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:3.2.1.21 (beta-glucosidase)
3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tumour peracidity in otherwise moderately hyperacidulated tumours or tumour regions of DS carcinosarcoma-bearing Wistar rats attained by glucose infusion was substantially increased by simultaneous infusion of amygdalin and intratumoral i.m. or i.v. application of beta-glucosidase. Here the pH value of healthy tissue, measured at the sceletal muscle, remained unchanged. By means of the said process, tumour hyperacidulation has been raised to a level of deltapH =0.97; attaining a pH difference between tumourous and normal tissue of up to deltapH = 1.6. In one case, the slope of pH reduction in the tumour increased to 870%. Moreover, combined administration of glucose, amygdalin and beta-glucosidase evoked a significant cancerostatic effect hypogenesis, tumour regression) being comparable with the action of an Ifosfamid dosage of 150 mg-kg-1. However, i.m. and i.v. application of beta-glucosidase under narcosis results in an overall process that still remains somewhat too toxic. Hence optimizing studies are intended with the particular aim to further improve the comparability of this process.
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PMID:[Tumour hyperacidulation through intravenous glucose infusion enhanced by amygdalin and beta-glucosidase application (author's transl)]. 0 Sep 79

Six patients with liver metastases from carcinoid or colon carcinoma underwent hepatic derterialization. This operation, known to cause both tumor necrosis and liver cell damage, caused considerable increases of several lysosomal acid hydrolases in the circulation. Thus, beta-glucosidase showed a small temporary increase during the operation, followed by a slower but higher reaction reaching a maximum 12 to 36 hours postoperatively. Similar reactions were noted for beta-glucuronidase, acid phosphatase, beta-galactosidase, arylsuphatase A, and N-acetyl-beta-glucosaminidase while no reactions were found for cathepsin D. Very high enzyme levels occurred in a patient dying from bleeding complications in the postoperative period.
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PMID:Plasma activities of lysosomal enzymes after hepatic dearterialization in man. 0 1

Rats bearing Reuber H-35 or Novikoff hepatomas and mice bearing L1210 or L5178Y murine leukemias exhibited elevated serum levels of fetuin : N-acetylneuraminic acid transferase (EC 2.4.99.1) activity. The serum transferase activity could be correlated with the growth rate of the tumor; in animals bearing the more rapidly growing Novikoff hepatoma, activity was higher than in animals bearing the Reuber H-35 hepatoma. Higher transferase levels were also found in L1210 leukemic mice than in mice with the slightly slower growing L5178Y leukemia. Serum from rats bearing Reuber H-35 hepatoma and mice bearing L1210 murine leukemia had elevated levels of alpha- and beta-glucosidase (EC 3.2.1.20 and EC 3.2.1.21), alpha- and beta-galactosidase (EC 3.2.1.22 and (3.2.1.23), beta mannosidase (EC 3.2.1.25), alpha- and beta-fucosidase (EC 3.2.1.- and EC 3.2.1.38), beta-N-acetylglucosaminidase (EC 3.2.1.30) and acid phosphatase (EC 3.1.3.2); alpha-mannosidase (EC 3.2.1.24), beta-N-acetylgalactosaminidase (EC 3.2.2.-) and beta-xylosidase (EC 3.2.1.37) were not elevated. In animals bearing Reuber H-35 hepatoma, host liver levels of glycosidases, beta-glucuronidase (EC 3.2.1.31) and acid phosphatase were elevated over both the control and the hepatoma values. The data are interpreted to mean that the tumors or various host tissues release large quantities of enzymes into the serum and that enzyme levels in host organs may also be affected by the tumor.
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PMID:Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors. 17 98

Amygdalin MF was evaluated alone and in combination with an activating agent, beta-glucosidase, against three transplantable rodent tumors; Ridgway osteogenic sarcoma, Lewis lung carcinoma, and P388 leukemia. In dose-response studies up to the LD20 in normal mice, amygdalin MF alone did not demonstrate significant antitumor activity against any of these three tumor systems. Similarly, at doses not exceeding the LD10 in normal mice, amygdalin MF plus beta-glucosidase did not demonstrate antitumour activity against any of these three tumor systems. Potentiation of the lethal toxicity of amygdalin MF by beta-glucosidase was observed in all studies where the two agents were given in simultaneous combination.
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PMID:Experimental studies of the antitumor activity of amygdalin MF (NSC-15780) alone and in combination with beta-glucosidase (NSC-128056). 106 May 11

Experiments are described in which four transplantable rodent tumors (L1210 lymphoid leukemia, P388 lymphocytic leukemia, B16 melanoma, and Walker 256 carcinosarcoma) were used to investigate the antitumor activity of amygdalin MF. Amygdalin MF was given alone and in combination with beta-glucosidase which was administered 1/2 hour prior to amygdalin MF, starting 24 hours after tumor implantation. No antitumor activity was observed in any of the four tumor systems tested with the drug alone or in combined therapy. The combined therapy showed potentiation of toxicity with doses of amygdalin MF greater than or equal to 100 mg/kg.
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PMID:Antitumor activity of amygdalin MF (NSC-15780) as a single agent and with beta-glucosidase (NSC-128056) on a spectrum of transplantable rodent tumors. 120 98

