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PubMed2000

The prevalence and severity of intestinal disaccharidase deficiency in human immunodeficiency virus-infected subjects.

BACKGROUND: Gastrointestinal symptoms are distressing features of human immunodeficiency virus (HIV) infection, and management is often empirical, including withdrawal of dietary lactose. We assessed the prevalence and severity of intestinal disaccharidase deficiency in vitro and in vivo. METHODS: Fifty-four HIV-seropositive patients (19 HIV well +/- mild diarrhoea, 7 acquired immunodeficiency syndrome (AIDS) well, and 28 AIDS with diarrhoea) were studied with a combined non-invasive absorption-permeability-disaccharidase test that enables quantitative assessment of the rate of intestinal hydrolysis of lactose, sucrose, and palatinose. Thirty patients had jejunal biopsy specimens suitable for histomorphometric assessment, and 36 had in vitro disaccharidase activity measurement. RESULTS: Patients with HIV (with mild diarrhoea) and AIDS (with and without severe diarrhoea) had frequent but mild histomorphometric changes in jejunal specimens. This was associated with frequent (21%-100%) and often severe in vitro jejunal disaccharidase deficiency. In vivo hydrolysis of lactose, sucrose, and palatinose was impaired in 25%-75% of patients, apart from HIV well patients, who were normal. The prevalence of the in vivo lactase and sucrase deficiency was significantly (P < 0.006) lower than in vitro and severe in about 30%. CONCLUSIONS: Intestinal disaccharidase deficiency is common both in vitro and in vivo in HIV-seropositive patients but sufficiently severe to consider lactose withdrawal only in about a quarter of the patients with AIDS and diarrhoea.

Acquired Immunodeficiency Syndrome↗
PubMed2001

Intestinal disaccharidase deficiency without villous atrophy may represent early celiac disease.

BACKGROUND: Intestinal disaccharidase activities are decreased in untreated celiac disease and also in other conditions without villous atrophy. Of 908 patients examined for suspected malabsorption, 37 (4.1%) had generalized disaccharidase deficiency without villous atrophy. The aim was to determine if generalized disaccharidase deficiency without villous atrophy represented latent celiac disease. METHODS: Case notes and histology of the 37 patients were reviewed. History and blood investigations including antigliadin and endomysial antibodies were checked. Where celiac disease was suspected, endoscopic duodenal biopsies for histology and disaccharidase estimation were repeated. RESULTS: Of the initial 37 patients, 6 patients had had repeat endoscopic biopsies; one having celiac disease. A further 18 patients were reviewed. The remainder declined further investigation. Eight had repeat endoscopic duodenal biopsies; one had celiac disease. Two with positive celiac serology also had enteroscopy with jejunal biopsies; both had celiac disease. CONCLUSIONS: At least 11% of patients with generalized disaccharidase deficiency without villous atrophy develop celiac disease. Enteroscopic biopsies from distal duodenum and proximal jejunum should be considered as the next investigation if endomysial or antigliadin antibodies are positive.

Adult↗
PubMed1977

Interaction between dietary carbohydrates and intestinal disaccharidases in experimental diarrhea.

The effects of carbohydrate intake on jejunal disaccharidases in rats with chronic mannitol-induced, osmotic diarrhea were studied. Weanling rats were force-fed 5 ml/100 g of body weight of water of 20% mannitol (w/v 1300 mOsm) daily for up to 14 days. Diets containing 70% of either starch, sucrose, glucose, or 20% lactose with 50% starch were fed ad libitum. Mannitol-fed rats had increased water intake and diarrhea. They gained weight, but less than controls. The levels of intestinal disaccharidases in mannitol-fed rats were related to dietary carbohydrate intake. Seven days of mannitol treatment led to lactase and sucrase deficiencies in rats fed starch whereas jejunal maltase and alkaline phosphatase were unchanged. Deficiencies in lactase and maltase but not in sucrase were induced when rats were fed a sucrose diet, while a decrease only in sucrase occurred in rats fed a lactose-starch diet. Rats with mannitol-induced diarrhea fed a glucose diet had reduced levels of all disaccharidases. The changes in intestinal disaccharidases were not associated with alterations in the number of epithelial cells or ultrastructural abnormalities. 3H-thymidine incorporation into DNA following 7 days of mannitol treatment was similar to water-fed controls. Absorptive epithelial cells were not damaged and the microvilli were normal in height and appearance. These data suggest that the levels of specific disaccharidases show and enhanced dependence upon the corresponding dietary substrates during diarrhea induced by an osmotic load.

