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)

Transport of glutamine by brush-border vesicles prepared from the renal cortex was studied. The transport system had both Na+-dependent and Na+-independent components. The presence of Na+ in the incubation resulted in an 'overshoot' at 30s at which time the rates of transport were approx. 8 times the values obtained in the absence of Na+. Variation of the glutamine concentration showed that the system obeyed Michaelis-Menten kinetics with Km and Vmax. values for the Na+-dependent system of 0.86 mM and 9.6 nmol/min per mg of protein respectively. Vesicles obtained from chronically acidotic rats showed similar kinetic characteristics. The Km and Vmax. values for the Na+-dependent system were 0.76 mM and 9.6 nmol/min per mg of protein respectively. There was increased uptake of glutamine by vesicles from acidotic rats and this increase was associated with increased activity of gamma-glutamyltransferase in these preparations. Vesicles from acidotic rats, however, showed no increase in glucose transport and no increase in the activity of maltase, another brush-border enzyme.
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PMID:Transport of glutamine by rat kidney brush-border membrane vesicles. 4 16

This study was performed to determine whether the addition of alanyl-glutamine (Ala-Gln) can prevent intestinal mucosal atrophy induced by standard solution of total parenteral nutrition (S-TPN). Forty-one male Sprague-Dawley rats weighing 250 g were randomly divided into four groups: group I was killed after overnight fasting; group II received S-TPN. The other groups received S-TPN supplemented with amino acids other than glutamine (group III) or supplemented with Ala-Gln 2 g/100 mL (group IV); both solutions were isocaloric and isonitrogenous. After 1 week of TPN the rats were killed, and the duodenum, proximal jejunum, mid-small bowel, and distal ileum were obtained for morphologic and functional analysis. Weight gain did not differ significantly among these four groups, and there was no difference in nitrogen balance between groups III and IV. Serum glutamine in group IV (102.8 +/- 13.3 mumol/dL) was significantly increased (p less than .05) compared with groups I, II, and III (66.2 +/- 3.9, 55.7 +/- 7.8, and 61.3 +/- 10.8 mumol/dL, respectively). Mucosal wet weight, protein, RNA, sucrase, and maltase of group IV were significantly increased (p less than .05) compared with groups II and III. Villus height was significantly increased (p less than .05) in the jejunum of group IV rats compared with groups II and III, but not in any other segments of the intestine. No significant changes were observed in crypt depth among all groups. Diamine oxidase in groups II, III, and IV was significantly decreased (p less than .05) compared with group I in all segments except for the ileum.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The dipeptide alanyl-glutamine prevents intestinal mucosal atrophy in parenterally fed rats. 137 46

This study was designed to measure the effect of free glutamine or glutamic acid supplementation on small intestinal growth and disaccharidase enzyme activity in 7-day-old miniature piglets. The piglets received one of three total parenteral nutrition solutions exclusively for 7 days. All three solutions were isonitrogenous and isocaloric, and glutamine or glutamic acid was included at physiological levels (5% of the total amino acid content) in two of the three solutions; the third (control) contained neither glutamine nor glutamic acid. No differences were seen between groups in plasma glutamine or glutamic acid concentrations. Similarly, no effect was observed on small intestinal protein or DNA content or on the specific activities of lactase, sucrase, or maltase. These data demonstrate that in the healthy miniature piglet, parenteral glutamine or glutamic acid supplemented at physiological doses does not influence small intestinal growth and development.
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PMID:Glutamine or glutamic acid effects on intestinal growth and disaccharidase activity in infant piglets receiving total parenteral nutrition. 167 20

Gut atrophy develops during prolonged total parenteral nutrition (TPN). TPN solutions do not contain glutamine, an energy substrate of the intestinal tract. This study evaluated the effect of addition of L-glutamine to TPN on gut nitrogen content, histology, and disaccharidase enzyme activity. Five groups of six Fisher 344 rats received rat chow, D5W, TPN (23% calories as lipid), or TPN with 1 or 2% L-glutamine. Animals given TPN received 30 kcal and 0.22 g nitrogen/100 g/day. Metabolic cages allowed nitrogen balance for each group. After 6 days infusion, stomach, small bowel, and colon were assayed for total nitrogen and sucrase, lactase, and maltase activity. Mucosal height and fatty infiltration of the liver were determined from histologic sections. Adding either 1 or 2% L-glutamine resulted in no toxic clinical effects. Glutamine preserved intestinal nitrogen content of the stomach and colon compared to standard TPN and increased nitrogen content of small bowel to greater than that in chow-fed animals. Glutamine maintained mucosal height of the stomach and colon, but was no better than TPN alone in maintenance of small bowel mucosal height. One percent glutamine increased and standard TPN depressed maltase activity compared to chow. Standard TPN and 1% glutamine both stimulated sucrase and lactase activity compared to chow. Addition of 1 or 2% glutamine protected the liver from fatty infiltration seen with standard TPN. These studies would suggest the addition of glutamine might be beneficial during provision of standard total parenteral nutrition.
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PMID:Use of L-glutamine in total parenteral nutrition. 313 88

