Brush border enzyme activities in the small intestine after long-term gliadin feeding in animal models of human coeliac disease
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9821309
DOI
10.1007/bf02820803
Knihovny.cz E-resources
- MeSH
- beta-Galactosidase metabolism MeSH
- Time Factors MeSH
- Celiac Disease enzymology MeSH
- Dipeptidyl Peptidase 4 metabolism MeSH
- Gliadin administration & dosage MeSH
- Rats MeSH
- Lactase MeSH
- Humans MeSH
- Microvilli enzymology MeSH
- Disease Models, Animal * MeSH
- Mice, Inbred BALB C MeSH
- Mice, Nude MeSH
- Mice MeSH
- Rats, Wistar MeSH
- Swine MeSH
- Sucrase metabolism MeSH
- Intestinal Mucosa enzymology MeSH
- Intestine, Small enzymology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- beta-Galactosidase MeSH
- Dipeptidyl Peptidase 4 MeSH
- Gliadin MeSH
- Lactase MeSH
- Sucrase MeSH
Coeliac disease is a human, genetically linked, disorder which develops in gluten-sensitive persons. The aim of this study was to investigate the effect of prolonged feeding of gliadin, a major fraction of gluten, on enzyme activities of enterocyte brush border membrane enzymes in rats, mice and pigs. Brush-border membranes were isolated from mucosal scrapings of the small intestine of 21-d-old rat pups hand-fed with formula milk diet, two-month-old nu/nu and +/+ BALB/c mice and two-month-old piglets fed three times a week starting at birth with high doses of gliadin. Activities of lactase, sucrase and dipeptidyl peptidase IV (DPP IV) were determined. Individual animal models differed in their response to gliadin feeding. In comparison with albumin fed controls the activities of DPP IV and lactase were decreased in rat pups, nu/nu BALB/c mice and piglets. DPP IV activity was mostly affected in the ileum of rats and piglets fed with gliadin starting at birth. On the other hand, lactase and sucrase activities of nu/nu BALB/c mice and piglets decreased to the largest extent in jejunum.
See more in PubMed
Biochim Biophys Acta. 1972 Sep 19;284(1):235-47 PubMed
Gut. 1996 Sep;39(3):374-81 PubMed
Clin Sci (Lond). 1988 Feb;74(2):193-200 PubMed
Anal Biochem. 1976 Aug;74(2):466-76 PubMed
Am J Physiol. 1993 Jul;265(1 Pt 1):G81-9 PubMed
Biochim Biophys Acta. 1978 Jan 4;506(1):136-54 PubMed
Folia Biol (Praha). 1989;35(1):19-26 PubMed
Physiol Bohemoslov. 1990;39(2):135-46 PubMed
Biochem Int. 1990 Nov;22(3):495-508 PubMed
Adv Exp Med Biol. 1995;371A:501-5 PubMed
Gut. 1995 Mar;36(3):321-3 PubMed
Anal Biochem. 1964 Jan;7:18-25 PubMed
Gastroenterology. 1990 Mar;98(3):667-75 PubMed
Exp Physiol. 1990 Jul;75(4):613-6 PubMed
J Nutr. 1989 Nov;119(11):1737-40 PubMed
Nutr Metab. 1978;22(4):244-55 PubMed
Scand J Gastroenterol. 1996 Jun;31(6):551-7 PubMed
Adv Exp Med Biol. 1995;371B:1191-8 PubMed
Folia Microbiol (Praha). 1995;40(4):385-91 PubMed
Crit Rev Biochem Mol Biol. 1995;30(3):197-262 PubMed
Physiol Bohemoslov. 1983;32(4):334-45 PubMed
