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PubMed1983

Genetic control of levels of murine kidney glucuronidase mRNA in response to androgen.

A cis-acting genetic element, designated Gus-r, regulates the androgen-induced rates of murine glucuronidase (EC 3.2.1.31) synthesis in kidney tubule cells and is tightly linked to the glucuronidase structural gene, Gus-s. To investigate the molecular mechanism underlying this regulation, we have cloned a glucuronidase-specific cDNA sequence in plasmid pBR322. This cloned DNA has been utilized as a probe in blot hybridization analyses to determine whether the control of androgen responsiveness of kidney glucuronidase synthesis by Gus-r is exerted over the level or the translatability of glucuronidase mRNA. Three important observations emerged from these studies: (i) glucuronidase mRNA exists as a single size class of approximately 2,800 nucleotides; (ii) androgen stimulation of glucuronidase synthesis is directly related to the level of glucuronidase mRNA; and (iii) strain differences in levels of kidney glucuronidase mRNA accumulated in response to androgen are controlled by alleles of Gus-r. Thus, Gus-r regulates the androgen responsiveness of glucuronidase synthesis by controlling the amount of glucuronidase mRNA available for translation and is a cis-acting genetic element that regulates the hormonal responsiveness of a specific mRNA.

Alleles↗
PubMed1999

Relationship of beta-glucuronidase to differentiation and invasion of human colorectal carcinoma.

OBJECTIVE: To investigate the relationship between beta-glucuronidase and tumor differentiation and invasion in human colorectal carcinoma. METHODS: The expression of beta-glucuronidase in human colorectal carcinoma tissue was determined by streptavidin-peroxidase immunohistochemical method. Four human colorectal carcinoma cell lines were analysed for beta-glucuronidase in the medium by spectrophotometry method. RESULTS: Compared with well differentiated colorectal carcinomas, beta-glucuronidase expression was higher in poorly differentiated tumors. An association was found between beta-glucuronidase overexpression in colorectal carcinoma and more advanced tumor Dukes' stage (P < 0.05). With increasing maximum depth of invasion, tumors more frequently show higher beta-glucuronidase expression (P < 0.05). The analysis of colorectal carcinoma cell lines for beta-glucuronidase showed that low levels of beta-glucuronidase (activity range, 1.29 to 1.96 micrograms/10(6) cells per hour) were associated with the well differentiated cell lines which have low invasiveness (CX1, CCL187), and this was in contrast to the elevated level of the enzyme (2.46 to 2.73 micrograms/10(6) cells per hour) present in the medium derived from the poorly differentiated cells with high invasiveness (CCLI227, CCL228) (P < 0.05). CONCLUSIONS: Poorly differentiated human colorectal carcinoma cells could synthesize more beta-glucuronidase, enhance local invasion. Immunohistochemical staining for beta-glucuronidase might be helpful to diagnosing the differentiation degree and invasiveness of human colorectal carcinomas, and the secreted beta-glucuronidase might provide a useful measurement of the differentiation degree and invasiveness of cultured human colorectal carcinoma cells.

Adult↗
PubMed1989

Involvement of the carboxyl-terminal propeptide of beta-glucuronidase in its compartmentalization within the endoplasmic reticulum as determined by a synthetic peptide approach.

The proenzyme form of beta-glucuronidase is compartmentalized in large quantities within the endoplasmic reticulum by binding to the esterase, egasyn. Also, the propeptide of the proenzyme form of beta-glucuronidase is likely located at the carboxyl terminus. We have, therefore, tested if this carboxyl-terminal peptide is important in binding to egasyn. A polyclonal antibody to a 30-mer synthetic peptide, corresponding to the carboxyl-terminal 30 amino acids of pro-beta-glucuronidase, provided evidence that egasyn binds to the carboxyl terminus of beta-glucuronidase. This antibody interacted with proenzyme beta-glucuronidase-egasyn complexes in which one, two, or three egasyn molecules were bound to the beta-glucuronidase tetramer, but not with those complexes (M4) which contained four egasyn molecules. We interpret these results as indicating that all available carboxyl termini of the beta-glucuronidase proenzyme tetramer are shielded by egasyn in the M4 complexes. The same antibody did not recognize the mature lysosomal form of beta-glucuronidase, indicating that only the proenzyme form of microsomal beta-glucuronidase contains the original carboxyl terminus. Also, the synthetic 30-mer was found to be a specific and potent inhibitor (50% inhibition at 1.3 microM) of the esterase activity of purified egasyn but exhibited little inhibitory activity toward other purified esterases including a rat trifluoroacetylated esterase or egasyn esterase from another species. Together, these data describe a potent interaction of the exposed carboxyl terminus of precursor glucuronidase with the esterase catalytic site of egasyn, which in turn results in the specific localization of glucuronidase within the lumen of the endoplasmic reticulum.

