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Human serum procarboxypeptidase A.

L M Peterson, B Holmquist

    Biochemistry
    |June 21, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Serum procarboxypeptidase A activation by various enzymes was measured. Pancreatic inflammation increases both precursor and active enzyme levels, with variable activation degrees, offering new insights into zymogen regulation.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Proteolysis

    Background:

    • Zymogen activation is a critical biochemical process with significant physiological and pathological roles.
    • Understanding the regulation of enzyme precursor activation is essential for comprehending various biological functions and diseases.

    Purpose of the Study:

    • To simultaneously quantify serum procarboxypeptidase A (precursor) and carboxypeptidase A (active enzyme).
    • To investigate the activation pathways and regulation of serum procarboxypeptidase A.
    • To explore the implications of procarboxypeptidase A levels and activation in pancreatic inflammation.

    Main Methods:

    • Simultaneous measurement of procarboxypeptidase A and carboxypeptidase A in serum.
    • Utilized an affinity resin and the synthetic peptide substrate N-(2-furanacryloyl)-L-phenylalanyl-L-phenylalanine.

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  • Assessed activation by various proteases including trypsin, chymotrypsin, plasmin, subtilisin, and urokinase.

    • Main Results:

    • Serum procarboxypeptidase A is activated by trypsin, chymotrypsin, plasmin, subtilisin, and urokinase, but not by thrombin or enteropeptidase.
    • The molecular weight of procarboxypeptidase A is 5,000-10,000 Da greater than that of carboxypeptidase A.
    • During pancreatic inflammation, both procarboxypeptidase A and carboxypeptidase A increase in serum, with activation varying up to 2000-fold independently of precursor levels.

    Conclusions:

    • The presence of pancreatic proteolytic precursor in serum provides a novel model for studying zymogen activation.
    • The variable degree of activation suggests complex regulatory mechanisms controlling carboxypeptidase A activity in vivo.
    • These findings open new avenues for investigating zymogen activation and its regulation in health and disease.