Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.108 (lactase)
 2,133 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adult rats when fed a high carbohydrate diet of 70% sucrose or glucose for 24 h following a 4-day fast showed increased concentrations of intestinal sucrase-isomaltase (EC 3.2.1.48, EC 3.2.1.10) and maltase-glucoamylase (EC 3.2.1.20) but not lactase-phlorizin hydrolase (EC 3.2.1.23, EC 3.2.1.62). The concentration increases of these enzymes were accompanied by corresponding acceleration of their synthesis rates. Contrary to earlier studies by others, suggesting that upper villus cells in the fasted intestine are unresponsive to stimulation of sucrase activity by refeeding a high-sucrose diet, the concentration increases of both sucrase-isomaltase and maltase-glucoamylase were seen to occur in cells all along the length of the villus column. The earlier studies differed from the present study by basing enzyme assays relative to protein rather than the DNA content of villus cell fractions. We have shown that villus cells increase their protein content severalfold while migrating to villus tip, providing the basis for the difference between earlier and the present findings. Further evidence that stimulation of sucrase-isomaltase and maltase-glucoamylase by high carbohydrate is not restricted to the crypt and lower villus region was obtained by the finding that their synthesis rates appeared to be equally stimulated along the length of the villus column.
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PMID:Dietary CHO and stimulation of carbohydrases along villus column of fasted rat jejunum. 249 55

The effect of oral refeeding after total parenteral nutrition (TPN) on brush border hydrolases was measured in the proximal jejunum and ileum of adult rats. The animals received intravenously for 4 days a mixture of Intralipid 10% and Vamine-Glucose. At the end of TPN, oral feeding was reinstituted and the rats were fed with an isocaloric standard diet (60% carbohydrate, 17% protein, 3% lipid). Sucrase, isomaltase, lactase, and aminopeptidase N activities were measured at the end of TPN and at 1, 3, and 5 days after TPN. Sham-operated rats nourished orally with the standard diet were used as controls. In both intestinal segments, lactase activity showed no significant changes at the end of TPN or during oral realimentation. Isomaltase, and especially sucrase activities, exhibited an important drop at the end of TPN. After TPN, a complete restoration of isomaltase and sucrase activities was obtained in the jejunum only. During oral refeeding a 40% deficit in sucrase activity persisted in the ileum throughout the experimental period, whereas normal isomaltase activity was restored in this segment. Aminopeptidase N activity was lowered by TPN and recovered normal values within a few hours after oral realimentation. Thus, reinstitution of oral feeding after TPN should take into account that the intestine is capable of digesting normal amounts of dietary protein but has a reduced tolerance for carbohydrates.
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PMID:Imbalance between jejunum and ileum in the response of brush border hydrolases to oral feeding after intravenous alimentation in rats. 249 65

Seven patients with congenital sucrase-isomaltase deficiency corresponding to the known diagnostic criteria and five patients having combined disaccharidase deficiencies with unusual pattern characterized by more pronounced sucrase than lactase deficiency were found among 505 children investigated by first jejunal biopsy. On the base of the case histories, the complications and the comparative evaluation of patient and control groups' data (the latter consisted of nine untreated coeliacs) the congenital sucrase-isomaltase deficiency was found to make the patients to be especially susceptible to enteral infections and consequently to postinfectious intestinal damages. These complicated cases do not correspond to the classic diagnostic criteria of the congenital enzyme deficiency causing diagnostic errors. In order to avoid the misdiagnoses the authors suggest modification of the diagnostic criteria of congenital sucrase-isomaltase deficiency as follows: the diagnosis of congenital enzyme deficiency might be verified in spite of mild histological signs and hypolactasia if the degree of lactase deficiency repeatedly and significantly is exceeded by the degree of sucrase deficiency.
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PMID:[Congenital saccharase-isomaltase defect--diagnostic difficulties]. 251 45

