Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 activity and distribution of acid phosphatase, alkaline phosphatase, nonspecific esterases, beta-glucuronidase, and aminopeptidase were examined in the transplantable R-3327 rat prostatic adenocarcinoma and compared with those in the four prostatic lobes of the rat. Both the well and poorly differentiated tumor cells in R-3327 carcinoma were characterized by high activities of beta-glucuronidase and aminopeptidase. The poorly differentiated cells had a high alkaline phosphatase activity. The enzymatic profile of the R-3327 adenocarcinoma closely resembled that of the anterior and dorsal prostate. The origin of the tumor in one of these prostatic lobes is probable, but not certain.
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PMID:Enzyme activity and distribution in rat prostatic adenocarcinoma. 63 35

Activities of the lysosomal enzymes, cathepsin B1 (CBI), beta-glucuronidase, and beta-N-acetyl-D-glucosaminidase, as well as sialyl transferase, alkaline phosphatase, and placenta-like alkaline phosphatase, were determined on blind-coded serums from 99 women exposed to diethylstilbestrol (DES) in utero and 40 unexposed subjects of comparable age range. Cathepsin B1 averaged 100%, 1040% (P less than 0.001), 2720 % (P less than 0.001), and 4760% (P less than 0.001) of controls in DES-exposed women with no genital tract abnormalities (N = 11), adenosis (N = 68), adenosis with concomitant dysplasia (N = 15), and clear-cell adenocarcinoma (N = 5), respectively. The later two groups also exhibited 0.01). Activities of the other four enzymes in serums of DES-exposed women were unchanged from those controls, suggesting that alterations in CBI were not due to generalized increases in lysosomal membrane instability or other gross cellular damage. In 2 DES-exposed women with clear-cell adenocardinoma, from whom serial samples were available, preoperative levels of serum CBl fell from a mean of 4280% to values indistinguishable from controls by 7--12 days after tumor excision, concurrently with objective signs of remission. Recrudescence of serum CBI levels preceded by at least 3 months clinical evidence of persistent adenosis accompanied by vaginal dysplasia. Although the nature of the increments in CBI-like activity in the majority of subjects with DES-related pathology remains to be determined, the findings may complement present methods of physical diagnosis and prognosis.
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PMID:Elevated serum cathepsin B1 and vaginal pathology after prenatal DES exposure. 70 88

In the human adenocarcinoma cell line Caco-2 a substantial amount of a precursor form of the lysosomal enzyme alpha-glucosidase is not segregated into lysosomes, but instead secreted from the apical membrane. In this study we addressed the question whether this process is mediated by mannose 6-phosphate receptors. The subcellular distribution of the cation-independent mannose 6-phosphate receptor was studied by means of electron microscopic immunocytochemistry. The bulk of label was found in the perinuclear region in electron-lucent and dense vesicles, some of the latter bearing a coat. Receptor-containing dense vesicles were also found throughout the cytoplasm. In the apical part of the cells, label for the receptor was present over the surrounding membrane and the interior vesicles of multivesicular bodies, but not over lysosomes. Label on the plasma membrane was mainly restricted to the apical domain. In contrast to alpha-glucosidase, the secreted forms of the lysosomal enzymes cathepsin D, beta-hexosaminidase and beta-glucuronidase are mainly found in the basolateral medium. Enzyme activity measurements and immunoprecipitation of metabolically labeled cells showed that incubation with NH4Cl leads to an enhanced secretion of these enzymes into the basolateral medium, but has no effect on the basolateral secretion of alpha-glucosidase. In addition, NH4Cl caused a minor decrease in the secretion of these enzymes from the apical side and had little or no effect on the secretion of alpha-glucosidase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The cation-independent mannose 6-phosphate receptor is not involved in the polarized secretion of lysosomal alpha-glucosidase from Caco-2 cells. 132 37

