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Physiology · Gastrointestinal physiology: enteropeptidase
Sample itemAn infant has failure to thrive, diarrhoea and hypoproteinaemic oedema from weaning. Duodenal fluid has trypsinogen but almost no trypsin or chymotrypsin activity, and adding enteropeptidase restores activity. Which defect is present?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
D. Deficiency of duodenal brush-border enteropeptidase, so trypsinogen is not activated
Enteropeptidase on the duodenal brush border converts trypsinogen to trypsin, which then activates the other pancreatic proenzymes. Its absence produces protein malabsorption with hypoproteinaemia, diarrhoea and failure to thrive despite a structurally normal pancreas.
Option by option
A. Absence of pancreatic lipase only
Isolated lipase deficiency causes steatorrhoea but not impaired protein digestion.
B. Defective chloride channel (CFTR) in pancreatic ducts
CFTR defects cause thick secretions and are not corrected by adding enteropeptidase.
C. Absence of pancreatic secretory trypsin inhibitor
Loss of the trypsin inhibitor causes premature activation and pancreatitis.
D. Deficiency of duodenal brush-border enteropeptidase, so trypsinogen is not activated (correct)
Correct. Without enteropeptidase, trypsin and downstream enzymes remain inactive.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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