4M, respectively. Upon seedling exposure to the synthetic auxin naphthaleneacetic acid, NO accumulation was differentially enhanced in argah1-1 and argah2-1 compared with the wild type. In all genotypes, much 3-amino,4-aminomethyl-2',7'-difluorofluorescein diacetate fluorescence originated from mitochondria. The arginases are both localized to the mitochondrial matrix and closely related. However, their expression levels and patterns differ: ARGAH1 encoded the minor activity, and ARGAH1-driven beta-glucuronidase (GUS) was expressed throughout the seedling; the ARGAH2::GUS expression pattern was more localized. Naphthaleneacetic acid increased seedling lateral root numbers (total lateral roots per primary root) in the mutants to twice the number in the wild type, consistent with increased internal NO leading to enhanced auxin signaling in roots. In agreement, argah1-1 and argah2-1 showed increased expression of the auxin-responsive reporter DR5::GUS in root tips, emerging lateral roots, and hypocotyls. We propose that Arg, or an Arg derivative, is a potential NO source and that reduced arginase activity in the mutants results in greater conversion of Arg to NO, thereby potentiating auxin action in roots. This model is supported by supplemental Arg induction of adventitious roots and increased NO accumulation in argah1-1 and argah2-1 versus the wild type.
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PMID:Arginase-negative mutants of Arabidopsis exhibit increased nitric oxide signaling in root development. 1856 26