Alkaline Phosphatase↗
PubMed1985

Interaction of intestinal disaccharidases with phospholipids: effect of cholesterol.

Although the rat intestinal brush border disaccharidases are the most easily solubilized protein components, the nature of the lipid-protein interactions in the membrane is incompletely understood. Phospholipid vesicles were prepared using the lecithin fraction from brush border membranes and synthetic lecithins. Addition of cholesterol to brush border lecithins enhanced the binding of disaccharidases, but not of alkaline phosphatase. The addition of cholesterol to synthetic lecithin vesicles enhanced the binding of disaccharidases only when added above the transition temperature of the lecithin used. The maximal effect occurred at an equimolar ratio of lecithin to cholesterol. Binding of disaccharidases to phospholipid vesicles was independent of charge or the nature of the polar head group, and the enzyme was inserted so that the catalytic domain was excluded from the lipid matrix. These results demonstrate that membrane attachment of disaccharidases is hydrophobic, involving primarily fatty acyl chains and an interaction with cholesterol. The membrane interaction does not seem to affect enzyme activity.

Animals↗
PubMed1990

Effect of zinc-deficient diet of varying duration on intestinal disaccharidase activity in the rat.

To determine whether zinc has a specific role on weight gain and intestinal disaccharidase activity, 42 male Sprague-Dawley rats were assigned to one of seven groups (n = 6 each). These were a baseline control group (0) that was killed to analyze initial intestinal disaccharidase (sucrase and maltase) activity, a second group (A) fed a zinc-deficient diet for 1 week, a third group (B) pair-fed control for A, a fourth group (C) fed a zinc-deficient diet for 2 weeks, a fifth group (D) pair-fed control for C, a sixth group (E) fed a zinc-deficient diet for 3 weeks, and a seventh group (F) pair-fed control for E. All experimental groups received distilled deionized drinking water, whereas control groups received zinc-enriched (25 micrograms of zinc/ml) distilled deionized water. Water was given ad libitum. After killing, the mucosa of the proximal half of the small intestine was analyzed for protein and disaccharidase activity, and liver, kidney, and heart were analyzed for zinc concentration. Protein content and disaccharidase activity of the jejunal mucosa in the experiment and control groups did not differ significantly. However, animals on the zinc-deficient diet demonstrated mildly depressed growth rates that were proportional to the duration of the experiment, and significantly lower zinc concentration in the kidney in the experimental groups. The data indicate that administration of a zinc-deficient diet for up to 3 weeks did not result in significant changes in intestinal mucosa protein content or in disaccharidase activity.

Animals↗
PubMed1990

Activity of duodenal disaccharidases in relation to normal and abnormal mucosal morphology.

Endoscopic duodenal biopsy specimens from 100 predominantly adult Caucasian patients under investigation for gastrointestinal symptoms were used to establish reference ranges for lactase, sucrase, and maltase in the duodenum. Duodenal and jejunal disaccharidase values were compared and the association between disaccharidase activity and morphology in the duodenum was examined. Mean lactase activities were about 40% lower in the duodenum compared with the jejunum; maltase was reduced to a lesser extent; and sucrase activities were much the same in the two sites. Lactase deficiency was found in 24 patients of whom 14 (58%) had duodenal disease. The presence of moderate to severe duodenal lesions was associated with a significant decrease in all disaccharidase activities, while only lactase was reduced in mild lesions. Twelve patients had normal lactase activity, despite the presence of duodenal disease. It is concluded that specific reference ranges for duodenal mucosal disaccharidase activity are required as this is less than that of jejunum. Reduced duodenal disaccharidase activity is usually but not invariably associated with morphological abnormality.

Adolescent↗
PubMed1978

Disaccharidase deficiency in infants with cow's milk protein intolerance. Response to treatment.

7 infants, aged 5 weeks to 11 months, with clinically documented intolerance to cow's milk protein, chronic diarrhea, and failure to thrive, underwent small intestinal (peroal, suction) biopsy before and after withdrawal of milk proteins. Mucosal specimens were examined by light microscopy and assayed for disaccharidase activities. In all patients, moderate to severe mucosal changes were presented, associated with marked inflammation of lamina propria and damages to the brushborder. Disaccharidase activities (lactase, sucrase, maltase and palatinase) were markedly depressed in all. Follow-up biopsies were obtained in 6 infants, after 3-5 months on a milk-protein-free diet. At the time of the second biopsy, the disaccharidase activities had risen significantly and histologic improvement had occurred in each instance. In infancy, intestinal mucosal lesions due to intolerance to cow's milk protein are histologically indistinguishable from those seen in gluten-sensitive enteropathy and are associated with marked secondary disaccharidase deficiencies. Following therapy, the activity of the disaccharidases become normal or near normal prior to the complete morphologic recovery of the small intestinal mucosa.

