1,720,972 research outputs found
Espressione e attività enzimatica della transglutaminasi tissutale nella mucosa intestinale di pazienti celiaci
No full textExpression and enzymatic activity of small intestinal tissue transglutaminase in celiac disease.
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Analysis of lactase processing in rabbit
No full textAbstractThe proteolytic processing of rabbit intestinal lactase-phlorizin-hydrolase (LPH) was studied by pulse-chase and continuous labeling experiments in organ culture from 15-day-old rabbits in the presence of glycosylation and processing inhibitors. Monensin and brefeldin A inhibited the two proteolytic cleavages of the precursor indicating that they are post-Golgi events as previously reported for the unique cleavage of LPH in man [1]. The inhibition was not related to a concomitant alteration glycosylation; in fact, if trimming was blocked by MDNM the abnormal glycosylated precursor was proteolytically processed normally. Finally the use of the anti-microtubular drug colchicine strongly inhibited both cleavages and caused accumulation of the complex-glycosylated precursor form in the brush border fraction indicating that proteolytic events depend on intact microtubule (transport)
Interleukin 18 and associated markers of T helper cell type 1 activity in coeliac disease.
No full textInterleukin 18 and associated markers of T helper cell type 1 activity in coeliac disease.
No full textIn vitro biosyntesis of lactase in suckling and adult rabbits. Regulatory mechanisms involved in the decline of the lactase activity.
No full textSteady state forms, levels and the in vitro biosynthesis of lactase-phlorizin hydrolase (LPH) proteins have been studied in proximal and middle intestine of suckling and adult rabbits. In most adult tissues the lactase activity and the LPH protein content were low and the synthesis rate of the 200 kDa lactase precursor was reduced in comparison to suckling tissues. In a few tissues with low enzymatic activity the LPH protein content was relatively high, and high lactase synthesis occurred. In addition, the ratio (labeled lactase)/(lactase protein) was lower in the middle jejunum of the adult rabbit than in the proximal region. Both decreased synthesis of LPH precursor and increased turnover or inactivation of the enzyme may cause the decline of the lactase activity
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