The anticancer activity of the N-terminal CARD-like domain of arginine deiminase (ADI) from Pseudomonas aeruginosa

Madhuchhanda Kundu, Johnson Thomas, Arsenio M. Fialho, Jennifer M. Kwan, Leonilde M. Moreira, Magdy Mahfouz, Tapas K. Das Gupta, Ananda M. Chakrabarty

    Research output: Contribution to journalArticlepeer-review

    5 Scopus citations

    Abstract

    While arginine deiminase (ADI) from Mycoplasma arginini is a well-known anticancer agent, very little is known about any such role of ADI from other bacteria. Additionally, M. arginini ADI is believed to exert its anticancer activity due to depletion of arginine from cancer cells. In this report, we demonstrate anticancer activity of ADI from Pseudomonas aeruginosa. We have also cloned and expressed a truncated form from the P. aeruginosa ADI which harbors a caspase recruitment domain (CARD). This polypeptide, called Pa-CARD, demonstrates anticancer activity without exhibiting any ADI enzymatic activity by inducing apoptosis in cancer cells but not in normal cells. Microarray experiments suggest that Pa-CARD modulates NF-kB signaling pathway genes to exert its anticancer activity.

    Original languageEnglish (US)
    Pages (from-to)403-412
    Number of pages10
    JournalLetters in Drug Design and Discovery
    Volume6
    Issue number6
    DOIs
    StatePublished - Sep 2009

    Keywords

    • Anticancer agents
    • Arginine deiminase (ADI)
    • Azurin
    • CARD domain
    • Pseudomonas aeruginosa

    ASJC Scopus subject areas

    • Pharmaceutical Science
    • Drug Discovery
    • Molecular Medicine

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