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)

Follow-up studies on 36 children, in whom celiac disease (gluten-sensitive enteropathy) was established by gluten challenge, were carried out after management on gluten-free diets for a mean of six years. Evaluations included measurement of height and weight, which for the group approximated normal distributions, and histologic examination of the duodenal or jejunal mucosa. Mucosal morphology was regarded as normal in 16, and there were minimal changes in 20. Epithelial cell height was within the normal range in all the children. Interepithelial lymphocytes were within normal range in the majority and lymphoid cells in the lamina propria were not different from those in control subjects. Mucosal lactase was significantly lower in patients than in control subjects in the duodenum and the jejunum, whereas sucrase and alkaline phosphatase values were significantly lower in the jejunum but not in the duodenum. Low content of mucosal lactase and increased numbers of interepithelial lymphocytes may be sensitive indicators of persisting ingestion of gluten in mucosa that is otherwise normal or approximately so in appearance.
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PMID:Mucosal recovery in treated childhood celiac disease (gluten-sensitive enteropathy). 95 66

Although gluten withdrawal is likely to remain the mainstay of treatment for adult coeliac disease, many patients find the diet inconvenient and unpalatable and compliance among asymptomatic patients is often poor. Oral corticosteroids have been used for patients who seem to be resistant to gluten withdrawal but preparations with low systemic bioavailability might be preferable. We have given a new glucocorticoid (fluticasone propionate) to 12 adults with untreated coeliac disease for six weeks while they were on a normal diet. One patient defaulted and one suffered a relapse in a pre-existing neoplasm. Excluding these, there was an improvement of symptoms, a mean weight gain of 2 kg, and a rise in albumin of 5.4 g/l. There was a significant improvement in the lactulose/mannitol excretion ratio (p less than 0.05) and in all histological variables examined in paired biopsy specimens (surface and crypt intraepithelial lymphocyte/enterocyte and goblet cell/enterocyte ratios and enterocyte height, p less than 0.01 or better). In six paired specimens sucrase and alkaline phosphatase activity increased in all (p less than 0.05) and lactase in five of six. No appreciable side effects were observed, but two patients had suppressed cortisol values and synacthen responses at six weeks. A further three, with normal pretrial results, had a blunted tetracosactrin response at six weeks. Fluticasone propionate seems worthy of further assessment in the treatment of coeliac disease as an adjunct to gluten withdrawal.
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PMID:A pilot study of fluticasone propionate in untreated coeliac disease. 190 62

110 children suffering from malabsorption underwent several biopsies of the gut to confirm coeliac disease (CD) following the ESPGAN criteria. We studied the values for alkaline phosphatase (AP) in the intestinal mucosa after gluten challenge. In 42 patients the after challenge biopsy was normal, thus excluding coeliac disease. In 68 children the mucosa was severely damaged confirming CD. In all biopsy specimens lactase, invertase, maltase and alkaline phosphatase were measured. We found a good correlation between PA values and severity of mucosal damage, showing that measurement of PA in the mucosa is helpful in assessing the degree of mucosal atrophy in children suffering from malabsorption.
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PMID:[Alkaline phosphatase in the intestinal mucosa of children with the malabsorption syndrome]. 250 30

The effect of peptic-tryptic digested gliadin (PT-gliadin) on the increase in sucrase activity in different fractions of tissue cultured fetal chick duodenum was investigated and compared with that of monensin, a known perturbant of the Golgi complex. PT-gliadin diminished the rise in sucrase activity in the tissue homogenate, in a brush border fraction, and in the high speed supernatant, whereas the activity in a Ca2+-pelleted fraction including endoplasmic reticulum and Golgi apparatus was unaffected. In contrast, monensin caused a proportional inhibition of the increase in sucrase activity in all fractions examined. The findings might suggest that PT-gliadin is able to affect intracellular processing of sucrase with the site of attack being distal to that of monensin in the biogenesis of the enzyme. Whether the effect of PT-gliadin on fetal gut is relevant also for celiac intestine remains to be established.
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PMID:Effect of gliadin on the distribution of sucrase among different fractions of fetal chick intestine. 277 45

1. Biochemical estimates of lactase, sucrase and maltase activities, carried out on intestinal biopsies appearing histologically normal, were compared with those obtained from children suffering from coeliac disease, cow's milk protein intolerance/postenteritis syndrome and the intractable diarrhoea syndrome of infancy. Lactase deficiency in these children was found to be more pronounced than sucrase or maltase deficiencies. 2. Quantitative cytochemical investigations showed characteristic disease-induced changes in the ability of enterocytes to express alpha- and beta-glucosidases, but not alkaline phosphatase activities, during migration along stunted villi. 3. Separate estimates of the time course describing hydrolase development in normal and coeliac tissue showed the initial rate of lactase appearance to be halved in coeliac patients, while that for alpha-glucosidases remained constant and that for alkaline phosphatase increased by a factor of four. Enteroblastic replacement of mature enterocytes cannot provide a general explanation for hydrolase deficiency in diseased intestine.
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PMID:Selective alteration of brush-border hydrolases in intestinal diseases in childhood. 312 20

