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A novel human chymotrypsin-like digestive enzyme

J E Reseland1, F Larsen, J Solheim

  • 1Biotechnology Centre of Oslo and The Animal Department, The National Hospital, University of Oslo, P.O. Box 1125, Blindern, N-0317 Oslo, Norway.

The Journal of Biological Chemistry
|March 21, 1997
PubMed
Summary

Researchers cloned a novel human pancreatic enzyme, chymotrypsin-like enzyme-1 (CTRL-1). This digestive enzyme exhibits unique features and is secreted by the pancreas upon feedback stimulation.

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Area of Science:

  • Biochemistry
  • Genetics
  • Molecular Biology

Background:

  • Human pancreas secretes various digestive enzymes.
  • Serine proteases play crucial roles in digestion and other physiological processes.
  • Novel enzymes contribute to understanding complex biological functions.

Purpose of the Study:

  • To clone and characterize a novel chymotrypsin-like serine protease from human pancreas.
  • To investigate the gene structure, expression, and functional properties of the enzyme.
  • To determine its physiological relevance and potential role in digestion.

Main Methods:

  • Gene cloning and sequencing.
  • Northern blot analysis for gene expression.
  • Antibody production and Western blotting for protein detection.

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  • Enzyme activity assays and substrate specificity determination.
  • Recombinant protein expression and characterization.

    • Main Results:

    • The chymotrypsin-like enzyme-1 (CTRL-1) gene was cloned and mapped to chromosome 16q22.1.
    • CTRL-1 mRNA was detected exclusively in pancreatic tissue.
    • The active enzyme was identified in pancreatic homogenate, duodenal juice, and urine.
    • CTRL-1 demonstrated chymotrypsin- and elastase-2-like activities, with broad substrate specificity.
    • Pancreatic secretion of CTRL-1 increased upon protease inhibitor administration, indicating feedback regulation.

    Conclusions:

    • CTRL-1 is a novel digestive enzyme belonging to the chymotrypsin superfamily, with distinct biochemical and physiological characteristics.
    • Its presence in duodenal juice suggests a role in protein digestion.
    • The enzyme's secretion is regulated by feedback mechanisms, highlighting its importance in pancreatic function.