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)

The circadian rhythms of sucrase, maltase, isomaltase, trehalase, lactase, gamma-glutamyltransferase, leucylnaphthylamide hydrolyzing activity, alkaline phosphatase and monosaccharide transport were assessed in each fifth of the small intestine of the rat in order to determine if an entire enzyme or transport system population responded in a similar manner or if there were regional differences. Animals were maintained under a light-dark cycle and fed from 1400-1800, EST for 7 days. Functional activities were assessed every 4 h for 24 h, inclusively. Quantitative, and in a few instances, qualitative differences in different areas of the intestine were found for all functions. There were portions of the lactase and alkaline phosphatase populations which displayed no rhythmicity in activity. When rhythmicity was observed there were differences in the activity patterns along the intestine for all functions. Thus, the rhythm patterns obtained from homogenates of the entire small intestine are a composite of the patterns in regions of high average activity. Also, there appears to be a reasonable amount of local control of the various functions.
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PMID:Regional variability in circadian rhythmicity of intestinal digestive-absorptive functions. 4 53

Dog enterocyte brush border proteins have been studied after a 75% proximal resection of the small bowel. This study was carried on microvillar membrane preparations purified from ileal mucosa sampled before and after regeneration on neighbouring intestinal segments, each animal acting as its own control. After six weeks of regeneration a statistically significant decrease of the following enzyme specific activities was observed: lactase, cellobiase, maltase, sucrase, palatinase, dextranase, trehalase, alkaline phosphatase, aminopeptidase and gamma-glutamyl transferase. Analysis of brush border proteins by polyacrylamide gel electrophoresis in presence of sodium dodecyl sulphate have shown after regeneration a decreased rate for the proteins with a molecular weight higher than 100,000 daltons. Modifications of electrophoretic patterns seem to be related to the specific activity decreases observed for brush border enzymes after regeneration, since the molecular weight of these enzymes were found between 116,000 and 285,000 daltons, after gel filtration.
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PMID:Effect of massive proximal small bowel resection on intestinal brush border membrane proteins in the dog. 8 27

Intestinal mucosa from 40 patients obtained by fiber-endoscopic biopsy was assayed for disaccharidases to determine suitability of this tissue for assay. The combined specimens from each patient provided 4.7-38.7 mg of tissue, adequate in all instances for duplicate determinations of protein, lactase, sucrase, and maltase. Tissue remained for assays of palatinase in 39 instances, trehalase and cellobiase in 37, and alkaline phosphatase in 22 cases. Twenty-four subjects had normal lactose tolerance tests and normal sucrase/lactase ratios. Thirteen patients with abnormal oral lactose tolerance tests were identified as having a primary low lactase activity on the basis of elevated sucrase/lactase ratios. This ratio was most helpful in making the diagnosis of a primary low lactase, since the mucosal specimens were not obtained from comparable areas. Tissue from three subjects with an abnormally low maltase was unsuitable for diagnosis. Endoscopic biopsy of mucosa appears to be satisfactory for disaccharidase assays in most instances.
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PMID:Adequacy of endoscopic biopsy specimens for disaccharidase assays. 10 20

Different hydrolases (cellobiase, enterokinase, lactase, leucine aminopeptidase, alcaline phosphatase and trehalase) of the brush border's enterocytes of the rat have been studied by electrofocusing. Every hydrolase is focused in a single peak, the pI of which is given.
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PMID:[Electrofocusing of hydrolases in rat brush border enterocytes]. 12 72

Mucosal response of alkaline phosphatase, ATPase and disaccharidase (lactase, maltase and trehalase) activities to sex hormones were studied by comparing male and female rats and castrated males and by injecting testosterone into castrated males. Alkaline phosphatase showed a very steep gradient in the small intestine from the oral to the aboral end, whereas ATPase activity in the ileum was still about 50% of that in the duodenum. Both enzymes showed only minor sex variations and weal response to castration. Lactase and maltase had peak activities in the jejunum, but trehalase activity was nearly equally high in the duodenal mucosa as in the jejunum. Jejunal lactase activity was about 50% lower in female than in male rats and castration decreased activity in males to the same low level as found in females. The administration of testosterone to castrated male rats did not enhance activity. Maltase activity showed similar sex variation, although castration was not able to decrease activity during the test period. Trehalase activity was lower in female than in male rats. The administration of testosterone enhance activity in castrated males.
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PMID:Sex variation in the activities of mucosal hydrolytic enzymes in the small intestine of the rat. 12 35

