Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The JCR:LA-cp rat is one of a number of strains that carry the mutant autosomal recessive cp gene. Animals, of all strains, that are homozygous, for the gene (cp/cp) become obese, insulin resistant, and hypertriglyceridemic. Heterozygotes or homozygous normal rats (+/+) are lean and metabolically normal. The JCR:LA-cp rat is unique in the development of a frank vasculopathy with atherosclerotic lesions and associated ischemic myocardial lesions. The cardiovascular disease is strongly correlated with the hyperinsulinemia, which develops as the animals mature from 4 to 8 weeks of age. The hyperinsulinemia can be decreased by marked food restriction, ethanol consumption, or reduction of the postprandial glucose and insulin responses through the use of alpha-glucosidase inhibitors. Any treatment that reduces plasma insulin levels is associated with a reduction in cardiovascular disease. In contrast, a reduction in plasma triglyceride concentrations, alone, has no effect on end-stage lesions. JCR:LA-cp rats, particularly those that are cp/cp, are, however, sensitive to cholesterol in the diet, unlike other strains that are highly resistant. Further, the rats have abnormal vascular smooth muscle cells that, especially in the cp/cp animals, are hyperplastic and activated and migrate into the intimal space. Our findings suggest that susceptibility to cardiovascular disease requires hypermsulinemic stress coupled with excessive dietary intake and the presence of one or more other necessary, but not sufficient, genetic factors. One of these may be a genetic abnormality of vascular smooth muscle cells. A similar situation may occur in humans.
Mol Cell Biochem 1998 Nov
PMID:Cardiovascular disease in the JCR:LA-cp rat. 982 17

Suidatrestin, isolated from a Streptomyces strain, was characterized as a new trehalase inhibitor. Its inhibitory potential was 7 to 50-fold higher than that of validamycin when tested against insect, fungal and mammalian trehalases. The kinetic properties of suidatrestin were studied in vitro with trehalases from flight muscle mitochondria of the fly, Protophormia terraenovae, from larval midgut of the moth, Spodoptera littoralis, and from porcine kidney, as well as with maltase from yeast. Suidatrestin was inactive on maltase but inhibited all trehalases with IC50 values of 0.08-0.1 microM; Ki values ranged from 0.02 to 0.05 microM. The very low Ki/K(m) ratios (3.9 x 10(-6) -4.9 x 10(-6)) indicated excellent in vitro inhibitory action of suidatrestin. When injected into larvae of S. littoralis, suidatrestin required high and repetitive doses which lead to reversible inhibition of larval growth only. Consecutive omission of the inhibitor even stimulated weight increase above that of controls. Significant mortality was achieved at a rather high dose only. Injection of a growth-inhibiting dose of suidatrestin did not change hemolymph osmolality as a measure of sugar concentration. The discrepancy between in vitro and in vivo potency of suidatrestin may be understood once its chemical structure is fully known.
Comp Biochem Physiol B Biochem Mol Biol 1998 Aug
PMID:Comparative studies of suidatrestin, a specific inhibitor of trehalases. 985 11

The phenotypic response of digestive enzymes was assessed in two species of rodents with different foods habits. Species were Phyllotis darwini (omnivorous) and Octodon degus (herbivorous). The activity of sucrase, maltase and aminopeptidase-N were determined in vitro in animals feeding two contrasting diets. No effect of dietary chemistry on sucrase and maltase activities was observed. Nevertheless, aminopeptidase-N showed a reversible response to diet in P. darwini but not in O. degus. Through Principal Component Analysis we separated the specific and non-specific modulation of the enzymes. The analysis showed that aminopeptidase-N activity is up-regulated by dietary protein in P. darwini. Differences in the phenotypic response of this species apparently reflect the historic levels of specific substrates of the natural diets for this enzyme, linking dietary flexibility and digestive plasticity in an evolutionary context.
Comp Biochem Physiol A Mol Integr Physiol 1999 May
PMID:Test of the adaptive modulation hypothesis in rodents: dietary flexibility and enzyme plasticity. 1042 31

