Colipase Overview
Colipase (CLPS) is a small secreted protein that acts as an essential cofactor for pancreatic triglyceride lipases during dietary fat digestion. It binds both to the C-terminal domain of pancreatic lipases and to emulsified lipid surfaces, anchoring and stabilizing the enzyme at the lipid-water interface even in the presence of inhibitory bile salts. This interaction allows efficient hydrolysis of dietary triglycerides into absorbable fatty acids and monoglycerides within the intestinal lumen. Colipase itself has no enzymatic activity but plays an indispensable structural role in enabling normal fat absorption. In humans, it is encoded by the *CLPS* gene and secreted from the pancreas as inactive procolipase, which becomes activated upon cleavage by trypsin in the intestine[1][2][3]. Deficiencies can lead to impaired fat absorption but there are no current therapies targeting this molecule directly.
Mechanism of Action
Not applicable; colipase itself does not have direct mechanisms targeted by drugs. Its biological role is to enable/activate pancreatic lipases.
Biological Functions
Disease Associations
Safety Considerations
- No notable safety concerns are associated with targeting colipase directly, as it is not used therapeutically nor targeted by drugs.
Interacting Drugs
Associated Biomarkers
| Biomarker |
|---|
| No established biomarkers for patient selection or efficacy monitoring specific to colipase. |
Gosset