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

The ascites form of a chemically induced guinea pig hepatoma, line-10, was resistant to killing in vitro by xenogeneic antibody and guinea pig complement. Pretreatment of line-10 cells with certain proteolytic enzymes rendered tham susceptible to the killing action of antibody and guinea pig complement. The effects of enzyme pretreatment were dependent on enzyme concentration, temperature, and could be blocked by addition of competitive or non-competitive inhibitors. The effect of the enzyme treatment could reversed by incubating the treated cells at 37 degrees C (but not at 0 degrees C), in the absence of the enzyme. Effective enzymes included ficin, bromelain, pronase, elastase, papain, trypsin, collagenase, lipases type I and type VI, and the neuraminidase preparation isolated from Clostridium perfringens. The activity of the lipase preparations and the neuraminidase preparation isolated from Clostridium perfringens appeared to be caused by proteolytic enzyme contamination. Enzyme preparations that proved ineffecitve in rendering the line-10 cells sensitive to killing by antibody and guinea pig complement included DNase, RNase, beta-glucuronidase type 6A or type B10, hyaluronidase type V or type VI, and pectinesterase.
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PMID:Lysis of tumor cells by antibody and complement. VI. Enhanced killing of enzyme-pretreated tumor cells. 17 70

1. Incubation of rabbit tracheal explants with N-[(3)H]acetyl-d-glucosamine and N-acetyl-d-[1-(14)C]glucosamine led to labelling of a number of soluble macromolecular products separable from the medium, after papain digestion, by ion-exchange chromatography. 2. With N-acetyl-d-[1-(14)C]glucosamine in the incubation medium, a neutral glycoprotein, two acidic glycoprotein fractions, hyaluronic acid and a glycosaminoglycan fraction were obtained and all were radioactively labelled. Similar labelling occurred with N-fluoroacetyl-d-[1-(14)C]glucosamine or N-fluoro[(3)H]acetylglucosamine as precursor. 3. Maximal labelling was obtained at 96h after incubation of cultures. N-Fluoroacetyl-glucosamine under these conditions was incorporated into hyaluronate less efficiently than N-acetylglucosamine. 4. With N-fluoroacetyl-d-[1-(14)C]glucosamine as precursor, a hyaluronate component was separated that on enzymic degradation by glycosidases (hyaluronidase, beta-glucuronidase and N-acetyl-beta-hexosaminidase) yielded a (14)C-labelled oligosaccharide fraction together with N-acetyl-d-[1-(14)C]glucosamine and N-fluoroacetyl-d-[1-(14)C]glucosamine, consistent with some exchange of N-acetyl groups having occurred. 5. The results on enzymic degradation of labelled macromolecules by glycosidases suggest that the presence of incorporated N-fluoroacetyl side chains may render the hyaluronate analogue more resistant to hyaluronidase.
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PMID:Incorporation of N-fluoroacetyl-D-glucosamine into hyaluronate by rabbit tracheal explants in organ culture. 51 60

In an effort to determine the mechanism of papain action in causing an emphysema-like lesion in hamsters, the number and types of cells and the activities of two lysosomal enzymes in the lung were determined after papain exposure. Three and four weeks after a 3-h exposure to an aerosol of 3% papain the following alterations in lung structure and function were observed: (1) the mean linear intercept, or average distance between adjacent alveoli, was increased; (2) the internal surface area declined; (3) the dynamic compliance was elevated at low breathing frequencies. The numbers of cells present free in the lung increased from a control value of 2.0 +/- 0.2 x 10 (6) to 6.6 +/- 0.5 x 10 (6) 5 days after exposure. The free beta-glucuronidase, alysosomal enzyme, likewise increased over threefold during the first 3 days after exposure. These results are consistent with the hypothesis that papain induces an inflammatory-type responses, and this may be in part responsible for inducing the lesion.
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PMID:Pathogenesis of papain-induced emphysema in the hamster. 68 Sep 50

