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Pancreatic Juice and Secretion

Pancreatic Juice and Secretion

Pancreatic juice is a clear fluid produced by the pancreas, containing water, salts, sodium bicarbonate, and enzymes vital for digestion in the small intestine. It helps break down large molecules, facilitating nutrient absorption.
When acidic chyme from the stomach enters the duodenum, it triggers the release of secretin, a hormone that prompts pancreatic juice secretion. After a fatty meal, cholecystokinin, another hormone, stimulates gallbladder contraction and enhances enzyme-rich...

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Related Experiment Video

Updated: Jan 13, 2026

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

Human CELA1 has pancreatic elastase-like activity.

Deepti Jamwal¹, Prince Kumar¹, Kunal Meena²

¹Infection and Immunology, Translational Health Science and Technology Institute, Faridabad, 121001, Haryana, India.

|January 11, 2026

Summary

This summary is machine-generated.

Human chymotrypsin-like elastase 1 (CELA1) exhibits pancreatic elastase-like enzymatic activity. This digestive enzyme, activated by trypsin, shows higher substrate affinity than porcine pancreatic elastase.

Keywords:

CELA1 Enzyme Keratinocyte Pancreatic elastase lungs

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Area of Science:

Biochemistry
Enzymology
Digestive Physiology

Background:

Chymotrypsin-like elastase 3A (CELA3A) and 3B (CELA3B) are key pancreatic elastases involved in digestion and markers for pancreatic exocrine insufficiency.
Human chymotrypsin-like elastase 1 (CELA1), unlike its counterparts, is not typically found in the pancreas but has been identified in mouse lung and human keratinocytes.

Purpose of the Study:

To investigate the enzymatic activity and functional mechanism of human CELA1.
To characterize the activation and kinetics of recombinant human CELA1 (pro-hCELA1).

Main Methods:

Purification and recombinant expression of pro-hCELA1.
Enzymatic assays to determine activation by trypsin and elastase-like activity.
Kinetic analysis using steady-state enzyme kinetics.
Inhibition studies using aprotinin.

Main Results:

Recombinant pro-hCELA1 is activated by trypsin, demonstrating pancreatic elastase-like activity.
Aprotinin effectively blocks the trypsin-mediated cleavage and activation of pro-hCELA1.
The active form of hCELA1 exhibits steady-state kinetics and a higher substrate affinity compared to commercial porcine pancreatic elastase.

Conclusions:

Human CELA1 possesses functional elastase activity relevant to pancreatic digestive processes.
CELA1 activation is regulated by trypsin, and its kinetics suggest a significant role in substrate hydrolysis.
These findings expand the known functions of the CELA family and highlight CELA1 as a potential player in digestive enzyme research.