Letters in Drug Design & Discovery

Author(s): Madhuchhanda Kundu, Johnson Thomas, Arsenio M. Fialho, Jennifer M. Kwan, Leonilde M. Moreira, Magdy Mahfouz, Tapas K. Das Gupta and Ananda M. Chakrabarty

DOI: 10.2174/157018009789057580

DownloadDownload PDF Flyer Cite As
The Anticancer Activity of the N-Terminal CARD-Like Domain of Arginine Deiminase (ADI) from Pseudomonas aeruginosa

Page: [403 - 412] Pages: 10

  • * (Excluding Mailing and Handling)

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.

Keywords: Arginine deiminase (ADI), Azurin, Pseudomonas aeruginosa, CARD domain, Anticancer agents