Chronic exposure of rats to 10% aerosols of papain or trypsin resulted in marked increases in lung weights and lung beta-glucuronidase and arylsulfatase activities. Destruction of alveolar walls was demonstrated microscopically as a decrease in the number of air spaces touching a line of known length. The pregnenes, progesterone and medroxyprogesterone acetate, but not the 19-nortestosterone derivative norethindrone, partially prevented the papain-induced breakdown of alveolar septa and elevation of beta-glucuronidase. The steroidal anti-inflammatory agent, paramethasone, completely inhibited the rise in lung weight and beta-glucuronidase activity, but did not prevent destruction of alveolar walls. The non-steroidal anti-inflammatory agent, indomethacin, afforded little or no protection. Limited prophylaxis against both histological and enzymatic changes was observed in rats treated with the anti-metabolite, cyclophosphamide, and the proteolytic enzyme inhibitor, aprotinin. The various lung abnormalities resulting from papain inhalation may thus be individually influenced by specific pharmacologic agents.
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PMID:Lung enzymes in emphysematous rats: effects of progestagens, antiphlogistics and metabolic inhibitors. 116 8

We have developed a radioiodinated photoaffinity label, N-formyl-Nle-Leu-Phe-Nle-125I-Tyr-Lys-N-6-(4'-azido-2'-nitrophenylamino) hexanoate (where Nle represents norleucine) (125I-PAL), which forms a covalent complex with the formyl peptide chemotactic receptor of living human neutrophils. Labeling was 12 to 16% efficient and did not alter cell viability. The receptor on live neutrophils and neutrophil membranes has an apparent molecular weight of 50,000 to 70,000 by sodium dodecyl sulfate-polyacrylamide electrophoresis. The receptor on intact cells possesses one predominant papain cleavage site, yielding a 35,000-Da fragment. This receptor fragment retains an affinity for N-formyl-Nle-Leu-Phe-Nle-125I-Tyr-Lys indistinguishable from the receptor on control cells (KD = 1.9 and 1.8 nM, respectively). The 35,000-Da papain fragment was biologically active as evidenced by an unchanged dose-response curve for peptide-stimulated beta-glucuronidase release and fluorescent peptide uptake. Papain treatment of 125I-PAL-labeled neutrophil membranes or of digitonin-soluble 125I-PAL-labeled receptors produced a predominant 28,000-Da fragment without evidence of the 35,000-Da fragment seen with whole cells. Pronase, which did not cleave the receptor on intact cells, produced multiple receptor fragments when used to treat 125I-PAL-labeled membranes.
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PMID:Formyl peptide chemotactic receptor. Evidence for an active proteolytic fragment. 630 46

XCP1 is a xylem-specific papain-like cysteine peptidase in Arabidopsis. To determine whether XCP1 could be involved in tracheary element autolysis, promoter activity and localization of XCP1 were investigated using XCP1 promoter-beta-glucuronidase fusions and immunofluorescence confocal microscopy. A tracheary element expression pattern was detected for XCP1. Results from confocal microscopy and biochemical subcellular fractionation indicated that XCP1 was localized in the vacuole. Ectopic expression of XCP1 resulted in a reduction in plant size in some lines and early leaf senescence, as indicated by early loss of leaf chlorophyll. Reduced plant size was correlated with higher levels of XCP1, as shown by immunoblot and peptidase activity gel analyses. The XCP1 prodomain exhibits exceptionally high similarity (greater than 80%) to the prodomains of papain and other papain-like enzymes isolated from papaya (Carica papaya) laticifers when compared with all other reported papain-like enzymes. The potential for XCP1 and papain to perform common functions as catalysts of autolytic processing following cell death due to programmed suicide or to wounding is discussed.
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PMID:The Arabidopsis xylem peptidase XCP1 is a tracheary element vacuolar protein that may be a papain ortholog. 1178 55

A method using polymerase chain reaction (PCR) was developed to detect the genetically modified (GM) papaya (55-1 line), of which the mandatory safety assessment has not been finished in Japan because of insufficient data. The papaya intrinsic papain gene was used as an internal control. The results of PCR amplification of the papain gene segment indicated that a commercial silica membrane type kit (QIAGEN DNeasy plant mini) was useful for extraction of DNA from papaya fruit, but not for extraction from canned papaya fruit. On the other hand, a commercial ion-exchange type kit (QIAGEN Genomic-tip) provided enough purified DNA for PCR from canned papaya fruit. Compared with the parental line and other commercial non-GM papayas, the DNA from GM papaya fruit provided specific amplification bands in PCR with five primer pairs (Nos. 2-6) including beta-glucuronidase and neomycin phosphotransferase II gene-specific ones. On the other hand, the primer pairs recognizing these genes showed false-positive results when we used DNAs from canned papaya. Therefore, we recommend that the primer pairs (Nos. 5 and 6) recognizing the sequences derived from two different species of organism should be used in order to detect specifically the GM papaya in canned fruits.
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PMID:[Detection of recombinant DNA from genetically modified papaya]. 1181 37