Animals↗
PubMedDate not supplied

Total parenteral nutrition energy composition affects small intestinal disaccharidase activity in the newborn miniature pig.

Total parenteral nutrition (TPN) decreases disaccharidase activity in the small intestine of humans and miniature piglets. The possibility, however, that specific components of TPN (eg, the energy mix) will increase disaccharidase activity has largely been unexplored. The identification of such components would be particularly useful in the treatment of premature infants with immature gastrointestinal tracts and patients with small intestinal mucosal disease associated with decreased disaccharidase activity. To determine whether the TPN energy composition affects small intestinal disaccharidase activity, 7-day-old miniature piglet littermates were randomized to receive TPN containing either glucose (group G) or glucose and fat (group G/F) as the nonnitrogen energy source(s). The TPN regimens were isonitrogenous and isoenergetic. The piglets were not allowed oral intake during the 7 days they were maintained on TPN. At 14 days of age the piglets were killed and the small intestines analyzed for weight, protein, DNA, and disaccharidase activity. Body weight was similar between groups at both the beginning and end of the study. The TPN regimen did not affect small intestinal weight of protein and DNA content. However, jejunal and ileal sucrase and ileal maltase activities (mumol/min.kg body wt +/- SD) were greater in group G than those in group G/F (28 +/- 9 vs 19 +/- 11, p = 0.04; 13 +/- 7 vs 7 +/- 4, p = 0.037; and 31 +/- 8 vs 19 +/- 10, p = 0.0088, respectively). No differences in lactase activity were noted between groups.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1995

Intestinal disaccharidase activity in human immunodeficiency virus disease.

BACKGROUND: The relationship between disaccharidase activity, progression of human immunodeficiency virus (HIV) disease, and diarrhoea and weight loss was investigated. METHODS: Forty-six HIV-positive patients ingested a solution of lactose, palatinose, sucrose, and lactulose after 24 h of dietary exclusion and overnight fasting, after which urine was collected for 10 h. Urinary disaccharide (activity) ratios-lactose/lactulose (L/LL), palatinose/lactulose (P/LL), and sucrose/lactulose (S/LL)-were measured by thin-layer chromatography. RESULTS: There was a significant decrease in disaccharidase activity (L/LL, P/LL, and S/LL) with advancing clinical stage of HIV disease (p < 0.05, Wilcoxon rank sum test) as well as decreasing CD4 count (p < 0.05, Spearman correlation). Patients with weight loss/diarrhoea also had significantly (p < 0.05) decreased disaccharidase activity compared with control but not as compared with AIDS patients. Anti-retroviral therapy did not influence disaccharidase activity. CONCLUSION: Impairment of disaccharidase activity occurs with advancing HIV disease, but its role in HIV patients with weight loss and diarrhoea remains to be determined.

Adult↗
PubMed1992

Disaccharidase activity in the small intestine of susceptible and resistant mice after primary and challenge infections with Giardia muris.

The activities of four disaccharidases were examined in resistant (C57Bl/6) and susceptible (C3H/HeN) mice during the primary infection with Giardia muris and after challenge with either trophozoite extract or cysts. Significant decreases in lactase, sucrase, trehalase, and maltase activities in C57Bl/6 mice and lactase and sucrase activities in C3H/HeN mice in the anterior 25% of the small intestine were observed on day 10 after infection. The activities of maltase, sucrase, trehalase, and lactase in the jejunum of C3H/HeN mice were significantly reduced after challenge with trophozoite extract, when compared with the uninfected or infected, but not challenged animals. Decreases in enzyme activities of C3H/HeN mice were evident as early as 12 hours after challenge with the extract. The resistant C57Bl/6 mice showed little change in disaccharidase activity after challenge with trophozoite extract. On the other hand, challenge with cysts resulted in a few decreases in disaccharidase activities in both strains of mice: C57Bl/6 mice showed decreases in the duodenum, while disaccharidases of C3H/HeN mice had lower activity more posteriorly. Thus, challenge with parasite antigen results in a more severe disaccharidase deficiency in susceptible hosts when compared with resistant ones.