Amino Acid Sequence↗
PubMed1977

Effects of di-isopropyl phosphorofluoridate on rat liver microsomal and lysosomal beta-glucuronidase.

iPr(2)P-F (di-isopropyl phosphorofluoridate) administration to rats produces a liver-dependent specific elevation of plasma beta-glucuronidase activity. The response is unaffected by puromycin pretreatment. By using subcellular-fractionation techniques, the rise in plasma beta-glucuronidase activity was correlated temporally with a fall in liver microsomal beta-glucuronidase activity. After iPr(2)P-F treatment, liver microsomal membranes are depleted of beta-glucuronidase but slowly return to normal over 1 week. On the other hand, liver lysosomal beta-glucuronidase activity is high at early time points (less than 60min) after iPr(2)P-F administration but decreases to below control values; this lasts for a few days. The response to iPr(2)P-F was demonstrated in isolated hepatocytes prepared from iPr(2)P-F-treated rats. In such preparations, microsomal beta-glucuronidase is lost rapidly, followed by a specific decrease in hepatocyte lysosomal beta-glucuronidase. The results suggest that a pool of microsomal beta-glucuronidase serves as precursor to plasma beta-glucuronidase in iPr(2)P-F-treated rats, and further, that microsomal beta-glucuronidase may serve as precursor to lysosomal beta-glucuronidase.

Journal Article↗
PubMed1987

Abnormal subcellular distribution of beta-glucuronidase in mice with a genetic alteration in enzyme structure.

Liver beta-glucuronidase is structurally altered in inbred strain PAC so that a peptide subunit with a more basic isoelectric point, GUS-SN, is produced. This allele of beta-glucuronidase was transferred to strain C57BL/6J by 12 backcross matings to form the congenic line B6 X PAC-Gus(n). Liver beta-glucuronidase activity was halved in males of the congenic strain compared to normal males. The lowered activity was specifically accounted for by a decrease in the lysosomal component. There was no alteration in the concentration of microsomal activity. This alteration in the subcellular distribution of beta-glucuronidase in Gus(n)/Gus(n) mice was confirmed by two independent gel electrophoretic systems which separate microsomal and lysosomal components. beta-Glucuronidase activity was likewise approximately halved in mutant spleen, lung, and brain, organs which contain exclusively or predominantly lysosomal beta-glucuronidase. The loss of liver lysosomal beta-glucuronidase activity was shown by immunotitration to be due to a decrease in the number of beta-glucuronidase molecules in lysosomes of the congenic strain. The Gus(n) structural alteration likely causes the lowered lysosomal beta-glucuronidase activity since the two traits remain in congenic animals. Heterozygous Gus(n)/Gus(b) animals had intermediate levels of liver beta-glucuronidase. Also, the effect was specific, in that three other lysosomal enzymes were not reproducibly lower in Gus(n)/Gus(n) mice. Gus(n) is, therefore, an unusual example of a mutation which causes a change in the subcellular distribution of a two-site enzyme.

Animals↗
PubMed2006

Novel carbohydrate-binding activity of bovine liver beta-glucuronidase toward lactose/N-acetyllactosamine sequences.

Beta-glucuronidase is a lysosomal enzyme that plays an essential role in normal turnover of glycosaminoglycans and remodeling of the extracellular matrix components in both physiological and inflammatory states. The regulation mechanisms of enzyme activity and protein targeting of beta-glucuronidase have implications for the development of a variety of therapeutics. In this study, the effectiveness of various carbohydrate-immobilized adsorbents for the isolation of bovine liver beta-glucuronidase (BLG) from other glycosidases was tested. Beta-glucuronidase and contaminating glycosidases in commercial BLG preparations bound to and were coeluted from adsorbents immobilized with the substrate or an inhibitor of beta-glucuronidase, whereas beta-glucuronidase was found to bind exclusively with lactamyl-Sepharose among the adsorbents tested and to be effectively separated from other enzymes. Binding and elution studies demonstrated that the interaction of beta-glucuronidase with lactamyl-Sepharose is pH dependent and carbohydrate specific. BLG was purified to homogeneity by lactamyl affinity chromatography and subsequent anion-exchange high-performance liquid chromatography (HPLC). Lactose was found to activate beta-glucuronidase noncompetitively, indicating that the lactose-binding site is different from the substrate-binding site. Binding studies with biotinyl glycoproteins, lipids, and synthetic sugar probes revealed that beta-glucuronidase binds to N-acetyllactosamine/lactose-containing glycoconjugates at neutral pH. The results indicated the presence of N-acetyllactosamine/lactose-binding activity in BLG and provided an effective purification method utilizing the novel carbohydrate binding activity. The biological significance of the carbohydrate-specific interaction of beta-glucuronidase, which is different from the substrate recognition, is discussed.

Amino Sugars↗