Various enzyme activities involved in the active transport system, glycolysis, and digestion were assayed in various parts of the gastrointestinal tracts of germfree, conventional, and gnotobiotic rats associated with indigenous bacteria. The activity levels of alkaline phosphatase, glucose 6-phosphatase, adenosine triphosphatase, and disaccharidases in the upper small intestine were highest in all parts of the gastrointestinal tracts of various kinds of gnotobiotic, conventional, and germfree rats. Alkaline phosphatase, glucose 6-phosphatase, and adenosine triphosphatase activities in the upper small intestine of germfree rats were, respectively, 2.3-, 2.9-, and 1.7-fold higher than those in conventional rats. Similar to the results of these enzymes, sucrase, maltase, trehalase, and lactase activities in the upper small intestine of germfree rats were, respectively, 1.6-, 1.5-, 2.3-, and 1.8-fold higher than those in conventional rats. In various gnotobiotic rats, enzyme activity levels were intermediate between those in germfree and conventional rats. These findings suggest that those enzymatic activities are strongly depressed by the association with the indigenous microorganisms in the epithelial mucosa of the upper small intestine of rats. The levels of pyruvate kinase, hexokinase, and lactate dehydrogenase activities were highest, respectively, in the stomach, cecum, and the upper small intestine and cecum in all parts of the gastrointestinal tracts in various kinds of gnotobiotic, conventional, and germfree rats. It was also shown that six kinds of gastrointestinal bacteria, including lactobacilli, significantly depressed the enzyme activity levels to levels between those of the germfree and conventional rats in the upper small intestine of gnotobiotic rats.
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PMID:Intestinal enzyme activities in germfree, conventional, and gnotobiotic rats associated with indigenous microorganisms. 20 6

A genetically conditioned mouse model of exocrine pancreatic insufficiency (epi) has been used to study the effect of the absence of lumenal proteases on small intestinal mucosal proteins. The small bowel was divided into eight equal segments. Enzyme activity was increased only in the first three segments in the case of maltase, sucrase, and lactase (all mol wt above 200,000). Alkaline phosphatase (mol wt 145,000), trehalase (mol wt 95,000), and peptidase (mol wt 175,000) activities were unaffected in proximal segments from epi mice. Proximal brush border proteins were identified and measured quantitatively by sodium dodecyl sulfate acrylamide gel electrophoresis. Those enzymes with increased activity were associated with increased amounts of protein in epi mice. Double labeled studies of protein turnover revealed a longer half-life for large brush border proteins (mol wt above 175,000) in epi mice than in normal mice. Enterokinase activity (a marker for duodenal mucosa) was nearly absent from the duodenum of epi mice. Receptors for the intrinsic factor-vitamin B12 complex (markers for ileal mucosal) were present in the ileum equally in normal and in epi mice. Enterokinase activity can be induced in epi mice by feeding its substrate trypsinogen, but not by trypsin or chymotrypsinogen. Epi mice thus retain the ability to synthesize enterokinase. Pancreatic proteases play an important role in the turnover of certain large mucosal proteins and in the induction of enterokinase.
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PMID:Effect of exchange exocrine pancreatic insufficiency on small intestine in the mouse. 20 83

