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:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have previously demonstrated that intake of fat as well as carbohydrate affects the activity and immunoreactive amount of sucrase-isomaltase (S-I) in rat jejunum. To examine whether diet-related changes in sucrase and isomaltase activities are accompanied by the variations of sucrase-isomaltase mRNA levels, 7-week-old rats were fed either a high-long-chain triacylglycerols diet (73 energy% as corn oil), a high-medium-chain triacylglycerols (MCT) diet (66 energy% as MCT, 7 energy% as corn oil) or a high-carbohydrate diet (70 energy% as corn starch) for 7 days. Northern blot analysis revealed that S-I mRNA levels were abundant in the jejunum of rats fed the high-MCT diet; the levels were similar to those in the rats fed the high-carbohydrate diet. Force-feeding a high-sucrose diet (40 energy% as sucrose) brought about a parallel rise in both S-I mRNA and sodium/D-glucose cotransporter (SGLT1) mRNA levels within 12 h. Force-feeding the high-MCT diet also produced an elevation of S-I mRNA and SGLT1 mRNA. However, force-feeding a diet containing alpha-methylglucoside, a non-metabolizable but actively transported sugar, did not increase S-I mRNA or SGLT1 mRNA level; sucrase activity was nevertheless elevated by feeding alpha-methylglucoside diet. These results suggest that not only carbohydrate intake but also MCT intake might influence S-I mRNA and SGLT1 mRNA levels in the jejunum, presumably through common metabolite(s) of carbohydrates and MCT, and that carbohydrate may play another role in enhancement of the sucrase activity through modulation of translation and/or posttranslational modifications of the sucrase-isomaltase complex.
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PMID:Dietary regulation of sucrase-isomaltase gene expression in rat jejunum. 787 73

The role of luminal nutrients in regulating enterocyte gene expression was studied in a natural model for long-term fasting, the hibernating ground squirrel. Squirrels were studied during the active season and during the hibernation season when they had not eaten for at least 12 wk. The specific activities of sucrase, isomaltase, and intestinal alkaline phosphatase in jejunal brush-border membranes were similar in hibernating and active squirrels, whereas amino-oligopeptidase was reduced in hibernators. Na(+)-K(+)-adenosinetriphosphatase activity in jejunal mucosa was unchanged by hibernation. Densitometric analysis of Western blots showed that abundance of sucrase-isomaltase (SI), amino-oligopeptidase, and the Na(+)-glucose cotransporter SGLT1 was similar in the two activity states. Preservation of SI abundance in hibernation was confirmed by immunocytochemistry. Slot-blot analysis revealed no differences in mRNA levels for these proteins between hibernating and active squirrels. Enterocyte proliferation and migration rates were greatly suppressed in torpid squirrels but increased immediately upon rewarming during arousals. These results demonstrate the striking constancy of enterocyte gene expression despite long-term fasting in a hibernating mammal.
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PMID:Preservation of intestinal gene expression during hibernation. 894 94

After massive small bowel resection, the intestine adapts to compensate. In addition to proliferation, enterocytes also undergo selective functional adaptation. In this study we examined the effect of intraperitoneal administration of epidermal growth factor (EGF) on the expression of the brush border dissacharidase sucrase, the sodium glucose cotransporter (SGLT1), and the sodium-potassium ATPase pump (NaK ATPase) by enterocytes in the remnant intestine after massive small bowel resection. Adult Lewis rats underwent either ileal transection or 70% proximal intestinal resection. These animals were subdivided into groups that received either saline or EGF intraperitoneally for 1 week. Ilea from each group were harvested 4 weeks postoperatively. Enterocytes were separated from these segments by calcium chelation. The total protein from the isolated cells was subjected to Western blot analysis. Administration of EGF to animals that underwent transection did not significantly alter the expression of sucrase, SGLT1, or NaK ATPase. After intestinal resection, the expressions of sucrase and SGLT1 were significantly increased. The combination of EGF administration and intestinal resection resulted in a further increase in SGLT1 expression. The intraperitoneal administration of EGF selectively enhanced the expression of SGLT1 by enterocytes after massive small bowel resection. Administration of EGF to sham-operated animals did not have similar effects. These results suggest that EGF augments the adaptive response and may therefore have a therapeutic role in the management of patients with short bowel syndrome.
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PMID:Epidermal growth factor selectively enhances functional enterocyte adaptation after massive small bowel resection. 907 Jan 88

