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Related Experiment Videos

Protease nexin. Properties and a modified purification procedure.

R W Scott, B L Bergman, A Bajpai

    The Journal of Biological Chemistry
    |June 10, 1985
    PubMed
    Summary

    Protease nexin, a serine protease inhibitor synthesized by human fibroblasts, exhibits broad specificity against trypsin-like proteases. Its properties suggest evolutionary links to other protease inhibitors.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Human fibroblasts secrete protease nexin, a serine protease inhibitor.
    • Protease nexin constitutes approximately 1% of secreted fibroblast proteins.
    • Its chemical and functional properties are investigated.

    Purpose of the Study:

    • To characterize the chemical and functional properties of protease nexin.
    • To determine its evolutionary relationship to other serine protease inhibitors.
    • To elucidate its inhibitory specificity and kinetics.

    Main Methods:

    • Amino acid composition analysis of purified protease nexin.
    • Equilibrium sedimentation for molecular weight determination.
    • Kinetic analysis of protease inhibition using various serine proteases.

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  • Heparin affinity studies.

    • Main Results:

    • Protease nexin is synthesized by fibroblasts and is evolutionarily related to antithrombin III and heparin cofactor II.
    • It contains approximately 6% carbohydrate, including sialic acid.
    • It is a broad-specificity inhibitor of trypsin-like serine proteases, including trypsin, thrombin, urokinase, and plasmin.
    • Heparin significantly enhances thrombin inhibition by protease nexin, revealing two heparin affinity classes.

    Conclusions:

    • Protease nexin is a significant serine protease inhibitor produced by fibroblasts with broad inhibitory activity.
    • Its structural and functional characteristics suggest a role in regulating protease activity.
    • The interaction with heparin highlights its potential involvement in heparin-mediated biological processes.