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)

We studied 24 patients with end-stage chronic renal failure not treated with hemodialysis (CRF1) and 16 patients on regular hemodialysis (CRF2), to investigate the digestive, absorptive and morphological aspects of the small intestinal mucosa. Serum d-xylose test and biochemical parameters of absorption (serum calcium and proteins) were determined. Jejunal mucosal biopsies were obtained and tissue homogenates assayed for disaccharidases (sucrase, maltase and lactase) and dipeptidases (glycyl-glycinase, leucyl-glycinase and leucyl-aminopeptidase). Histological changes were classified according to the severity of abnormality and compared with biopsies obtained from control subjects. Serum d-xylose test, calcium and proteins were normal in patients with CRF. Maltase specific activity was higher in CRF1 than in controls (p less than 0.05). Lactase and leucyl-aminopeptidase showed a tendency to decrease in CRF, but this difference did not reach statistical significance. Sucrase, glycyl-glycinase and leucyl-glycinase specific activity in CRF was similar to the control group. Histological changes of the small intestinal mucosa of mild to moderate degree were noted in 68% of patients with CRF vs 36% in control subjects (p less than 0.01). No significant difference was noted in the incidence of absorptive, enzymatic (with the exception of maltase) and histological changes between the two groups of patients with CRF. These changes are not influenced by hemodialysis, a long-term treatment averaging 6 months, they appear to represent primary manifestations of CRF and may be related to the nutritional status of patients with CRF.
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PMID:Small intestinal function and structure in patients with chronic renal failure. 339 24

The relationship between primary lactase deficiency, the amount of lactose in the diet, and symptoms of intolerance continues to be debated. Primary adult lactase deficiency is common with a worldwide occurrence of near 70%. Lactase-deficient individuals malabsorb lactose but may or may not show intolerance symptoms. The development of symptoms appears to depend on the dose of lactose ingested, whether it is accompanied by a meal or other food, rate of gastric emptying, and small intestine transit time. Lactose loads of 15 g or greater produce symptoms in the majority of lactase-deficient persons. However, when lactose loads of up to 12 g are fed, symptoms can be minimal or absent. Tolerance to yogurt, acidophilus milk, and other microbe-containing dairy foods has been suggested and is thought to be due to either a low lactose content or in vivo autodigestion by microbial beta-galactosidase. Up to 20 g of lactose in yogurt is tolerated well by lactase-deficient persons. Associated with the consumption of yogurt is a three- to fourfold reduction in lactose malabsorption as compared with similar lactose consumption in milk. Improved lactose digestion appears due to autodigestion by microbial beta-galactosidase. This enzyme may be released from yogurt culture by gastric or bile acid digestion. Feeding yogurt that was pasteurized following fermentation, with only trace amounts of microbial beta-galactosidase activity, results in a threefold increase in lactose malabsorption as compared with feeding yogurt with a viable culture. However, pasteurized yogurt also is tolerated well by lactase-deficient persons, suggesting that tolerance of up to 20 g of lactose in yogurt may be independent of lactose malabsorption. The enhanced lactose absorption and tolerance observed with yogurt feeding are not apparent when unfermented acidophilus milk or cultured milk are fed.
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PMID:Milk intolerance and microbe-containing dairy foods. 355 56

Seventy-two hour starvation in neonatal rabbits was studied. Fasted animals received no feeds, only water every 8 h for 72 h. Fed animals were suckled by the dam. There was no difference in birth weight, serum albumin, blood urea nitrogen, electrolytes, or urine specific gravity between fed and fasted animals. Weight at 72 hr was less in fasted (p less than 0.01) than fed rabbits. Serum cortisol (p less than 0.05) and corticosterone (p less than 0.01) levels were higher in the fasted group. Proximal and distal small bowel homogenates had less DNA and protein (p less than 0.01) in the fasted group, but the protein/DNA ratio was the same in the proximal and distal small bowel homogenates from both groups. Sucrase (E.C.3.2.1.26) specific activity was significantly increased in proximal small bowel homogenates from the fasted group (p less than 0.01) but was the same in distal small bowel homogenates from both groups. Sucrase total activity per proximal segment was the same in fed and fasted animals but was significantly less per segment in distal small bowel homogenates from fasted animals. Alkaline phosphatase (E.C.3.1.3) total and specific activity was decreased in proximal (p less than 0.01) and distal (p less than 0.05) small bowel homogenates from the fasted group. Lactase (E.C.3.2.1.23) total activity was decreased in proximal and distal (p less than 0.01) small bowel homogenates from the fasted group but lactase specific activity was unchanged. Thus, a brief period of malnutrition in neonatal animals can result in a variety of regional functional changes in the gastrointestinal mucosa.
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PMID:Short-term malnutrition in neonatal rabbits. I. Brush border enzymes. 368 82