Rates of fructose uptake by the small intestine of neonatal rats are typically very low from parturition through weaning but undergo a dramatic increase immediately after weaning is completed. In this study, we used intestinal fructose transport as a model to determine whether nutrient transport, normally enhanced only after completion of weaning, can be enhanced earlier during development. We found that ontogenetic changes in levels of GLUT5 mRNA correlate well with already known ontogenetic changes in rates of intestinal fructose transport: low levels and rates during suckling and weaning, and high levels and rates after weaning. In contrast, levels of GLUT2 and SGLT1 mRNA were relatively more elevated throughout the suckling and weaning periods. We then found that increased expression of GLUT5 mRNA caused by dietary fructose or sucrose paralleled diet-dependent increases in brush-border fructose uptake. Rates of brush-border glucose uptake and levels of SGLT1 and GLUT2 mRNA were not enhanced by dietary fructose, glucose, or sucrose. Finally, we found that rates of fructose uptake, levels of GLUT5 mRNA, and specific sucrase activity each increased with increasing concentrations of dietary fructose given precociously to midweaning rats. In contrast, brush-border glucose uptake was independent of dietary fructose concentration. Thus precocious introduction of dietary fructose causes enhanced expression of fructose transporters earlier during development. This effect is specific: only luminal fructose is effective, and only brush-border fructose transport can be modulated. These results unveil the potential for regulating nutrient transport early in development.
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PMID:Dietary fructose enhances intestinal fructose transport and GLUT5 expression in weaning rats. 912 64

The mu-opioid agonist loperamide is an antidiarrhoeal drug which inhibits intestinal motility and secretion. Its anti-absorptive effects are less well investigated, but may be mediated through calmodulin. We have investigated further the effect of loperamide on the intestinal Na+-dependent D-glucose transporter (SGLT1). Brush-border membrane vesicles were prepared from mouse small intestine, and uptake of [3H]glucose was measured. Na+-dependent glucose uptake displayed the typical overshoot at 34 s; the peak value was 1.6 nmol mg(-1). The overshoot disappeared in the presence of phlorizin or when Na+ was replaced by K+. Extravesicular loperamide dose-dependently inhibited SGLT1 activity with an IC50 value of 450 micromol L(-1). Loperamide displayed a mixed inhibition type: the apparent Vmax decreased from 0.9 to 0.5 nmol mg(-1)/15 s, the apparent Km increased from 0.23 to 1.13 mmol L(-1) glucose. Na+ kinetics were more complex, but loperamide inhibited net glucose uptake by 90% at 100 mmol L(-1) Na+. Glucose uptake was unchanged by agents affecting calmodulin activity. Loperamide inhibited intestinal Na+, K+-ATPase activity, whilst sucrase activity was unaffected. SGLT1 activity was inhibited by loperamide, but this effect was not mediated through calmodulin. As this action is only evident at high concentrations of loperamide a nonspecific mechanism may be involved.
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PMID:Effect of loperamide on Na+/D-glucose cotransporter activity in mouse small intestine. 1087 45

It has been recently demonstrated in the laboratory that the cytoskeletal inhibitor cytochalasin E has an indirect inhibitory effect on the function of the intestinal Na+-sugar cotransporter (SGLT1). The present work confirms that cytochalasin E inhibits SGLT1 activity through cytoskeleton disruption, showing that in anaerobic conditions (N2 bubbling), which implies low cytosolic ATP levels, the inhibition is not observed. As it occurs in sugar transport, the Na+-dependent intestinal transport of phenylalanine decreases if cytochalasin E is present in the incubation medium. However, the activity of the brush border enzymes sucrase, amino peptidase N and gamma-glutamyl transferase is not affected by the inhibitor. These enzymes only have one transmembrane domain and the active center is projected to the intestinal lumen. Therefore, cytoskeleton changes that could modify the transmembrane enzyme segment do not alter the activity of these enzymes. Examination of the intestine morphology after 30 min incubation with cytochalasin E shows only light modifications which do not seem to explain the inhibitory effects of the toxin on Na+-sugar or Na+-phenylalanine cotransporters function. On the whole, these results indicate that the inhibition of cytochalasin E on galactose and phenylalanine intestinal transport is secondary to its action on cytoskeleton through protein structure modifications.
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PMID:Cytoskeleton involvement on intestinal absorption processes. 1087 78