Variations of glycoprotein components such as hexose, hexosamine, and sialic acid and lysosomal glycosidases such as beta-D-glucosidase, beta-D-galactosidase, and N-acetyl-beta-D-glucosaminidase were studied in the tumor tissue from various stages of cervical carcinoma of the uterus. Carbohydrate components of glycoprotein were found to be markedly reduced, and the reduction was very much significant in hexosamine and sialic acid in the advanced stages. Lysosomal glycosidases exhibited a significant increase, and among them N-acetyl-beta-D-glucosaminidase exhibited a prominent increase, in the advanced stages of cervical carcinoma of the uterus.
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PMID:Studies on variations of glycoproteins and lysosomal hydrolases in human uterine cervical carcinoma. 144 83

The fecal microflora enzymes, beta-glucuronidase and beta-glucosidase, as well as fecal bacterial counts, were examined during colon carcinogenesis in rats administered parenteral 1,2-dimethylhydrazine and fed nutritionally equivalent diets free of fiber or containing one of three single sources of dietary fiber (cellulose, hemicellulose, and pectin). Whereas pectin-fed animals had increased fecal beta-glucuronidase activities, those fed cellulose and hemicellulose, two fibers protective in dimethylhydrazine colon neoplasia, had decreased activities. Although fecal bacterial counts were not significantly changed, similar differential changes in fecal beta-glucosidase activity were noted: cellulose but not pectin or hemicellulose feeding was associated with reduced activity. Although cellulose fiber may cause differing physiological effects resulting in a reduction in colonic neoplasia development in this experimental animal model, decreased bacterial metabolic enzyme activation of carcinogens or cocarcinogens may lead to diminished exposure of colonic cells to exogenous or endogenous mutagens.
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PMID:Effects of differing purified cellulose, pectin, and hemicellulose fiber diets on fecal enzymes in 1,2-dimethylhydrazine-induced rat colon carcinogenesis. 301 27

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

The H-2Kk glycoprotein has been isolated by monoclonal antibody affinity chromatography, and an analysis of the asparagine-linked oligosaccharides present at the two major glycosylation sites has been performed. Antigen obtained from the AKTB-1b B-cell lymphoma that had been labeled with [2,6-3H]mannose for 5 or 21 h or for 5 h followed by a 5-h chase was digested exhaustively with trypsin. Each glycosylation site was then isolated by reverse phase high performance liquid chromatography using a C18 column. After removal from the peptide backbone by the almond emulsin peptide: N-glycosidase, the oligosaccharides from each isolated site were analyzed by gel filtration, ion exchange chromatography, concanavalin A affinity chromatography, and glycosidase treatment to assess the contribution of sialic acid and branching patterns of the oligosaccharide backbones to the overall microheterogeneity. The glycosylation of the H-2Kk antigen derived from several different AKTB-1b tumor preparations was examined during a period covering 1 year, during which time the tumor was passaged continuously in vivo in 2-week cycles. Our results conclusively demonstrate that the pattern of oligosaccharide microheterogeneity at the two glycosylation sites of the H-2Kk antigen derived from AKTB-1b cells is stable and that each site differs as to the specific array of oligosaccharide types found on the fully processed glycoprotein. In addition, this report describes an analytical scheme employing reverse phase high performance liquid chromatography to follow oligosaccharide processing and hydrolysis of the N-glycosidic bond by the peptide: N-glycosidase.
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PMID:Stable oligosaccharide microheterogeneity at individual glycosylation sites of a murine major histocompatibility antigen derived from a B-cell lymphoma. 660 28

Human tumor cells of neurectoderm origin contain a high proportion of alpha-L-fucosyl linkages were determined by high-resolution, 500-MHz, 1H-n.m.r. spectroscopy which gave signals characteristic for alpha-L-Fucp-(1 leads to 3)-D-GlcNAc residues these L-fucosyl residues. This was shown by use of a specific alpha-L-fucosidase from almond emulsin and a broad-spectrum alpha-L-fucosidase from rat testes. The exact alpha-L-fucosyl linkages were determined by high-resolution, 500-MHz, 1H-n.m.r. spectroscopy which gave signals characteristic for alpha-L-Fucp-(1 leads to 3)-D-GlcNAc residues linked to branches and for alpha-L-Fucp-(1 leads to 6)-D-GlcNAc residues linked to the core. More than 95% of the asparagine-linked GlcNAc residues were substituted with (1 leads to 6)-alpha-L-fucosyl groups. Further definition of the range of neutral glycopeptides was obtained with immobilized lectins. Binding to E-PHA-agarose suggested the presence of a beta-D-mannopyranosyl residue substituted at O-4 by a 2-acetamido-2-deoxy-D-glucopyranosyl group. alpha-L-Fucp-(1 leads to 3)-GlcNAc interfered with this binding since removal of alpha-L-fucosyl groups by almond emulsin alpha-L-fucosidase increased the binding by 100%. These studies demonstrate the ability of a combination of high-resolution 1H-n.m.r., enzyme degradation, and lectin-binding affinities to delineate structural elements of small amounts of oligosaccharide residues.
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PMID:Characterization of the neutral glycopeptides containing the structure alpha-L-fucopyranosyl-(1 leads to 3)-2-acetamido-2-deoxy-D-glucose from human neuroblastoma cells. 662 47


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