Enhancement of the autocatalytic activation of trypsinogen to trypsin by bile and bile acids.
Level 5 - mechanism / opinion, no new human data
In vitro bench biochemistry study
PubMed 3986221 · doi:10.1016/0304-4165(85)90007-8
What was done
In vitro biochemical assays evaluated the effect of human bile and individual bile salts on the autocatalytic conversion of trypsinogen to trypsin across varying calcium concentrations and pH levels.
What was found
Bile salts and human bile significantly accelerated trypsinogen autocatalysis. The effect depended on calcium ion concentration and peaked around pH 5.4 and pH 7.8. Each bile salt exhibited an optimal concentration, with certain bile salts increasing activation rates by up to 55-fold.
Why it matters
The findings demonstrate an alternative or supportive pathway for trypsinogen activation in the gut, offering a mechanistic explanation for why patients with impaired bile secretion often have reduced duodenal trypsin activity.
Limits
This was an in vitro biochemical study with no in vivo measurements in humans or animals. The abstract does not specify the number of human bile samples tested, the specific bile salt species evaluated, or the kinetic comparison relative to enterokinase-driven activation.
Cited by
- supports Bile acids secreted from the gallbladder enhance the activity of intestinal proteolytic enzymes.