The sodium-D-glucose cotransporter (SGLT1) was expressed in a yeast mutant strain NY 17 (sec6-4) that accumulates secretory vesicles at a nonpermissive temperature because of a block in the delivery of these vesicles to the plasma membrane. By differential centrifugation a microsomal fraction enriched in secretory vesicles was prepared with a high specific activity of the vanadate-sensitive H+-ATPase and invertase. In this membrane fraction one protein band of an apparent molecular weight of 55 kDa representing the nonglycosylated SGLT1 protein could be detected by immunochemical analysis. In addition, higher molecular weight protein bands probably representing dimers and aggregates were found. In transport studies with the microsomes D-glucose fluxes showed asymmetric properties: efflux experiments revealed the typical properties of the SGLT1 such as sodium dependence, inhibition by phlorizin and potential dependence. Influx of D-glucose showed no dependence on sodium and was not inhibited by phlorizin. Furthermore, the transporter exhibited a striking asymmetry with regard to the D-glucose affinity and the sugar specificity. These results suggest that the orientation of the SGLT1 expressed in yeast secretory vesicles is, indeed, inverted with regard to its configuration in the plasma membrane of epithelial cells. Moreover, there are striking functional differences between the periplasmic and cytoplasmic face of the transporter.
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PMID:Functional asymmetry of the sodium-D-glucose cotransporter expressed in yeast secretory vesicles. 1122 Mar 64

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.
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PMID:Metabolic evidence of a 'rumen bypass' or a 'ruminal escape' of nutrients in roe deer (Capreolus capreolus). 1122 90

Noninsulin-dependent diabetes mellitus (NIDDM) is an increasingly common disease, which brings a number of life-threatening complications. In rats with experimentally induced diabetes, there is an increase in the capacity of the intestine to absorb monosaccharides. We have examined the activity and the expression of monosaccharide transporters in the intestine of patients suffering from NIDDM. Na(+)-dependent D-glucose transport was 3.3-fold higher in brush-border membrane (BBM) vesicles isolated from duodenal biopsies of NIDDM patients compared with healthy controls. Western analysis indicated that SGLT1 and GLUT5 protein levels were also 4.3- and 4.1-fold higher in diabetic patients. This was associated with threefold increases in SGLT1 and GLUT5 mRNA measured by Northern blotting. GLUT2 mRNA levels were also increased threefold in the intestine of diabetic patients. Analysis of other BBM proteins indicated that the activity and abundance of sucrase and lactase were increased by 1.5- to 2-fold and the level of the structural proteins villin and beta-actin was enhanced 2-fold in diabetic patients compared with controls. The increase in the capacity of the intestine to absorb monosaccharides in human NIDDM is due to a combination of intestinal structural change with a specific increase in the expression of the monosaccharide transporters SGLT1, GLUT5, and GLUT2.
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PMID:Expression of monosaccharide transporters in intestine of diabetic humans. 1180 45

Dietary carbohydrates, when digested and absorbed in the small intestine of the horse, provide a substantial fraction of metabolisable energy. However, if levels in diets exceed the capacity of the equine small intestine to digest and absorb them, they reach the hindgut, cause alterations in microbial populations and the metabolite products and predispose the horse to gastrointestinal diseases. We set out to determine, at the molecular level, the mechanisms, properties and the site of expression of carbohydrate digestive and absorptive functions of the equine small intestinal brush-border membrane. We have demonstrated that the disaccharidases sucrase, lactase and maltase are expressed diversely along the length of the intestine and D-glucose is transported across the equine intestinal brush-border membrane by a high affinity, low capacity, Na+/glucose cotransporter type 1 isoform (SGLT1). The highest rate of transport is in duodenum > jejunum > ileum. We have cloned and sequenced the cDNA encoding equine SGLT1 and alignment with SGLT1 of other species indicates 85-89% homology at the nucleotide and 84-87% identity at the amino acid levels. We have shown that there is a good correlation between levels of functional SGLT1 protein and SGLT1 mRNA abundance along the length of the small intestine. This indicates that the major site of glucose absorption in horses maintained on conventional grass-based diets is in the proximal intestine, and the expression of equine intestinal SGLT1 along the proximal to distal axis of the intestine is regulated at the level of mRNA abundance. The data presented in this paper are the first to provide information on the capacity of the equine intestine to digest and absorb soluble carbohydrates and has implications for a better feed management, pharmaceutical intervention and for dietary supplementation in horses following intestinal resection.
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PMID:Molecular characterisation of carbohydrate digestion and absorption in equine small intestine. 1211 1


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