Fifty two children in whom coeliac disease was confirmed by persistent enteropathy while they were taking gluten were monitored to assess the effects of compliance with a gluten free diet (GFD). Between the ages of 17.8 and 18.5 years height (in 45 patients followed up for a mean of 14.9 years) and weight (in 43 followed up for a mean of 15.2 years) were significantly lower in those complying poorly with a GFD compared with those complying well. Of the 37 patients still attending the clinic after a mean of 25 years, having been followed up for a mean of 18.4 years, 16 who had complied well with the diet had normal or only slightly abnormal mucosal morphology whereas all 10 who had not complied had abnormal morphology. In these 10 lactase, sucrase, and alkaline phosphatase activities were significantly less than values in those who complied well. Mucosal sucrase and alkaline phosphatase activities in those who complied well were no different from those in a control population, whereas lactase activity was significantly lower. It is concluded that failure to comply with a GFD during childhood results in decreased adult stature and in persisting active enteropathy with depressed brush border enzyme activity.
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PMID:Compliance with gluten free diet in coeliac disease. 363 17

Highly sensitive techniques have been used for the assay of a range of marker enzymes including lactase, sucrase, alkaline phosphatase, leucyl-beta-naphthylamidase (brush border), and 5'-nucleotidase (basolateral membrane) in jejunal biopsy homogenates from patients with adult coeliac disease with and without steatorrhoea and from a control group. The absorption of D-xylose and vitamin B12 was compared in the two groups with coeliac disease. All enzymes assayed were equally depressed in both groups of coeliac disease as compared with the controls. The absorption of D-xylose and vitamin B12 were reduced in the patients with steatorrhoea compared with those without steatorrhoea. The findings suggest that lack of steatorrhoea in some patients with coeliac disease is due to better preservation of the ileal function rather than to a less severe jejunal mucosal injury.
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PMID:Enzyme activities in jejunal biopsy samples from patients with adult coeliac disease with and without steatorrhoea. 632 31

Activities of lactase, sucrase, and maltase were determined in small intestinal biopsies of 125 children with coeliac disease, cow's milk protein intolerance, transient gluten intolerance, nonspecific enteropathies, and controls. Four cases of primary disaccharidase deficiencies could be identified. In the enteropathies, morphometric data were more closely correlated to the degree of the mucosal lesion (r = -0.92 for crypt depth) than were disaccharidase activities (r = 0.61 for lactase). In a stepwise discriminant analysis of the patient groups, based upon immunological, morphometric, and biochemical variables, lactase activity was a valuable secondary criterion, ranking third among the variables used.
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PMID:[Disaccharidase activity as a diagnostic criterion for the mucosa of the small intestine]. 641 Jan 84

In 30 children presenting with complaints characteristic of malabsorption in whom congenital enzyme deficiency could be excluded, determination of the enzymes lactase, saccharase and maltase was performed in the tissue sample obtained by jejunal biopsy; histology was also carried out in all cases. In 23 cases the diagnosis of coeliac disease could subsequently be confirmed, in the other 7 cases the diagnosis could neither be rejected nor established with certainty. All three enzymes had a decreased activity in cases displaying subtotal or total villous atrophy, the most sensitive among them being lactase: in 69% of cases no lactase activity could be shown while saccharase and maltase were absent in 29 respectively 4% of the cases. No close correlation exists between the light-microscopic findings and the activity of enzymes since total absence of enzyme activity may be associated with only moderate villous atrophy. Lack of disaccharidase activity in the upper section of the small bowel does not necessarily mean disaccharide malabsorption exhibiting clinical symptoms, it only indicates a reduced capacity of disaccharide splitting. It has been concluded that routine determination of disaccharidase activities is not justified within the diagnostic procedure of coeliac disease.
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PMID:Disaccharidases in coeliac disease. 641 72

Lactase, sucrase, and alkaline phosphatase activities were measured in 833 peroral small intestinal biopsies from 373 patients with coeliac disease. Enzyme activities decreased with increasing degrees of mucosal damage. Enzyme activities in mucosae of patients with coeliac disease in remission were lower than in control groups matched for age, sex, and site of biopsy. Enzyme activities were measured in 81 patients when the mucosa was severely damaged and later when considerable improvement had occurred. Lactase activity remained low in 13% of patients under the age of 18 and in 33% of those over 18 years. Sucrase activity usually improved with histological recovery, but alkaline phosphatase activity tended to remain depressed in patients in whom lactase activity failed to improve.
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PMID:Intestinal lactase, sucrase, and alkaline phosphatase in 373 patients with coeliac disease. 642 95


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