The binary toxin (Bin) from Bacillus sphaericus crystals specifically binds to soluble midgut brush border membrane proteins from Culex pipiens larvae. A single 60 kDa midgut membrane protein is identified as the binding protein. This protein is anchored in the mosquito midgut membrane via a glycosyl-phosphatidylinositol (GPI) anchor, and is partially released by phosphatidylinositol specific-phospholipase C (PI-PLC). Fractionation of soluble proteins by anion exchange chromatography indicates that the binding protein does not co-elute with leucine aminopeptidase activity. After partial purification, the sequences of internal amino acid fragments of the 60 kDa protein were determined. The peptide sequences were compared with data in GenBank, and showed a very high degree of similarity with enzymes belonging to the alpha-amylase family. Further enzymatic investigation showed that the receptor of the Bin toxin in C. pipiens larval midgut may be an alpha-glucosidase.
Insect Biochem Mol Biol 1999 Aug
PMID:Identification of the receptor for Bacillus sphaericus crystal toxin in the brush border membrane of the mosquito Culex pipiens (Diptera: Culicidae). 1045 23

Both male and female adult stages of the sand fly Lutzomyia longipalpis have detectable amylase activity in their salivary glands, as indicated by formation of p-nitrophenyl-alpha-D-maltoside from p-nitrophenyl-alpha-D-octoside and by hydrolysis of 4-nitrophenyl-alpha-D-maltoheptaoside-4,6,-O-ethylidene. No salivary alpha-glucosidase was detected. Amylase activity was also found in the crop and midgut of female flies, although in a smaller amount. Salivary amylase is significantly reduced from the salivary glands immediately after a blood meal, as is the case with salivary alpha-glucosidases in mosquitoes. Presence of salivary gland amylase in these sand flies, and absence of salivary alpha-glucosidase, indicates that in nature these insects may have a significant intake of carbohydrates in the form of starch, as suggested by their plant-feeding behavior, previously demonstrated by Schlein and Warburg (Schlein, Y., Warburg, A., 1986. Phytophagy and the feeding cycle of Phlebotomus papatasi (Diptera: Psychodidae) under experimental conditions. Journal of Medical Entomology 23, 11-15), and Alexander and Usma (Alexander, B., Usma, M.C., 1994. Potential sources of sugar for the phlebotomine sandfly Lutzomyia youngi (Diptera: Psychodidae) in a Columbia coffee plantation. Ann. Trop. Med. Parasitol. 88, 543-549).
Insect Biochem Mol Biol 2000 Apr
PMID:Salivary amylase activity of the phlebotomine sand fly, Lutzomyia longipalpis. 1072 93

Insectivorous/frugivorous passerine species studied so far lack the ability to modulate intestinal maltase activity, in contrast to galliformes. We tested for dietary modulation of small intestine (SI) enzymes including maltase in house sparrows to understand whether the difference between the galliformes on the one hand, and the passerines on the other, reflects a phylogenetic pattern (maltase modulated in galliformes but not passerines), a dietary pattern (maltase modulated in granivores but not insectivore/frugivores), some other pattern, or chance. We also tested the prediction that intestinal peptidase activity would be increased on a high protein (HP) diet. Birds were fed three diets high in starch, protein, or lipid for 10 days. For birds on the HP diet (60.3% protein) we observed the predicted upward modulation of aminopeptidase-N activity, as compared with the lower-protein, high starch (HS) (12.8% protein) diet. In contrast, birds eating the HS diet had similar maltase and sucrase activities, and only slightly higher isomaltase activity, compared with birds eating the high protein (HP), starch-free diet. Birds eating high lipid (HL) diet had low activities of both carbohydrases and peptidase. Considering that the statistical power of our tests was adequate, we conclude that house sparrows show little or no increase in carbohydrases in response to elevated dietary carbohydrate. We cannot reject the hypothesis that maltase lability among avian species has a phylogenetic component, or that high dietary fat has a depressing effect on both carbohydrase and peptidase activities.
Comp Biochem Physiol A Mol Integr Physiol 2000 Jan
PMID:Dietary modulation of intestinal enzymes of the house sparrow (Passer domesticus): testing an adaptive hypothesis. 1077 27

The complete sequence of the 3-kb cDNA and the 5' genomic structure are reported for the gene encoding the shrimp alpha-glucosidase. Alpha-glucosidase cDNA was isolated from a shrimp digestive gland cDNA library. The 2830-base pair cDNA contains an open reading frame that encodes 919 amino acids. The shrimp alpha-glucosidase cDNA shows a high level of identity with that of the human sucrase-isomaltase, human maltase-glucoamylase, and human acid lysosomal alpha-glucosidase, indicating that the protein shares the same structural domains. The similarities among these proteins are found as clusters and characterize the glycosyl hydrolase family 31. To our knowledge, this is the first report to describe a satellite sequence in the 5' genomic structure before the TATA box in an invertebrate sequence.
Cell Mol Life Sci 2000 Jul
PMID:Molecular cloning of a cDNA encoding alpha-glucosidase in the digestive gland of the shrimp, Litopenaeus vannamei. 1096 50