Human lactase purified from detergent extracts of the total membrane fraction of postmortem jejunum by means of monoclonal immunoadsorbent chromatography appears to be a dimer of subunits identical in Mr (160K). Trypsin or papain removes a small hydrophobic anchoring peptide from each subunit to give a hydrophilic enzyme which no longer interacts with detergent micelles. Lactase hydrolyzes, besides lactose, cellobiose and the synthetic substrates, 4-methylumbelliferyl-beta-galactoside and beta-glucoside, as well as phlorizin; but it does not hydrolyze glucocerebroside. Phlorizin hydrolase is associated with lactase under all conditions investigated; coincident staining on immunodiffusion and immunoelectrophoresis, coincident elution on immunoadsorbent chromatography and on gel filtration in a dissociating buffer, and correlated reduction in activity in lactase-nonpersistent individuals. Adult and infant lactases are indistinguishable by titration or immunodiffusion against polyclonal rabbit antibodies. Adult individuals low in lactase activity also show a corresponding reduction in cross-reacting material. These observations suggest that lactase persistence is due to the continued synthesis of the infant enzyme.
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PMID:Human lactase and the molecular basis of lactase persistence. 392 64

Developmental profiles describing the expression of lactase, alpha-glucosidase, and alkaline phosphatase activities have been determined quantitatively in mouse jejunal enterocytes during migration over villi and Peyer's patch lymphoid tissue. The predicted maximal lactase and alpha-glucosidase activities expressed by enterocytes migrating over Peyer's patch follicles were about one-quarter and one-half of values found in control villi. Alkaline phosphatase activity was, on the other hand, one third greater in Peyer's patch compared with villus enterocytes. Expression of lactase and alpha-glucosidase activities was initially less in enterocytes migrating along interfollicular compared with control villi. Subsequent increase in hydrolase activities occurred during the later stages of enterocyte migration over interfollicular villi. Lactase activity in athymic mice Peyer's patch enterocytes was identical to that recorded for control mice. The corresponding value for villus lactase was, however, only half that found in control tissue. Factors produced locally in lymphoid follicles are probably responsible for selective effects on enterocyte differentiation.
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PMID:Selective expression of brush border hydrolases by mouse Peyer's patch and jejunal villus enterocytes. 393 May 23

To elucidate the mechanism of the developmental decline in intestinal lactase activity at weaning, we examined lactase synthesis in suckling and adult rats. Lactase was purified to homogeneity from pooled intestines of newborn rats and used to raise a monospecific antibody. Using this antibody, we developed a quantitative immunoprecipitation assay for lactase. Intestinal microvillus membrane proteins were labeled in 15-day and adult rats by intraluminal pulse-chase with 3H-leucine, and newly synthesized lactase quantified by immunoprecipitation. When lactase synthesis was expressed as the quantity of microvillus membrane lactase synthesized relative to total microvillus membrane protein synthesized, a significantly greater proportion of 3H-leucine incorporation into lactase was demonstrated in the suckling animals. No structural differences between newly synthesized suckling and adult lactase were observed when they were compared by SDS-polyacrylamide gel electrophoresis and fluorography. These data suggest that a change in the rate of lactase synthesis plays a role in the postweaning decline in enzyme activity.
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PMID:Intestinal lactase synthesis during postnatal development in the rat. 393 Oct 41

