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Updated: Aug 10, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
15:43

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes

Published on: January 7, 2013

Inactivation of (Na-++K-+)-stimulated ATPase by a cytotoxic protein from cobra venom in relation to its lytic effects

A Zaheer, S H Noronha, A V Hospattankar

    Biochimica Et Biophysica Acta
    |June 25, 1975
    PubMed

    Insights

    Cobra venom

    Area of Science:

    • Biochemistry
    • Toxicology
    • Cell Biology

    Background:

    • Cytotoxic proteins from cobra venom (Naja naja) exhibit selective toxicity.
    • The (Na-++K-+)-ATPase enzyme is crucial for cell membrane function and ion transport.

    Purpose of the Study:

    • To investigate the mechanism of action of cytotoxic protein P6 from cobra venom.
    • To determine the effect of P6 protein on (Na-++K-+)-ATPase activity in various cell systems.

    Main Methods:

    • Studied the effects of P6 protein on (Na-++K-+)-ATPase in Yoshida sarcoma cells, erythrocytes, and cell lines (KB, Hela, L-132).
    • Assessed the correlation between P6-induced (Na-++K-+)-ATPase inhibition and lytic activity.
    • Attempted reconstitution of inactivated (Na-++K-+)-ATPase using phospholipids.

    Main Results:

    • P6 protein inhibited (Na-++K-+)-ATPase activity, correlating with its cytotoxic and lytic effects.
    • Reconstitution of enzyme activity was achieved with phosphatidylserine and phosphatidic acid.
    • P6 protein binds to membrane components of susceptible cells.

    Conclusions:

    • Cell lysis by P6 protein likely results from ion imbalance (K+, Na+) due to (Na-++K-+)-ATPase inhibition.
    • The protein's structure and basicity facilitate interaction with membrane lipids, affecting enzyme conformation and activity.

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