Glutamine (GLN) is an important fuel and epidermal growth factor (EGF) is a potent mitogen for intestinal mucosa cells. GLN-enriched parenteral nutrition was administered to male Wistar rats, and subcutaneous injections of EGF were given for 3, 6, and 7 days. Control animals were fed a non-GLN-containing solution. Other groups of animals received GLN or EGF alone. Mucosal samples were obtained from the jejunum, ileum, and colon for measurement of weight, DNA, protein, and mucosal thickness. Disaccharidase activity was measured in the jejunum. After 3 days, only animals that received both GLN and EGF had a significant increase in small-bowel mucosal protein and thickness relative to controls. A similar pattern was observed in the colon, where animals that received both agents had a greater mucosal thickness, DNA, and protein content than controls. At 7 days, animals that received EGF or GLN had greater nitrogen retention. In addition, animals that were treated with EGF had elevated sucrase and maltase activity compared with GLN-fed animals at this time. Animals treated with GLN and EGF tended to have increased sucrase activity relative to controls. GLN feeding was associated with increased mucosal DNA and protein contents throughout the intestine for the combined series. EGF increased mucosal DNA and protein in the small intestine but not in the colon. The effect of EGF on the protein content of the small-bowel mucosa was dose dependent. The effects of GLN and EGF on the small bowel and colonic mucosa were additive. These studies suggest that specific nutrients and hormones may be used in combination to decrease the mucosal atrophy that commonly occurs after gut disuse or disease.
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PMID:Combined effects of glutamine and epidermal growth factor on the rat intestine. 313 28

Mutations in the SSN6 gene suppress the invertase derepression defect caused by a lesion in the SNF1 protein kinase gene. We cloned the SSN6 gene of Saccharomyces cerevisiae and identified its 3.3-kilobase poly(A)-containing RNA. Disruption of the gene caused phenotypes similar to, but more severe than, those caused by missense mutations: high-level constitutivity for invertase, clumpiness, temperature-sensitive growth, alpha-specific mating defects, and failure to homozygous diploids to sporulate. In contrast, the presence of multiple copies of SSN6 interfered with derepression of invertase. An ssn6 mutation was also shown to cause glucose-insensitive expression of a GAL10-lacZ fusion and maltase. The mating defects of MAT alpha ssn6 strains were associated with production of two a-specific products, a-factor and barrier, and reduced levels of alpha-factor; no deficiency of MAT alpha 2 RNA was detected. We showed that ssn6 partially restored invertase expression in a cyr1-2 mutant, although ssn6 was clearly not epistatic to cyr1-2. We also determined the nucleotide sequence of SSN6, which is predicted to encode a 107-kilodalton protein with stretches of polyglutamine and poly(glutamine-alanine). Possible functions of the SSN6 product are discussed.
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PMID:Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae. 331 83

Strain SF22, a glutamine-requiring (Gln-) mutant of Bacillus subtilis SMY, is likely to have a mutation in the structural gene for glutamine synthetase, since this strain synthesized 22 to 55% as much glutamine synthetase antigen as did wild-type cells in a 10-min period but had less than 3% of wild-type glutamine synthetase enzymatic activity. The expression of several genes subject to glucose catabolite repression was altered in the Gln- mutant. The induced levels of alpha-glucosidase, histidase, and aconitase were 3.5- to 4-fold higher in SF22 cells than in wild-type cells grown in glucose-glutamine medium, and citrate synthase levels were 8-fold higher in the Gln- mutant than in wild-type cells. The relief of glucose catabolite repression in the Gln- mutant may result from poor utilization of glucose. Examination of the intracellular metabolite pools of cells grown in glucose-glutamine medium showed that the glucose-6-phosphate pool was 2.5-fold lower, the pyruvate pool was 4-fold lower, and the 2-ketoglutarate pool was 2.5-fold lower in the Gln- cells than they were in wild-type cells. Intracellular levels of glutamine were sixfold higher in the Gln- mutant than in wild-type cells. Measurements of enzymes involved in glutamine transport and utilization showed that the elevated pools of glutamine in the Gln- mutant resulted from a threefold increase in glutamine permease and a fivefold decrease in glutamate synthase. The pleiotropic effect of the gln-22 mutation on the expression of several genes suggests that either the glutamine synthetase protein or its enzymatic product, glutamine, is involved in the regulation of several metabolic pathways in B. subtilis.
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PMID:Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression. 614 Nov 56

