Brush Border and Lysosomal Marker Enzyme Profiles in Duodenal Mucosa from Coeliac Patients before and after Organ Culture

Abstract

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.

Organ culture of gastrointestinal mucosa—a technique for the study of the human gastrointestinal tract

“…Such means of assessment of cultured tissue enabled the organ culture technique to be used to provide an in vitro model of coeliac disease (Howdle et aL,198 lb). Other workers confirmed these results using similar morphometric measurements (Fluge and Aksnes, 1981;Bramble, Watson and Record, 1981;Olives et al, 1981).…”

“…The technique of organ culture for gastrointestinal mucosa Browning and Trier (1969) described a method which has been used, with minor modifications, by several groups of workers, including the present author (Falchuk et a!., 1974a;Jos et al, 1975;Fluge and Aksnes, 1981;Howdle et al, 1981a). Usually mucosal biopsies are obtained for culture using an intestinal mucosa biopsy instrument.…”

“…Morphometry has proved to be a useful means of assessing cultured tissue, particularly since there has been some disagreement about the biochemical changes initially reported by Falchuk et aL (1974a), others not finding them so reproducible (Hauri et aL, 1978;Howdle et aL, 1981a;Fluge et al, 1982). Morphological assessment would also seem to be more appropriate since mucosal diseases, such as coeliac disease, are almost universally diagnosed using morphological criteria.…”

Bioactive antinutritional peptides derived from cereal prolamins: A Review

“…Bread wheat 0 a-Gliadin [69] 0 A-gliadin [73] 0 Tryptic a-gliadin digest [74] 0 Peptic-tryptic gluten digest [66,69,71,72] 0 Peptic-tryptic gliadin digest [33, 75 -78] 0 Peptic-tryptic-cotazym gliadin digest [33, 74, 78 -80] 0 Peptic-tryptic a-gliadin digest [33,41,66,75,76] 0 Peptic-tryptic b-gliadin digest [33,41,75,76] 0 Peptic-tryptic c-gliadin digest [33,41,75,76] 0 Peptic-tryptic x-gliadin digest [33,41,75,76] 0 Peptide 2R derived from a peptic-tryptic-cotazym digest of gliadin [81] 0 Peptides fractionated from a peptic-tryptic-cotazym digest including peptide fractions B 2 and B 3142 [40,41]. Peptide B 3142 is homologous to A-gliadin amino acid sequence 3 -55 [42] …”

An in Vitro Animal Model for the Study of Cereal Components Toxic in Celiac Disease

“…These results were consistent with those by Hekkens et al (32) who demonstrated that an a-gliadin fraction, coded A-gliadin (10,49), was capable of producing changes in epithelial tissue characteristic of celiac disease when instilled directly into the small intestine of celiac patients and with those by Falchuk et al (19) showing that this fraction had adverse effects on biopsied intestinal epithelium. Huge and co-workers (24)(25)(26) have developed a morphological, morphometric, and biochemical assessment of human duodenal biopsies from celiac patients maintained in organ culture and have tested with this in vitro system several gliadin fractions including a-gliadin and Frazer's fraction I11 and subfractions. Biopsies from patients with untreated celiac disease were susceptible to gliadin fractions, which provoked disorganization of crypt architecture, reduced height, and irregularities of enterocytes and crypt cells, together with detrition of surface epithelial cells and even tissue necrosis.…”