Physiological bases of digestion and absorption of carbohydrates are reviewed, as a preliminary step, in order to draw a general scheme of its patholophysiology. Clasification of different types of carbohydrate malabsorption is presented. Various exploration methods are discussed in terms of autors' own experiences. Relationship between a sugar screening test, faecal lactic acid contents and a simplified lactose tolerance test, is described in detail. Systematic diagnoses of these diseases are established. Different clinical pictures are reviewed. It is not yet well defined if a starch malabsorption can be caused by either a primary or secondary duodenal amylase deficiency. The clinical forms of congenital sucrose-isomaltose intolerance may be more attenuated than its classical form; incertain cases, secondary sucrose intolerance may also be present due to mucosa anatomic lesions. Maltose malabsorption has no clinical implications. As compared to other alpha-glycosidades, the trehalase activity has been not more affected by not using trehalose in feeding. Primary congenital lactase deficiency is not frequent, whereas secondary forms as much more usual and appear, in primary malabsorption syndromes and in the coeliac disease, very often along with clinical tolerance to lactose. In Spain, lactose nonabsorbers in 16.5% for adults 11.2% for adolescents and 18.3% for children, meaning, that it is being favored by environmental factors in the latter. The unspecified sugar malabsorption during the child's first year is still the most frequent cause of carbohydrate intolerance in children and, although certain progress has been achieved in its diagnosis and therapy, its pathogenic mechanism is not satisfactorily known yet.
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PMID:[Malabsorption of carbohydrates in children (author's transl)]. 23 44

The activities of rat intestinal enzymes, sucrase, lactase, maltase, trehalase, gamma-glutamyltransferase, leucylnaphthylamide-hydrolyzing activity, and the transport system for glucose follow diurnal rhythms on ad libitum and restricted feeding regimes. In response to 6 days of restricted feeding, food available between 1400 and 1800 Eastern Standard Time, all rhythms shifted in time and the daily levels of activities were changed. Alkaline phosphatase activity followed a diurnal rhythm only in restricted fed animals. In restricted fed rats several activity patterns were observed, some with short periods of maximum activity, 3 h or less, and some with plateaus of maximum activity, 5-9 h long. In respect to the time of day of the synchronizer, sucrase peaked before feeding, glucose transport peaked during feeding, alkaline phosphatase peaked after feeding, and the other enzymes had higher levels of activity before, during and after feeding. The effect of restricted feeding on the daily activity levels were: a decrease in leucylnaphthylamide-hydrolyzing activity, no change in alkaline phosphatase, and increases in the others. These enzyme and transport systems exhibit a large amount of individual regulation or control as reflected by the lack of a uniform activity pattern and response to the synchronizer, and the variation in direction and magnitude of the adaptations to restricted feeding.
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PMID:Effect of changes in feeding schedule on the diurnal rhythms and daily activity levels of intestinal brush border enzymes and transport systems. 24 Apr 40

The activity of the membrane-bound enzymes of the microvillous zone of the entreocytes (maltase, sucrase, trehalase, lactase, cellobiase, alkaline phosphatase and leucylaminopeptidase) was studied in mucosal smears from the proximal jejunum, ileum, caecum and sigmoid flexure in a group of control (C) (8) and germ-free (GF) (7) rabbits. The trypsin and chymotrypsin activity of the contents of the ileum, caecum and sigmoid flexure was studied in 6 C, 5 GF and 5 monocontaminated (MC) rabbits. In summing up it can be stated that the individual membrane-bound enzymes have a different gradient in the various intestinal segments of C and GF rabbits and that they differ reciprocally in character. The maximum statistically significant differences between GF and C rabbits were found in the ileum; in the jejunum they were somewhat smaller and in the caecum smaller still (in this localization the difference was C versus GF). Striking differences in the proportion of the individual disaccharidases were found inthe jejunum and ileum of C rabbits compared with GF rabbits, in which, in both these segments of small intestine the relationship maltase greater than sucrase greater than trehalase greater than lactase was preserved. The proteolytic activity of the intestinal contents likewise had a different gradient character in C, MC and GF rabbits. The maximum activities (especially trypsin) were found in MC animals. The microbial flora is one of the factors regulating the enzymatic activities of the microvillous zone of the enterocytes and it also significantly influences the proteolytic activity of the intestinal contents. This influence is particularly marked in the distal part of the alimentary tube.
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PMID:Digestive enzymes of the mucosa of the small intestine and trypsin and chymotrypsin proteolytic activity of the intestinal contents of germ-free, monocontaminated and conventional rabbits. 35 55


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