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Physiology · GI physiology: pancreatic enzymes
Sample itemA 3-month-old infant has diarrhoea, failure to thrive and oedema with low serum albumin. Duodenal fluid has normal trypsinogen but no trypsin activity. Which missing enzyme explains this?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Enteropeptidase of the duodenal brush border
Enteropeptidase (enterokinase) converts trypsinogen to trypsin at the duodenal brush border, and trypsin in turn activates the other pancreatic zymogens including chymotrypsinogen and procarboxypeptidase. In its absence, protein digestion fails and protein-losing malabsorption causes hypoalbuminaemia and oedema. Treatment is with pancreatic enzyme supplements.
Option by option
A. Enteropeptidase of the duodenal brush border (correct)
Absent enteropeptidase leaves trypsinogen inactive and prevents activation of the other zymogens.
B. Pancreatic lipase
Lipase deficiency would cause fat malabsorption, with a normal trypsin level.
C. Pepsin from gastric chief cells
Pepsin is not essential for normal protein digestion, since pancreatic proteases are sufficient.
D. Salivary amylase
Salivary amylase has a minor role, and pancreatic amylase compensates for its absence.
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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