To: tuck who wrote (195 ) 3/17/2004 6:39:20 PM From: Biomaven Respond to of 946 Well it may be no more than coincidence, but I was just reading about NADPH oxidase and cancer in the context of MSHL's phenoxodiol:marshalledwardsinc.com It may conceivably be that the variant form (dubbed tNOX by the Morre's) is more susceptible to producing ROS in the presence of arsenic than the regular CNOX. Here's some more on tNOX:Cancer Lett. 2003 Feb 20;190(2):135-41. Related Articles, Links Sera from cancer patients contain two oscillating ECTO-NOX activities with different period lengths. Wang S, Morre DM, Morre DJ. Department of Foods and Nutrition, Purdue University, West Lafayette, IN, USA. ECTO-NOX protein's are cell surface-associated and growth-related hydroquinone oxidases with both protein disulfide-thiol interchange activity and the capacity to oxidize NAD(P)H. The activities of these ECTO-NOX proteins are not steady state but fluctuate to create a repeating pattern of oscillations. Two forms of ECTO-NOX activities have been distinguished. The constitutive ECTO-NOX (CNOX), is hormone responsive and refractory to quinone-site inhibitors. A tumor-associated NOX (tNOX) is unregulated, refractory to hormones and growth factors and responds to quinone-site inhibitors. CNOX proteins are widely distributed and exhibit oscillations in enzymatic activity with a period length of 24 min. tNOX proteins are cancer specific and exhibit oscillations with a period length of about 22 min. Our findings now demonstrate the presence of the novel oscillating tNOX activity in sera of patients with cancer whereas the constitutive NOX of non-cancer cells is present in sera of both cancer patients and healthy volunteers. We conclude that ECTO-NOX proteins in sera exhibit oscillatory characteristics similar to those of ECTO-NOX forms of the cell surface.