Animals↗
PubMedDate not supplied

Comparison of duodenal and jejunal disaccharidase levels in patients with non ulcer dyspepsia.

AIMS: This study was conducted to compare the duodenal and jejunal disaccharidase levels in the same individual with duodenal ulcer or non ulcer dyspepsia. METHODS: Thirty seven patients (duodenal ulcer--11, non-ulcer dyspepsia--26) were included in the study. Endoscopic biopsy samples were obtained from jejunum and duodenum using pediatric colonofibroscope. RESULTS: Levels of jejunal disaccharidases were significantly higher than the duodenal disaccharidases. CONCLUSIONS: An estimate of jejunal disaccharidases can be had by multiplication of duodenal disaccharidased by a factor 1.48 for lactase, 1.50 for sucrase and 1.56 for maltase.

Disaccharidases↗
PubMed1978

Parallel between circadian rhythms of intestinal disaccharidases and foot intake of rats under constant lighting conditions.

The relationship between the circadian rhythmic changes in the disaccharidase activities of the small intestine and the circadian feeding pattern was investigated in rats kept in the dark or in the light continuously for 4 weeks. Rats kept continuously in the light and fed ad libitum showed no rhythmic change in food intake or disaccharidase activities, but when they were only fed during a restricted time of day, their disaccharidase activities showed rhythmic changes with higher activities around the feeding time. In contrast, rats kept continuously in the dark and fed ad libitum showed circadian variations in food intake and disaccharidase activities essentially similar to rats kept under the normal light-dark lighting schedule. These findings show that the rhythm of disaccharidase activities is synchronized with the feeding rhythm, not with the lighting rhythm.

Animals↗
PubMedDate not supplied

Amniotic fluid disaccharidases in the prenatal detection of cystic fibrosis.

Intestinal disaccharidases in amniotic fluid were studied in 41 pregnancies with a recurrence risk for cystic fibrosis (CF). In 11 out of 13 pregnancies with CF fetuses the maltase and sucrase activities were either below the control range (8 cases) or below the 10th percentile of control values (3 cases). Trehalase and lactase were slightly less informative indicators of CF. Of the other 28 pregnancies 3 had low amniotic fluid activities of several intestinal enzymes and were terminated, 12 resulted in the birth of a healthy child and 13 are continuing. The findings in fetal CF suggest an impairment of the defaecation of intestinal contents into the amniotic fluid. Reduced or low amniotic fluid disaccharidase activities were also found in other fetal disorders with demonstrated or presumed intestinal anomalies: e.g. anal atresia (2 cases), anencephaly (3 our of the 7 cases), trisomy 13 (5 cases), trisomy 18 (3 of the 5 cases) and trisomy 21 (19 of the 22 cases). Reduced amniotic fluid disaccharidase activities, although not specific for CF, are highly informative in pregnancies at high risk for CF. Using the 10th percentile of the normal range for amniotic fluid disaccharidase activities as an action line, the sensitivity of CF detection is estimated at 80 to 90 per cent, which could in high risk pregnancies reduce the risk of having another affected child from 1 in 4 to 1 in 20.

Amniocentesis↗
PubMed1994

Disaccharidase activities in pregnant and lactating rats.

The changes in intestinal disaccharidase activities in pregnancy and lactation could be explained as a result of an adaptation to the energy demands of each reproductive stage. To examine these changes, disaccharidase activities (lactase, sucrase, maltase, and trehalase) were measured in the jejunum and ileum of virgin, pregnant and lactating Wistar rats. Minor changes in disaccharidase activities were observed in pregnancy, whereas an increase of disaccharidase activities per small intestine length normalized to body mass was observed in lactation.

Animals↗
PubMed1992

Dietary-induced increases of disaccharidase activities in rat jejunum.

