Digestion of gliadin peptides by intestinal mucosa from control or coeliac children.
Gliadin, subsequently treated with pepsin, trypsin and pancreatic extract was further digested by small-intestinal mucosal homogenates from 10 control or 8 coeliac children. The amino acids liberated in the incubation mixture were measured and corrected for mucosal damage. In accordance with the data from the literature on adults, the total amount of amino acids released from gliadin peptides by the intestinal mucosa from children with active coeliac disease is significantly lower than that by the mucosa from control subjects. Qualitatively, however, no significant differences for the individual amino acids are observed with the exception of glutamine and proline, so that damaged coeliac mucosa liberates relatively more glutamine but less proline.
D000596:Amino Acids / Q000378:metabolism; D002446:Celiac Disease / Q000201:enzymology / Q000378:metabolism*; D002648:Child; D010450:Endopeptidases / Q000378:metabolism; D005903:Gliadin / Q000378:metabolism*; D006801:Humans; D007408:Intestinal Absorption; D007413:Intestinal Mucosa / Q000201:enzymology / Q000378:metabolism*; D007421:Intestine, Small / Q000201:enzymology / Q000378:metabolism*; D010434:Pepsin A / Q000494:pharmacology; D010455:Peptides / Q000302:isolation & purification / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D010455:Peptides; D010940:Plant Proteins; D005903:Gliadin; D010450:Endopeptidases; D014357:Trypsin; D010434:Pepsin A