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Related Experiment Videos

Aspartic proteinases: their activation and structural studies.

V Turk, V Puizdar, T Lah

    Progress in Clinical and Biological Research
    |January 1, 1982
    PubMed
    Summary
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    Cathepsin D zymogen activation releases peptides that inhibit its own activity and other aspartic proteinases. Bovine pepsinogen activation peptides do not inhibit cathepsin D or E.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Intracellular proteinase cathepsin D, like extracellular aspartic proteinases, is synthesized as a precursor.
    • Understanding the activation mechanisms and regulatory properties of aspartic proteinases is crucial.

    Purpose of the Study:

    • To investigate the activation mechanism of cathepsin D zymogen (procathepsin D).
    • To characterize the inhibitory activity of peptides released during cathepsin D activation.
    • To study the structural changes in aspartic proteinases using circular dichroism.

    Main Methods:

    • Analysis of cathepsin D zymogen activation.
    • In vitro assays to determine peptide inhibitory activity.
    • Circular dichroism (CD) spectroscopy to study protein structure.

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  • Near-UV CD spectrum analysis of pepstatin binding.

    • Main Results:

    • Cathepsin D zymogen is activated by a mechanism similar to pepsin, releasing inhibitory peptides.
    • These released peptides inhibit cathepsin D and other aspartic proteinases.
    • Activation peptides from bovine pepsinogen do not inhibit cathepsin D or E.
    • Pepstatin binding induces conformational changes in aspartic proteinases, observable via CD spectroscopy.

    Conclusions:

    • The activation segment of cathepsin D possesses intrinsic inhibitory properties.
    • This suggests a self-regulatory mechanism for cathepsin D activity.
    • Structural studies reveal insights into aspartic proteinase function and inhibitor interactions.