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Mucosal enterokinase activity in cow's milk protein sensitive enteropathy
N Iyngkaran1, M Yadav, C G Boey
1Department of Paediatrics, University Hospital, Malaysia.
Singapore Medical Journal
|August 1, 1995
Summary
Enterokinase activity in infants with diarrhea is less affected by mucosal damage than other brush border enzymes. This suggests its unique synthesis in goblet cells influences its resilience in pediatric enteropathies.
Area of Science:
- Biochemistry
- Gastroenterology
- Pediatric Medicine
Background:
- Enterokinase initiates protein digestion by converting trypsinogen to trypsin.
- It is synthesized by enterocytes and released into the intestinal lumen.
- Its role in pediatric diarrheal diseases requires further investigation.
Purpose of the Study:
- To analyze enterokinase activity in the duodenal mucosa of infants with diarrheal disease.
- To compare enterokinase depletion with other brush border enzymes in affected infants.
- To investigate the relationship between mucosal damage, goblet cell population, and enterokinase activity.
Main Methods:
- Analysis of duodenal mucosa samples from infants.
- Measurement of enterokinase activity.
- Comparison with activities of disaccharidases, peptidases, and alkaline phosphatases.
- Assessment of mucosal damage and goblet cell population.
Main Results:
- Enterokinase depletion was only 17% in infants with diarrhea, significantly less than other brush border enzymes (60-80%).
- Enterokinase activity was reduced in acute/chronic diarrhea with marked mucosal damage and goblet cell loss.
- Mild mucosal damage showed little effect on enterokinase activity.
Conclusions:
- Enterokinase activity in small bowel enteropathies is influenced by goblet cell damage, not just overall mucosal injury.
- The enzyme's resilience suggests a unique protective mechanism or synthesis pathway.
- Further research into pediatric enteropathies should consider specific enzyme vulnerabilities.