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A factor X-activating cysteine protease from malignant tissue

S G Gordon, B A Cross

    The Journal of Clinical Investigation
    |June 1, 1981
    PubMed
    Summary
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    Cancer procoagulant, a tumor-derived enzyme, was investigated to determine if it is a serine or cysteine protease. Results indicate cancer procoagulant is a cysteine endopeptidase, distinct from other coagulation factors.

    Area of Science:

    • Biochemistry
    • Oncology
    • Hematology

    Background:

    • A tumor-associated proteolytic procoagulant directly activates Factor X.
    • The enzyme's classification as a serine or cysteine protease was previously unclear.

    Purpose of the Study:

    • To determine if cancer procoagulant is a serine or cysteine protease.
    • To differentiate cancer procoagulant from other Factor X-activating proteases.

    Main Methods:

    • Purified cancer procoagulant from rabbit V2 carcinoma.
    • Affinity chromatography using p-chloromercurialbenzoate-agarose.
    • Enzyme inhibition assays with diisopropylfluorophosphate, phenylmethylsulfonylfluoride, HgCl2, and iodoacetamide.
    • Comparison with Russell's viper venom, a known serine protease.

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    Main Results:

    • Cancer procoagulant activity was inhibited by HgCl2 and iodoacetamide, characteristic of cysteine proteases.
    • Inhibition by diisopropylfluorophosphate and phenylmethylsulfonylfluoride was reversible with dithiothreitol.
    • Iodoacetamide inhibition was irreversible, further supporting a cysteine protease classification.
    • Russell's viper venom was not inhibited by HgCl2 or iodoacetamide.

    Conclusions:

    • Cancer procoagulant is identified as a cysteine endopeptidase.
    • This distinguishes it from other coagulation factors like tissue factor.
    • Neoplastic cells may produce this unique cysteine protease to initiate blood coagulation.