Since human colorectal tumors are insensitive to most chemotherapeutic agents, there is a need for the discovery of new drugs that would show activity against this disease. In an attempt to better appreciate the relevance of a widely used mouse colon tumor (colon adenocarcinoma Co38) as a screening model for human colorectal tumors, we compared the main phase I and phase II drug-metabolizing enzyme systems in both tumoral and nontumoral colon tissues. The following enzymes were assayed by Western blot: cytochromes P-450 (1A1/A2, 2B1/B2, 2C, 2E1, and 3A), epoxide hydrolase, and glutathione-S-transferases (GST-alpha, -mu, and -pi). The activities of the following enzymes or cofactors were determined by spectrophotometric or fluorometric assays: total cytochrome P-450, 1-chloro-2,4-dinitrobenzene-GST, selenium-independent glutathione peroxidase, 3,4-dichloronitrobenzene-GST, ethacrynic acid-GST, total glutathione, epoxide hydrolase, UDP-glucuronosyltransferase, beta-glucuronidase, sulfotransferase, and sulfatase. Results obtained by Western blot showed that mouse colon adenocarcinoma Co38 did not express any of the probed cytochromes P-450, whereas human colorectal tumors expressed only low levels of cytochrome P-450 3A. GST-alpha and GST-pi were detected in all tumoral and nontumoral tissues of both species. The neutral GST-mu was expressed in all murine tissues investigated and was found to be polymorphic in human tissues. For human peritumoral and tumoral colorectal tissues there was no significant difference between GST isoenzyme levels, whereas mouse colon adenocarcinoma Co38 had a lower expression of GST-mu and GST-pi, compared to normal mouse colon. Enzymatic activities for glutathione peroxidase, 3,4-dichloronitrobenzene-GST, and ethacrynic acid-GST confirmed the Western blot results for GST-alpha, GST-mu, and GST-pi, respectively. Total GSH levels were similar between murine and human tumors but were 3-fold higher in human tumors than in peritumoral tissues, whereas they were 7-fold lower in mouse colon tumor Co38, compared to normal mouse colon. Epoxide hydrolase was not expressed in either mouse colon adenocarcinoma Co38 or normal mouse colon tissues, whereas it was expressed in human colon peritumoral and tumoral tissues at similar levels. No significant difference was observed between human tumors and peritumoral tissues for UDP-glucuronosyltransferase, beta-glucuronidase, sulfotransferase, and sulfatase. For murine colon tissues, the conjugation pathways (UDP-glucuronosyltransferase and sulfotransferase) were lower in colon adenocarcinoma Co38, whereas the converse was observed for the corresponding hydrolytic enzymes (beta-glucuronidase and sulfatase).(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Comparison of mouse and human colon tumors with regard to phase I and phase II drug-metabolizing enzyme systems. 142 2

The specificity and sensitivity of the assay for beta-glucuronidase in cerebrospinal fluid were evaluated to determine the usefulness of this test for the detection of neoplastic meningitis. The enzyme activity was first measured in cerebrospinal fluid from 131 patients with various disorders and was then prospectively measured in cerebrospinal fluid from 30 patients with cytologic results that were positive for or suggestive of malignant disease. Within the first group, elevated levels of beta-glucuronidase were found only among patients with neoplastic processes in the central nervous system, including neoplastic meningitis. Among 26 patients with neoplastic processes in the central nervous system, including neoplastic meningitis. Among 26 patients with positive cytologic results, 13 had elevated beta-glucuronidase activities. Elevated values were more frequent among patients with adenocarcinoma (75%) and myelogenous leukemia (60%). The patients with these two disorders also had the highest enzyme activities. The correlation of th beta-glucuronidase level with other cerebrospinal fluid values, including total protein, glucose content, and cell count, was not significant. The findings of this study indicate that measurement of beta-glucuronidase in cerebrospinal fluid can be used as an adjunctive diagnostic test for neoplastic meningitis. The results should be interpreted with caution, however, because of the possibility that the elevated enzyme levels may be due to acute or subacute bacterial or fungal meningitis.
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PMID:Assay for beta-glucuronidase in cerebrospinal fluid: usefulness for the detection of neoplastic meningitis. 399 Mar 76

The activities of six glycosidases in a rat colorectal adenocarcinoma were measured and compared with those of normal colonic mucosa. The specific activities of beta-galactosidase (EC 3.2.1.23) and beta-glucuronidase (EC 3.2.1.31) in the adenocarcinoma were similar to those of the corresponding ones in the normal mucosa, whereas those of beta-N-acetylglucosaminidase (EC 3.2.1.30), alpha-L-fucosidase (EC 3.2.1.51), alpha-galactosidase (EC 3.2.1.22) and beta-glucosidase (EC 3.2.1.21) were reduced in the former as compared with those in the latter. In the case of alpha-L-fucosidase, two forms were newly detected in the tumor. The relative abundance of three forms of beta-N-acetylglucosaminidase was quite different between the adenocarcinoma and the normal mucosa, and the level of the intermediate form in the tumor was markedly reduced. However, thermostability and Km values of two forms A and B in the tumor were not different from those of the corresponding ones in the normal tissue.
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PMID:Alteration in glycosidases from well-differentiated colorectal adenocarcinoma of rat. 404 71

