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At least 1,711 records · Page 95Linked to original sources
PubMed1980

[Comparative toxicity of different cereals for subjects intolerant of gluten].

Coeliac disease is caused by prolamines, the storage proteins of some cereals, located in the endosperm. Cereals do not all have the same toxicity. The four wheat prolamine groups (alpha, beta, gamma and omega gliadins), visible in electrophoresis at acid pH, have been isolated and their toxicities compared by observing the morphological changes in intestinal biopsies cultured in vitro when peptic-tryptic digests of the studied proteins were added to the culture medium. The toxicity was found to be mainly located in the alpha and beta-gliadins and in peptides of 5 to 10 000 molecular weight. Peptides, resulting from peptic-tryptic hydrolysis, varied in length as a direct function of their proline content. In fact, peptide bond splitting by pepsin and trypsin is known to be blocked by proline. Thus, proline content determines peptide length and toxicity. Wheat, rye and barley toxicities were compared on the basis of a correlation between toxicity and the alpha- and beta-gliadin-like prolamine contents of these cereals. Electrophoretic estimation of alpha- and beta-gliadin-like prolamine content gave the following prediction of relative toxicity (in decreasing order): wheat, triticale, rye, barley and oats.

Amino Acids↗
PubMed1980

[Effect of a protein-deficient diet (5 p. 100 gluten) and of balanced refeeding (15 p. 100 casein) on potential lipase, colipase-dependent lipase and phospholipase A2 activities. II. In the pancreatic juice of the growing rat].

We experimented with a diet resembling a protein-deficient one eaten by man, having a low protein level and proteins of poor biological value. Malnutrition caused weight loss accompanied by an overall reduction of ingesta. However, the food intake, as compared to animal weight, was the same in the undernourished animals as in the controls. Bile and pancreatic juice outputs were not altered continuously and regularly but with the poor protein diet, they were lower. Refeeding a balanced diet caused these outputs to increase. When 0.6 p. 100 of methionine was added to the deficient diet, no significant difference was noted in the outputs of the rats eating the deficient diets. Enzyme activities in the juice and pancreas varied widely from one day to another during malnutrition and during refeeding. The mean values of specific activities, which masked these variations, showed that malnutrition did not significantly decrease the phospholipase A2 activity in the pancreatic juice, while potential lipase and colipase-dependent lipase activities declined. Refeeding temporarily stimulated specific phospholipase A2 and potential lipase activities the third day; colipase-dependent lipase activity was not activated. After 2 to 3 weeks of refeeding, the specific activities of the three enzymes were similar to the control values, but were no longer so at the end of refeeding. This would suggest a return to the normal, as shown by the oscillations around the control values. Protein malnutrition, as refeeding, did not in general cause the same changes in all the enzymes at the same time.

Animals↗
PubMed1995

[Life threatening epistaxis due to plasma coagulation disorder as a partial manifestation of gluten sensitive enteropathy].

We report on a 73 years old female patient receiving a recurrent epistaxis due to a severe plasmatic malcoagulation. In spite of since twenty years remaining diarrhoea coeliac disease has been diagnosed but now causative of the malcoagulation. On the occasion of this report clinical, current pathogenetical, immunological and pathohistological aspects of coeliac disease have been described. At last we agree to the differential diagnosis of anaemia in coeliac disease and in this connection to the metabolism of vitamin K too.

Aged↗