acid-phosphatase and Celiac-Disease

Topics: Abetalipoproteinemia; Acid Phosphatase; Adenosine Triphosphatases; Amino Acids; Biopsy; Celiac Disease; Esterases; Galactose; Glucose; Histocytochemistry; Humans; Intestinal Mucosa; Jejunum; Malabsorption Syndromes; Microscopy, Electron; Mitochondria; Oxidoreductases; Sprue, Tropical; Whipple Disease

Five brush border and 2 lysosomal enzymes were measured in duodenal tissue explants from 21 children and young adults (16 coeliac and 5 non-coeliac) before and after organ culture. Reduced activity of brush border enzymes and increased activity of lysosomal enzymes were recorded in flat mucosas from coeliac patients compared with remission coeliac explants and biopsy specimens from non-coeliac controls. Slightly increased activity of alkaline phosphate and sucrase was recorded during culture (24 h) of coeliac explants. Coeliac specimens in the exacerbation state showed increased activity of acid phosphatase after culture in the presence of gluten, whereas gluten did not provoke detectable alterations in brush border enzyme activities during culture unless the wet weight of material was 1.5 mg or more. In such explants lower activity of brush border enzymes was measured after in vitro gluten exposure than after culture on gluten-free medium. Mucus removed from the specimen surface after culture contained considerable amounts of brush border enzymes and reflected the variations in the tissue homogenates. Culture media contained smaller quantities of enzymes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Adult; Alkaline Phosphatase; alpha-Glucosidases; beta-Galactosidase; Celiac Disease; Child; Culture Techniques; Duodenum; Humans; Intestinal Mucosa; Leucyl Aminopeptidase; Lysosomes; Microvilli; Sucrase

Rat-liver lysosomes have been used to determine the toxicity of gliadin fractions in relation to coeliac disease. In this study we compared the activity in acid phosphatase release from rat-liver lysosomes by casein, gliadin and by their peptic-tryptic digests. The release of acid phosphatase is not specific for gliadin.

Topics: Acid Phosphatase; Animals; Caseins; Celiac Disease; Gliadin; In Vitro Techniques; Lysosomes; Plant Proteins; Rats; Rats, Inbred Strains

1. Reduced activities of four enzymes from brush borders were found in intestianl biopsies from patients with untreated coeliac disease. The activities returned towards control values after treatment by gluten withdrawal. Parallel changes were noted for the cytosol enzyme lactate dehydrogenase. 2. Measurement of brush-border integrity by differential centrifugation of biopsy extracts indicated increased fragility of the brush borders in biopsies from untreated patients. Normal values were obtained for biopsies from treated patients. 3. Increased activites of six acid hydrolases (lysosomal enzymes) were found in biopsies from untreated coeliac patients. Normal values were obtained for biopsies from treated patients. 4. Assement of lysosomal integrity by assay of latent N-acetyl-beta-glucosaminidase and of sedimentable activity of four acid hydrolases demonstrated increased lysosomal fragility in untreated coeliac mucosa. These lysosomal changes return to within the normal range after treatment by gluten withdrawal. 5. The lysosomal changes are consistent with their having a pathogenic role in the enterocyte damage of coeliac disease. Possible mechanisms for the lysosomal changes are discussed.

Topics: Acetylglucosaminidase; Acid Phosphatase; Alkaline Phosphatase; Biopsy; Celiac Disease; Galactosidases; Glucosidases; Glucuronidase; Humans; Intestinal Mucosa; Jejunum; Leucyl Aminopeptidase; Lysosomes; Phosphoric Diester Hydrolases

Topics: Acid Phosphatase; Alcohol Oxidoreductases; Alkaline Phosphatase; Celiac Disease; Cytoplasm; Glucosephosphate Dehydrogenase; Histocytochemistry; Humans; Intestinal Absorption; Intestinal Mucosa; Intestine, Small; Lactose Intolerance; Leucyl Aminopeptidase; Lipid Metabolism; Malabsorption Syndromes; Succinate Dehydrogenase; Thiamine Pyrophosphate; Whipple Disease

Topics: Acid Phosphatase; Biopsy; Celiac Disease; Child; Female; Glucosidases; Histocytochemistry; Humans; Isoenzymes; Jejunum; L-Lactate Dehydrogenase; Male; Parents; RNA

Topics: Acid Phosphatase; Alkaline Phosphatase; Biopsy; Celiac Disease; Diet Therapy; Diet, Gluten-Free; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Glutens; Histocytochemistry; Humans; Intestinal Absorption; Jejunum; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Lipid Metabolism; Lipids; Pathology; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adult; Celiac Disease; Golgi Apparatus; Humans; Jejunum

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Aminopeptidases; Celiac Disease; Chromaffin System; Clinical Enzyme Tests; Dihydrolipoamide Dehydrogenase; Esterases; Glycerophosphates; Histocytochemistry; Humans; Hydroxybutyrates; Isocitrate Dehydrogenase; Jejunum; L-Lactate Dehydrogenase; Malate Dehydrogenase; Male; NAD; NADP; Oxidoreductases; Pyrophosphatases

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Biomedical Research; Celiac Disease; Diet; Diet Therapy; Dihydrolipoamide Dehydrogenase; Endopeptidases; Enzymes; Esterases; Glucosephosphate Dehydrogenase; Glucuronidase; Histocytochemistry; Humans; Intestine, Small; Intestines; Jejunum; L-Lactate Dehydrogenase; Lipodystrophy; Monoamine Oxidase; Mucous Membrane; Oxidoreductases; Pathology; Succinate Dehydrogenase; Syndrome; Whipple Disease

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Celiac Disease; Enzymes; Glucosephosphate Dehydrogenase; Histocytochemistry; Humans; Hydroxybutyrate Dehydrogenase; Intestinal Mucosa; Jejunum; Malabsorption Syndromes; Mucous Membrane

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Biopsy; Celiac Disease; Diarrhea; Electron Transport Complex II; Glycosaminoglycans; Histocytochemistry; Intestinal Diseases; Intestine, Small; Lipid Metabolism; Lymphoid Tissue; Rats; Research; Sprue, Tropical; Succinate Dehydrogenase