beta-Glucuronidase from human maxillary sinus and lung cancers and from uninvolved tissues was studied. An elevation of beta-glucuronidase activity was observed in cancerous tissues as compared with the corresponding uninvolved tissues, and this increase was significant in adenocarcinoma and squamous cell carcinoma of the lung (p less than 0.01). beta-glucuronidase preparations purified from adenocarcinoma and large cell carcinoma of lung and from normal lung showed similar kinetic properties and antigenicity. beta-Glucuronidase from lung adenocarcinoma showed considerable negative charge heterogeneity in the pI range from 4.2 to 6.2 in an experiment involving isoelectric focusing on polyacrylamide gel. Similar charge heterogeneity was observed in the enzyme from lung large cell carcinoma. Upon treatment of the adenocarcinoma enzyme with exogenous alkaline phosphatase or endoglycosidase H, the heterogeneous variant forms of the tumor enzyme appeared to partly or completely lose their negative charge and to be converted into forms similar to those of the normal lung enzyme. An experiment on the labeling of beta-glucuronidase with [32P]-phosphoric acid provided further evidence that the acidic variants found in lung cancers are extensively phosphorylated forms of the enzyme.
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PMID:[beta-Glucuronidase in human maxillary sinus and lung cancers: elevation of activity level and appearance of phosphorylated variant forms]. 609 43

beta-Glucuronidase from human lung neoplasms of various histological types and from uninvolved tissues was studied. A significant elevation of beta-glucuronidase activity was observed in adenocarcinoma and squamous cell carcinoma of the lung as compared with the corresponding uninvolved tissues (P less than 0.01). Saccharo-1,4-lactone, a strong inhibitor of the enzyme, exhibited a substantially greater stabilizing effect on the adenocarcinoma enzyme than on the other enzymes. However, removal of the carbohydrate moiety from the adenocarcinoma enzyme by treatment with endo-beta-N-acetylglucosamidase H (endoglycosidase H) brought about a decrease in the stabilizing effect. Tumor beta-glucuronidase showed considerable negative charge heterogeneity in the pI range from 4.2 to 6.2 in isoelectric focusing on polyacrylamide gel. Upon treatment with exogenous alkaline phosphatase or endoglycosidase H, the heterogenous variant forms of the tumor enzyme appeared to partly or completely lose their negative charge and to be converted into forms similar to those of the normal lung enzyme. These data strongly suggest that the variants are highly phosphorylated on the oligosaccharide chains of the enzyme. An experiment on the labelling of beta-glucuronidase with [32P]-phosphoric acid provided further evidence that the acidic variants found in lung cancers are extensively phosphorylated forms of the enzyme.
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PMID:Cancer-associated alteration of beta-glucuronidase in human lung cancer: elevated activity and increased phosphorylation. 643 19

A case of adenocarcinoma of Bartholin's glands in a middle aged female is presented. This well known, but rather uncommon malignancy is reported since it shows an unusual structure consisting of a combination of two different histological entities, namely an adeno-cystic component and adenopapillary component. An interval of 21 years elapsed between the appearance of the primary lesion and the recurrence which showed extensive haematogenous and lymphogenous metastases and proved fatal within two years of the recurrence. The study includes an enzyme histochemical evaluation and a fine needle cytological examination. The former revealed a high degree of activity of the NADP+ regenerating enzymes of the pentose shunt as well as a definite, but variable, activity of many lysosomal enzymes, mainly non specific esterases, acid phosphatase, aryl sulphatase and beta-glucuronidase. In contrast to other adenocarcinomas arising in the female genital tract, especially those of endometrium and ovary, the tumour cells showed only a slight activity of alkaline phosphatase, As is the case in many other adenocarcinomas, the activity of lactate dehydrogenase was strongly evident.
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PMID:Histochemical and cytochemical studies of metastasizing carcinoma of Bartholin's gland. 645 95

Renal tissue sections from 178 patients, whose kidneys were either normal or altered by various conditions such as hydronephrosis, interstitial nephropathies, chronic graft rejection, renal cancer etc., were investigated by computer-assisted histophotometry. We used enzyme histochemical and immunologic methods to measure kidneys suffering from various urological diseases quantitatively. Through this procedure, we were able to obtain information that allowed us to determine the degree of alteration in the metabolic state of tubular epithelial cells. The tissue activities of the following enzymes of the proximal tubule were investigated: alanine aminopeptidase (AAP), alkaline phosphatase (AP) and maltase (Ma) as membrane-bound markers, and beta-glucuronidase (beta-Gl) as a lysosomal marker. In addition, AAP and gamma-glutamyltranspeptidase (GGTP) were measured by immunofluorescent microscopy after having added specific anti-enzyme antibodies to the tissue sections. Compared to normal kidneys, quantitative enzyme histograms of diseased kidneys revealed a significant decrease in marker protein concentration of the tubule. The decline in tissue enzyme activities of AP, AAP, Ma and beta-Gl was accompanied by a significant decrease of enzyme concentrations as measured by the immuno histological method. This was especially true in cases with kidney cancer and in kidney tissues adjacent to infiltration adenocarcinoma. Morphological analyses of alterations were generally improved by enzymatic and/or immunologic histophotometry.
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PMID:Quantitative enzymatic and immunologic computer-assisted histophotometry of human kidney tissue following neoplastic and other clinically significant alterations. 687 27


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