Small-intestinal disaccharidase activities of eight suckling T. vulpecula, aged from 34 to 150 days, and of two adult animals were investigated. Intestinal maltase, isomaltase and sucrase activities increased with age, whereas lactase activities decreased. Trehalase activities were relatively high in all animals and showed no obvious age-related changes. Three separate beta-galactosidase activities, one neutral and two acid, acted on lactose. The neutral beta-galactosidase activity appeared to be due to a brush border enzyme similar to that of eutherian mammals, whereas the acid beta-galactosidases were soluble and probably of lysosomal origin. One of these, acid beta-galactosidase-1, had similar properties to the sole intestinal beta-galactosidase of macropodid marsupials, whereas the other, acid beta-galactosidase-2, has not previously been described. Galactosyl oligosaccharides isolated from macropodid milk were readily hydrolysed by both acid beta-galactosidases but not by the neutral beta-galactosidase. The total intestinal lactase activity in animals aged up to 125 days was due mainly to acid beta-galactosidase-1, whereas in older animals it was due mostly to the neutral beta-galactosidase; this suggests that late in lactation the young T. vulpecula change from a macropodid mode of digestion of galactosyl oligosaccharides to a eutherian mechanism for the digestion of lactose. These findings may have implications for the hand-rearing of orphaned T. vulpecula.
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PMID:Intestinal lactase (beta-galactosidase) and other disaccharidase activities of suckling and adult common brushtail possums, Trichosurus vulpecula (Marsupialia:Phalangeridae). 251 66

Maturation of mechanisms for carbohydrate absorption occurs in a defined sequence during human fetal development. The intestinal enzymes, lactase, sucrase, maltase, isomaltase, and glucoamylase, are at mature levels in the term fetus. Mature levels of pancreatic amylase activity and glucose transport occur postnatally, and levels are low in both the term and preterm neonate. In the preterm infant, sucrase, maltase, and isomaltase are usually fully active, but lactase activity, which increases markedly from 24 to 40 weeks, may be low depending upon fetal age. Despite these developmental patterns, clinical lactose intolerance is uncommon. Postnatal adaptive responses to ingested carbohydrates lead to competent carbohydrate absorption. Inadequately absorbed carbohydrates are salvaged by colonic flora through fermentation of carbohydrates to hydrogen gas and short-chain fatty acids; the latter are readily absorbed by the colon. In this setting, carbohydrate tends to be absent from the stool. Noninvasive reflection of the status of carbohydrate absorption may be obtained from breath hydrogen testing, a technique of particular value in young infants.
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PMID:Development of carbohydrate absorption in the fetus and neonate. 257 23

The synthesis and secretion of apolipoprotein B (apo B) was studied in a human colon carcinoma (Caco-2) cell line and in explants from normal human intestine. In Caco-2 cells, the specific activity of the intestinal disaccharidases maltase, sucrase-isomaltase and lactase was enhanced 8-, 6- and 3-fold respectively, at 19 days post-confluence as compared with 1-day-post-confluence cultures. The level of apo B secreted into the medium increased from undetectable in the cells just reaching confluency, to 115 ng/ml at 18 days post-confluence. The presence of apo B-100 and apo B-48 with mobilities on SDS/polyacrylamide-gel electrophoresis corresponding to those of human very-low-density lipoproteins and lymph chylomicrons, respectively, was detected in the media from 7-, 12- and 18-days-post-confluence cells. These two apo B proteins were also found intracellularly in 7-day-post-confluence cultures. However, more differentiated cells (12 and 18 days post-confluence) accumulated large amount of a 214 kDa protein intracellularly. Apo B-related 214 kDa protein was also synthesized by normal human intestinal explants. A pulse-chase experiment with explants from normal human jejunum showed a slow intracellular conversion of the 214 kDa protein into the size of mature apo B-48 (264 kDa), concomitant with increasing amounts of mature apo B-48 in the medium, suggesting a precursor-product relationship. Despite large intracellular quantities, the 214 kDa protein from the normal human tissue and Caco-2 cells was absent from the medium. No apo B-100 synthesis was detected in the human explants. These findings may help in our understanding of cholesterol and lipid metabolism in health and in some disorders characterized by the inability to secrete apo B-containing lipoproteins.
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PMID:Biosynthetic precursor (214 kDa) of apolipoprotein B-48 is not secreted by Caco-2 cells and normal human intestine. 260 23