To characterize the mechanisms leading to dietary evoked increases of lactase and sucrase activities by carbohydrates, we performed a quantitative comparison of the effects of lactose and sucrose on the corresponding disaccharidases in the jejunum of 2-month-old rats. For 7-10 days the rats were fed a low-starch (5 cal%), high-fat (73 cal%) diet, and for various periods of time (3-72 h) were given an isocaloric sucrose or lactose (20, 40, or 70 cal%) diet. Lactase and sucrase activities in jejunal homogenates were significantly increased within 3 h after the initial feeding of the sucrose (40 cal%) diet. After 3 h of feeding the sucrose diet, sucrase activity gradually increased and reached its maximum at 24 h, whereas lactase activity did not exhibit further change. Increased intake of sucrose led to an increase of lactase and sucrase activity. Within a range of doses of digestible amounts of lactose, the effect of diet containing lactose on these disaccharidase activities was similar to the effect of the diet containing sucrose. This similarity suggests the important role of the common constituent sugar, i.e., glucose. Further, analyses of response to these disaccharides along the villus-crypt axis revealed that the increase of lactase activity occurs at a more apical and broader locus of cohort of epithelial cells along the height of the villus than that of sucrase, suggesting that different mechanisms are involved in dietary regulation of lactase and sucrase.
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PMID:Dietary regulation of intestinal lactase and sucrase in adult rats: quantitative comparison of effect of lactose and sucrose. 393 60

An increased prevalence of osteoporosis has been observed in lactase-deficient subjects. This association has been attributed to an avoidance of calcium-containing dairy products by lactase-deficient subjects and/or an adverse affect of lactose malabsorption on calcium absorption. Because the lactose in yogurt can be digested and absorbed by hypolactasic subjects, we tested the ability of lactase-deficient subjects and controls to absorb calcium from milk and yogurt. Subjects ingested 270 mg of Ca plus 45Ca in 250 g of milk or 147 g of commercial, unflavored yogurt, and blood radioactivity was assessed at intervals over 24 h. Based on the areas under the blood radioactivity curves, lactase-deficient subjects and controls absorbed calcium equally well from yogurt and milk. Lactase-deficient subjects absorbed 45Ca from both sources at least as well as did the controls. While we found no evidence to indicate that calcium in yogurt is better absorbed than calcium in milk, yogurt remains an excellent source of calcium because this fermented product is well tolerated by lactase-deficient subjects.
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PMID:Absorption of calcium from milk and yogurt. 393 56

Lactose malabsorption is not a cause of diarrhea during phototherapy. Jaundiced neonates under phototherapy develop diarrhea or loose stools during the treatment. These phenomena were attributed to an induced lactase deficiency caused by bilirubin breakdown products. We investigated lactose malabsorption in 59 neonates--29 normals and 30 jaundiced under phototherapy. Five-hour hydrogen breath tests were performed. Preprandial and postprandial (at 30, 60, 120, 180, 240, and 300 min) expired air samples were analyzed for hydrogen. Ten controls and five jaundiced neonates had positive hydrogen breath tests. Eighteen controls and 16 neonates under phototherapy had preprandial hydrogen (concentrations above 5 ppm). In our hands, lactase deficiency and lactose malabsorption were not induced by phototherapy. Lactase deficiency is therefore not the cause of diarrhea associated with phototherapy.
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PMID:Lactose malabsorption is not a cause of diarrhea during phototherapy. 398 20

Adenyl cyclase activity in intestinal membranes has been studied during development in the rabbit fetus from fetal day 17 to 10 days postnatally and in the human fetus from the 10th to the 17th wk of gestation. In the rabbit, the enzyme was already present by fetal day 17 and showed a fourfold peak rise in specific activity by 22 days. By 28 days, the specific activity had fallen toward adult levels and remained constant throughout gestation and the 1st wk of life. Fluoridestimulated activity showed a similar curve, and was 2.5-5 times the basal values. Activities in jejunum and ileum were comparable at all time points studied. Phosphodiesterase activity did not change during gestation. When fetal intestinal segments were incubated in vitro with purified cholera enterotoxin, adenyl cyclase activity in subsequently prepared membranes was increased two- to threefold. This level was not regularly further elevated by fluoride ion. Lithium ion inhibited both the basal and fluoride-stimulated enzyme activity in membranes prepared from rabbit fetuses at term. Lactase activity (reflecting the development of the microvilli) in either whole intestinal homogenates or in the membrane fractions showed a differnet pattern of development, with a rise beginning on fetal day 24 and a plateau just after birth. In intestinal membranes prepared from human fetuses, the activity of both basal and fluoride-stimulated adenyl cyclase tripled from the 10th to the 17th wk of gestation. The data both in the rabbit and in man show that intestinal adenyl cyclase is capable of responding to cholera enterotoxin quite early in gestation. In the rabbit, this occurs before the time of appearance or ville or of an enzyme marker (lactase) for microville. The results support the concept that adenyl cyclase is present in plasma membrane other than the brush border.
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PMID:Development of intestinal adenyl cyclase and its response to cholera enterotoxin. 435 79


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