The pathology and enzymology of the intestinal mucosae of lambs dosed daily with 2500 Trichostrongylus vitrinus larvae and killed at five, nine or 14 weeks were compared with worm-free animals. The proximal small intestines of the infected lambs exhibited extensive mucosal damage at five and nine weeks, but only isolated lesions were found at 14 weeks. Activities of the brush border enzymes alkaline phosphatase, leucine amino-peptidase, maltase and glycyl-L-leucine dipeptidase were all significantly depleted during infection, although the magnitude, time of onset and duration of the individual enzyme responses varied. Mucosal activities of the pancreatic enzymes, trypsin and to a lesser extent chymotrypsin were also markedly decreased particularly during the first nine weeks of infection. Specific acetylcholinesterase activity was significantly increased throughout the study, maximal levels being observed at five weeks. In contrast 'pseudo'-cholinesterase levels were consistently within the control range. During the early stages of infection (five weeks) glutamine-oxaloacetate transaminase activity was significantly decreased, while aldolase and creatine phosphokinase levels were significantly elevated. At nine weeks low glutamine-oxaloacetate transaminase activities were again detected and lactate dehydrogenase activity was also markedly reduced. At 14 weeks the mean activities of all four enzymes were within the normal range as were superoxide dismutase levels throughout. Significant correlations were found between alkaline phosphatase, trypsin, chymotrypsin, aldolase and glutamine-oxaloacetate transaminase activities and the degree of mucosal damage within the individual lambs.
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PMID:Changes in the intestinal enzyme activity of lambs during chronic infection with Trichostrongylus vitrinus. 710 Jun 47

Since epidermal growth factor (EGF) enhances gut mucosal regeneration, the present study was undertaken to evaluate the effect of EGF on brush-border membrane enzyme activity and glutamine uptake in the intestinal remnant following extensive small bowel resection. Twenty-four adult male New Zealand White rabbits were divided into three groups: Group 1 (n = 12) served as controls. Groups 2 and 3 (n = 6 each) underwent a 50-60% mid-jejunoileal resection with anastomosis of the remaining intestine, leaving 90 cm between the pylorus and the ileocecal valve. Group 3 rabbits had a subcutaneous osmotic pump implanted to deliver EGF for 7 days at 0.3 micrograms/kg/hr. Rabbits from Groups 2 and 3 were sacrificed 3 weeks postoperation. Mucosa from the proximal and distal segments of the remaining intestine was analyzed for wet/dry weight, maltase and aminooligopeptidase activity, and glutamine uptake. There was a twofold increase in mucosal dry weight/cm of intestine in rabbits without EGF at 3 weeks (Group 2) and a fourfold increase in those given EGF (Group 3). The maltase enzyme capacity (UEnzyme/rabbit) increased from 37 +/- 10 in controls (Group 1) to 167 +/- 30 without EGF and 207 +/- 30 with EGF. The aminooligopeptidase enzyme capacity (UEnzyme/rabbit) increased from 55 +/- 10 to 147 +/- 20 and 226 +/- 30 in Groups 1, 2, and 3, respectively. Glutamine uptake capacity (microM glutamine/min) also increased significantly, from 63 +/- 19 in Group 1 to 88 +/- 6 without EGF and 162 +/- 18 with EGF (P < 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The effect of epidermal growth factor on mucosal function after ileal resection. 779 29

Total parenteral nutrition (TPN) is associated with atrophic changes in the structure and function of the intestinal mucosa. Because rapidly renewing intestinal mucosal cells may require an external source of purines and pyrimidines for their optimal growth, it can be assumed that supplementation of nucleosides and a nucleotide mixture (OG-VI) during TPN may prevent the progression of mucosal atrophy by compensating for a relatively insufficient delivery from liver. To test that hypothesis, male Wistar rats receiving TPN for 7 days were divided into four groups according to different TPN solutions. Group C (n = 10) received a standard solution, group O (n = 10) received OG-VI in addition to the standard solution, and group G (n = 10) received a glutamine-rich TPN solution containing almost the same amount of calories and nitrogen as the standard solution. Group O+G (n = 10) received OG-VI in addition to the glutamine-rich solution. Various parameters were examined on the eighth day in the jejunal and ileal segments. The following significant changes in comparison with group C were observed: total wet weight of the jejunal segment in group O was significantly greater, as was mucosal wet weight of the jejunal and ileal segments in groups O and O+G; protein contents of the ileal segment in group O as well as the DNA content of the jejunal segment in group O increased significantly; and maltase activity of the jejunal segment in group O+G increased, as did the villus height of the jejunal segment in groups O and O+G and the villus height of the ileal segment in group G.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Intravenous administration of nucleosides and a nucleotide mixture diminishes intestinal mucosal atrophy induced by total parenteral nutrition. 809 74


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