In a retrospective study, jejunal mucosal disaccharidase and alkaline phosphatase activities have been investigated in 40 controls and patients with proven celiac sprue (n = 26), lactase deficiency (n = 26), osteoporosis or osteomalacia (n = 16), chronic pancreatitis (n = 12), giardiasis (n = 7), or Crohn's disease (n = 7). Apart from a nonselective reduction of mucosal enzyme activities in the sprue syndrome and a selective reduction of lactase activity in the patients with primary lactase deficiency, assays of mucosal disaccharidases revealed only inconstant or slight deviations from the control group and were not of diagnostic significance for any of the above-mentioned disorders. Isolated forms of enzyme deficiencies other than lactase deficiency, such as sucrase-isomaltase or trehalase deficiency were not present among 168 investigations carried out from 1972-1982. It is concluded that assay of small intestinal disaccharidase or alkaline phosphatase activities does not expand the diagnostic impact of morphological examination of small bowel biopsy specimens and modern noninvasive methods for the detection of carbohydrate malabsorption. Thus, the method does not appear a necessary or relevant investigation in routine clinical practice.
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PMID:Is the assay of disaccharidase activity in small bowel mucosal biopsy relevant for clinical gastroenterologists? 274 34

A patient with congenital asucrasia was investigated using in vivo differential urinary disaccharide excretion. Impaired hydrolysis of sucrose and isomaltose, but normal lactase activity, were demonstrated and confirmed by in vitro estimation. The technique of differential disaccharide excretion can now be used to assess three disaccharidases simultaneously, in vivo, including isomaltase.
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PMID:Intestinal disaccharidases assessed in congenital asucrasia by differential urinary disaccharide excretion. 291 Jun 70

The inhibitory action and mechanism of inhibition of two types of alpha-glucosidase inhibitors, acarbose (Bay-g-5421) and 1-deoxynojirimycin derivatives (Bay-m-1099 and Bay-o-1248), on small intestinal carbohydrases (sucrase, isomaltase, glucoamylase, trehalase and lactase) and pancreatic alpha-amylase were compared in vitro using small intestinal brush border membranes and pancreatic homogenates from adult Sprague-Dawley rats. Acarbose at a low (4 microM) concentration strongly inhibited the activities of glucoamylase, alpha-amylase and sucrase (98, 68, and 63%, respectively). At a high (200 microM) concentration, isomaltase activity was also inhibited (28%); effects on trehalase and lactase activities were negligible. Both the 1-deoxynojirimycin derivatives were even more potent inhibitors of sucrase (Ki = 8.6 x 10(-8) M for Bay-m-1099;Ki = 5.0 X 10(-8) M for Bay-o-1248) than acarbose (Ki = 9.9 x 10(-7) M). Whereas glucoamylase activity was strongly inhibited by the 1-deoxynojirimycin derivatives, alpha-amylase activity was not. In contrast to acarbose, the 1-deoxynojirimycin derivatives at high concentrations (20-200 microM) inhibited considerably trehalase and lactase (a beta-galactosidase) activities. The inhibition of lactase activity was stronger by Bay-m-1099 (Ki = 4.9 X 10(-6) M) than by Bay-o-1248 (Ki = 6.7 X 10(-5) M). Where inhibition was seen, kinetic analysis showed fully competitive inhibition of sucrase, isomaltase, trehalase, glucoamylase and lactase by all three inhibitors.
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PMID:Inhibitory mechanism of acarbose and 1-deoxynojirimycin derivatives on carbohydrases in rat small intestine. 296 44

Rat intestinal microvillus membrane contains at least 24 polypeptides, of which 18 can be solubilized using Triton X-114 at 4 degrees C. Upon phase separation at 32 degrees C, 11 proteins separated nearly completely into the detergent-rich phase, while 9 proteins were found exclusively in the aqueous phase. Enzymes which were uniquely included in the detergent phase were alkaline phosphatase, leucine aminopeptidase, gamma-glutamyl transpeptidase, and Ca2+-Mg2+ ATPase. The proteins which were excluded from the detergent phase and found exclusively in the aqueous phase included the disaccharidases (glucoamylase, sucrase-isomaltase, trehalase, lactase) and the ileal receptor for the intrinsic factor-cobalamin complex. Integral membrane proteins can thus be separated during solubilization into two groups prior to further purification or characterization.
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PMID:Phase separation of rat intestinal brush border membrane proteins using Triton X-114. 301 Jul 62


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