Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
 ...
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

The chemical synthesis of swainsonine [(1S,2R,8R,8 alpha R)-trihydroxyindolizidine] from trans-1,4-dichloro-2-butene was previously described [Adams, C. E., Walker, F. J., & Sharpless, K. B. (1985) J. Org. Chem. 50, 420-424]. A modification of that synthesis provided two other isomers, referred to here as "Glc-swainsonine" [(1S,2S,8R,8 alpha R)-trihydroxyindolizidine] and "Ido-swainsonine" [(1S,2S,8S,8 alpha R)-trihydroxyindolizidine]. To determine whether these new compounds had biological activity, they were compared to swainsonine as inhibitors of a number of commercially available glycosidases. While swainsonine is a potent inhibitor of jack bean alpha-mannosidase but does not inhibit other glycosidases, its two isomers were inactive on alpha-mannosidase but did inhibit other enzymes. Thus, Glc-swainsonine was an inhibitor of the fungal alpha-glucosidase amyloglucosidase, and this inhibition was of a competitive nature (Ki = 5 X 10(-5) M) with respect to the substrate p-nitrophenyl alpha-D-glucopyranoside. This alkaloid also inhibited beta-glucosidase, but much less effectively than alpha-glucosidase. On the other hand, Ido-swainsonine was more effective toward beta-glucosidase than toward alpha-glucosidase, and this inhibition was also of a competitive nature. None of these inhibitors were effective against beta-mannosidase or alpha- or beta-galactosidase. Glc-swainsonine was also tested against the glycoprotein processing glycosidases. Surprisingly, in this respect, the alkaloid was like swainsonine in that it inhibited mannosidase II but had no effect or only slight effect on glucosidase I, glucosidase II, and mannosidase I. Glc-swainsonine also inhibited glycoprotein processing in cell culture.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Effect of isomers of swainsonine on glycosidase activity and glycoprotein processing. 311 29

The antitumor activity of a glucuronide of 5-fluorouracil, methyl (5-fluoro-1H-2-oxo-4-pyrimidinyl beta-D-glucopyranosid) uronate (FU-O-G), which is a 5-fluorouracil (5-FU) derivative with remarkably low toxicity, was studied. The antitumor activity of this compound was superior to those of 5-FU and 1-(2-tetrahydrofuryl)-5-fluorouracil (Tegafur, Ftorafur) in the treatment of transplantable tumors, not only 5-FU-sensitive tumors such as adenocarcinoma 755, lymphosarcoma LS-1, and plasmacytoma X5563, but also 5-FU-resistant tumors such as Lewis lung carcinoma and Walker carcinosarcoma 256. Furthermore, in the treatment of Lewis lung carcinoma, which responds poorly to 5-FU and Ftorafur, daily administration of FU-O-G at a dose of 400 mg/kg for 30 days produced a 92% increase in life span without marked loss of body weight, though short-term administration (such as 5 days) was barely effective. Thus, it appears that FU-O-G is an antitumor agent suitable for long-term administration. These findings correspond with the results of an enzymological study which showed selective activation of FU-O-G by beta-glucosidase in tumor cells and indicated that the compound is a marked form of 5-FU.
 ...
PMID:Antitumor activity of methyl (5-fluoro-1H-2-oxo-4-pyrimidinyl beta-D-glucopyranosid)uronate against various experimental tumors. 679 41

The study of digestive enzymes, especially in important pests like Chilo suppressalis Walker (Lepidoptera: Pyralidae), which are a key constraint on rice production in a wide area of the globe and also in Iran, could be a successful procedure in the development of a safe and useful control strategy. Glycosidase are a type of digestive enzymes which have a critical role in the final stages of carbohydrate digestion; they hydrolyze alpha-D-(1,4)-glucose linkage such as p-nitrophenyl-alpha-D-glucoside in di and oligosaccharide components. Laboratory reared 4th instar larvae were randomly selected; midgut and salivary gland were removed by dissection under a stereo microscope and glucosidase activities were assayed by Ferreira and Terra's procedures. The activities of alpha- and beta-glucosidase in the midgut and salivary gland were 0.009, 0.0063, 0.005 and 0.003 micromol/min/mg protein, respectively. The optimal pH and temperature for enzyme activity were determined to be 9 and 45 degrees C for the glucosidases measured, values which are in agreement with other reports, especially in lepidopteran insects, which give values between 8-12 and 20-50 degrees C. The enzyme activity increased with the addition of NaCl, MgCl(2) and CaCl(2) and decreased due to the use of different concentrations of KCl, Urea, EDTA, SDS and Urea both in midgut and the salivary glands. Control of pests by using resistant varieties is one of the most important practices that are dependent on inhibitors in plants. Hence, characterization of digestive enzymes, especially the effect of inhibitors on enzyme activity, could be useful, on the one hand for a better understanding of enzyme roles in the nutrition physiology of insects, and on the other hand to reach safe and useful controls of insect pests.
 ...
PMID:Enzymatic properties of alpha- and beta-glocusidases extracted from midgut and salivary glands of rice striped stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae). 1952 3