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Related Experiment Videos

Elevated proteinase activities in mouse lung tumors quantitated by synthetic fluorogenic substrates.

R Grabske, A Azevedo, R E Smith

    The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society
    |November 1, 1979
    PubMed
    Summary

    Lung tumor tissues exhibit elevated proteinase activity compared to normal lung tissues. This suggests specific enzymes may play a role in lung cancer development and progression.

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    Area of Science:

    • Biochemistry
    • Oncology
    • Enzymology

    Background:

    • Proteinases play crucial roles in cellular processes, including tissue remodeling and degradation.
    • Aberrant proteinase activity is implicated in the progression of various cancers, including lung cancer.
    • Understanding specific proteinase profiles in tumors can offer insights into cancer mechanisms.

    Purpose of the Study:

    • To quantify and characterize proteinase activities in mouse lung tumor models.
    • To compare enzyme hydrolysis rates between malignant and normal lung tissues.
    • To investigate the potential involvement of cathepsin B-like enzymes in lung tumorigenesis.

    Main Methods:

    • Utilized two synthetic fluorogenic peptide substrates to measure proteinase activity.

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  • Assayed enzyme hydrolysis in homogenates of Lewis lung tumors and KHT tumors in mice.
  • Determined kinetic parameters (pH optimum, Km) and inhibitor profiles for specific substrates.

    • Main Results:

    • Lung tumor homogenates showed significantly higher hydrolytic activity for both tested substrates compared to normal lung homogenates.
    • One substrate (CBZ-Val-Lys-Lys-Arg-4-methoxy-2-naphthylamide) exhibited characteristics of cathepsin B-like enzyme activity (pH optimum 6.3, Km 2.1 x 10(-4) M, thiol-dependent, leupeptin-sensitive).
    • The second substrate (BZ-Gly-Gly-Arg-4-methoxy-2-naphthylamide) had a pH optimum of 6.7 and a Km of 3 x 10(-5) M.

    Conclusions:

    • Elevated proteinase activity is a hallmark of these mouse lung tumor models.
    • Cathepsin B-like enzymes may contribute to the altered proteolytic environment in lung tumors.
    • These findings highlight the potential of targeting specific proteinases in lung cancer therapy.