A study was carried out to examine whether the responsiveness of small intestinal epithelial cells to dietary carbohydrate varied during the daily 24 h cycle. The effect of sucrose on disaccharidase activities was compared during a period of decreasing disaccharidase activities, i.e. between 22.00 and 10.00 hours, and increasing disaccharidase activities, i.e. between 10.00 and 22.00 hours, in the jejunum of 7-week-old-rats. Rats were fed on a low-starch, high-fat diet (Lst; starch 5 and fat 73% of gross energy), or a high-starch, low-fat diet (Hst; starch 70 and fat 7% of gross energy). Both dietary groups exhibited typical diurnal variations in jejunal sucrase (EC 3.2.1.48), maltase (EC 3.2.1.20) and lactase (EC 3.2.1.23) activities, exhibiting a peak around 22.00 hours and a trough at approximately 10.00 hours. When rats were fed on diet Lst for 7 d and then force-fed on an isoenergetic sucrose diet (S; sucrose 40 and fat 37% of gross energy) for 6 or 12 h they exhibited increased sucrase, maltase and lactase activities compared with rats fed on diet Lst. The absolute increase in disaccharidase activities was similar regardless of the time diet S was given or whether rats were killed at 10.00 hours or at 22.00 hours. Analyses of sucrase and lactase activities along the villus-crypt columns showed that the distribution of cell cohorts that responded to diet S was not influenced by the time of introduction of diet S. These findings suggest that small intestinal epithelial cells possess the ability to respond to dietary carbohydrate throughout the daily 24 h cycle.

Animals↗
PubMed1998

Effects of diabetes and hyperglycemia on disaccharidase activities in the rat.

BACKGROUND AND METHODS: To elucidate the effect of hyperglycemia on disaccharidase activities, the specific and total activities of the disaccharidases were measured in the intestinal mucosa and kidney cortex of diabetic and hyperglycemic rats. The diabetes was induced with an intraperitoneal injection of streptozotocin (60 mg/kg). The rats were made hyperglycemic with an intravenous instillation of a solution containing 40% dextrose monohydrate at a rate of 1.5 ml/h for 24 h. RESULTS: The blood glucose level was 387+/-45 mg/dl and 382+/-35 mg/dl (mean +/- standard deviation) in diabetic and hyperglycemic rats, respectively. In diabetic rats the intestinal maltase, sucrase, and lactase activities were significantly higher than those in control rats. Similarly, disaccharidase activities in hyperglycemic rats were significantly higher than those in control rats. The renal maltase activity in diabetic rats was significantly lower than that in control rats. The maltase activity in hyperglycemic rats, however, was not significantly different from that in control rats. CONCLUSIONS: These results suggest that 1) hyperglycemia directly increases the activities of intestinal maltase, sucrase, and lactase; 2) hyperglycemia does not influence renal maltase activity; and 3) hyperglycemia is partly responsible for increased activities of intestinal disaccharidases in diabetes mellitus.

Animals↗
PubMed2003

Disaccharidase activities in Belgian children: reference intervals and comparison with non-Belgian Caucasian children.

AIM: To establish reference values for disaccharidase activities in Belgian children and to compare enzyme activities with those of non-Belgian Caucasian children. METHODS: Data from Belgian children who had undergone endoscopic jejunal biopsies (1994-2000) for suspected malabsorption were reviewed. The patients were divided into three groups based on histology: (A) normal (n = 201), (B) moderate changes (n = 58) and (C) (sub)total atrophy (n = 14). The 95% reference limits for disaccharidase activities (U/g protein) were calculated for group A after exclusion of patients with a positive hydrogen breath test, a history of lactose intolerance or coeliac disease (final population: n = 151, 0.1-12 y). Values were compared with those of 34 non-Belgian Caucasian children with normal histology (28 of Mediterranean origin). RESULTS: The reference limits (90% confidence interval) were 86 (65-111)-423 (366-494) for maltase, 9 (6-12)-91 (78-122) for lactase and 24 (18-30)-155 (120-184) for sucrase. No gender-related differences in enzyme activities were found. Lactase levels showed a slight decrease with increasing age. Disaccharidase activities of children with histologically confirmed mucosal injury were significantly lower than those of children with normal histology: median values for groups A, B and C were 208, 181 and 96, respectively, for maltase, 40, 28 and 7, respectively, for lactase and 69, 54 and 25, respectively, for sucrase. Median disaccharidase activities in biopsies with normal histology were lower in non-Belgian children, the difference being only statistically significant for lactase, 33 versus 40. CONCLUSION: The reference values for Belgian children are well in line with other reported values from Caucasian children. Although enzyme activities are lower in children with histologically confirmed mucosal damage, they do not allow differentiation between histology groups. Lower lactase values were found in non-Belgian children.

Atrophy↗
PubMed1975

Increased disaccharidase activity in human diabetics.

Disaccharidase activity has been shown to be increased in human diabetics. Diabetics controlled on diet therapy showed no change in disaccharidase activity while two diabetics controlled on insulin or insulin-producing drug, glibenclamide, showed a fall in disaccharidase values toward normal. Possible causes for the increased disaccharidase activity in diabetes are discussed.

Adult↗