Fertilization in Bufo arenarum requires the sperm to penetrate the egg envelopes. The incubation of isolated vitelline envelopes with sperm induces the acrosome reaction, releasing proteases and glycosidases to the media. In the present work N-acetyl-beta-D-glucosaminidase, beta-D-galactosidase, beta-D-glucosidase, alpha-D-mannosidase, alpha-L-fucosidase, and alpha-D-glucosidase activities are measured in spermatozoa. N-acetyl-beta-D-glucosaminidase is the major sperm glycosidase activity assayed. However, N-acetyl-beta-D-galactosamine show competitive inhibitory effect. The glycosidase pH optimum is 3.5 being inhibited at pHs higher than 7.5. In our study, N-acetyl-beta-D-glucosaminidase is the only glycosidase that in vitro binds to vitelline envelopes in conditions that resemble natural fertilization media. The isolation of the active enzyme will allow studies of its role in fertilization. The enzyme has been purified in a two-step procedure. After native gel electrophoresis, the activity-stained band was cut out and the eluted enzyme was finally subjected to ConA-sepharose chromatography. In SDS-PAGE, the denatured enzyme migrates as a single band with a molecular mass of 45 kDa. Furthermore, analysis by size-exclusion on HPLC showed a peak of activity at around 45 kDa. Preliminary localization studies showed higher relative activity in the acrosomal content. In addition, 10% of the N-acetyl-beta-D-glucosaminidase activity was associated with the reacted sperm. By in vitro fertilization assay, it was observed that the inhibition of the enzyme results in the inhibition of fertilization. This last study shows that N-acetyl-beta-D-glucosaminidase plays an important role in toad fertilization.
Mol Reprod Dev 2000 Oct
PMID:Purification and biological characterization of N-acetyl beta-D glucosaminidase from Bufo arenarum spermatozoa. 1098 20

The goal of this study was to assess the contributions of the most important acid glycosidases to the processes connected with testes involution (in the summer) and spermatogenesis during the reproductive season (the spring) in ganders. Statistically significant increases in the specific activity of N-acetyl-beta-D-hexosaminidase, alpha-D-galactosidase, beta-D-galactosidase, and alpha-L-fucosidase during the period of testes involution were detected. Alpha-D-galactosidase, beta-D-galactosidase, and alpha-D-glucosidase showed an increase in the relative contribution of those multiple forms which are characterized by less acidic values of the pI during the reproductive season. It is suggested that the observed increases in the specific activity of beta-HEX, alpha-GAL, beta-GAL and alpha-FUC may be connected with the catabolism of glycoconjugates, when the spermatogenic activity of the testes declines. The increases in the relative contribution of less acidic forms of alpha-GAL, beta-GAL, and alpha-GLU during the reproductive season may be linked to the rise in the number of spermatocytes, spermatids and spermatozoa during spermatogenesis.
Comp Biochem Physiol B Biochem Mol Biol 2000 Nov
PMID:Sesonal changes in acid glycosidases from gander testes. 1112 69

As short chain fatty acids produced in the forestomach are insufficient to satisfy the energy requirements of the concentrate selecting roe deer (Capreolus capreolus), it is proposed that these animals may have other mechanisms to avoid energy losses due to microbial fermentation. Nutrients bypassing down the ventricular groove (rumen bypass) or ruminal escape of unfermented or partially fermented nutrients may be two alternatives. As metabolic evidence for incomplete fermentation in the forestomach we investigated: (1) the abundance of the sodium-dependent glucose co-transporter (SGLT1) in the duodenum; (2) enzyme activities of maltase, saccharase and alpha-amylase in duodenal and pancreatic tissue; and (3) the proportion of essential, polyunsaturated fatty acids in depot fat samples from ruminants of different feeding type and--for comparison--from animals with a simple stomach. The high abundance of SGLT1, high enzyme activity and the high proportion of polyunsaturated fatty acids in the concentrate selecting ruminants support the hypothesis of rumen bypass or ruminal escape of nutrients in roe deer and reflect differences in nutrient utilization by ruminants that belong to different feeding types.
Comp Biochem Physiol A Mol Integr Physiol 2001 Feb
PMID:Metabolic evidence of a 'rumen bypass' or a 'ruminal escape' of nutrients in roe deer (Capreolus capreolus). 1122 90


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