Literature DB >> 7008982

Intestinal peptidases and sucrase in coeliac disease.

H Sjöström, O Norén, P A Krasilnikoff, E Gudmand-Høyer.   

Abstract

The activities of microvillus aminopeptidase (microsomal, EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.-), glycyl-leucine dipeptidase (EC 3.4.13.11), proline dipeptidase (EC 3.4.13.9), sucrase (EC 3.2.1.48) and gamma-glutamyl transpeptidase (EC 2.3.2.2) were measured in peroral intestinal biopsies taken from patients with coeliac disease in the acute phase and in remission. A comparison with the amounts of corresponding activities from a reference group showed that all the measured activities were significantly decreased in the acute phase of the disease. In patients in remission only microvillus aminopeptidase and dipeptidyl dipeptidase IV displayed a substantial depression as compared to the reference group. It is suggested that a primary mucosal digestion defect will result in lack of substrate for other intestinal enzymes. This is a situation comparable to starvation and may explain the variation in the grade of restitution for the different enzymes.

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Year:  1981        PMID: 7008982     DOI: 10.1016/0009-8981(81)90136-4

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  3 in total

1.  Coeliac disease: A review of the causative agents and their possible mechanisms of action.

Authors:  H J Cornell
Journal:  Amino Acids       Date:  1996-03       Impact factor: 3.520

2.  Breakdown of gliadin peptides by intestinal brush borders from coeliac patients.

Authors:  G Bruce; J F Woodley; C H Swan
Journal:  Gut       Date:  1984-09       Impact factor: 23.059

3.  Brush border enzymes in coeliac disease: histochemical evaluation.

Authors:  J Mercer; M E Eagles; I C Talbot
Journal:  J Clin Pathol       Date:  1990-04       Impact factor: 3.411

  3 in total

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