Author/Authors :
Yantiri، نويسنده , , Ferda and Morré، نويسنده , , D.James and Yagiz، نويسنده , , Kader and Barogi، نويسنده , , Silvia and Wang، نويسنده , , Sui and Chueh، نويسنده , , Pin-Ju and Cho، نويسنده , , NaMi and Sedlak، نويسنده , , Dagmar and Morré، نويسنده , , Dorothy M.، نويسنده ,
Abstract :
NADH oxidases of low specific activities from urine of cancer patients were found to be inhibited or stimulated by the vanilloid capsaicin (8-methyl-N-vanillyl-6-noneamide). Similar activities, inhibited or stimulated by capsaicin, were reported previously for sera of cancer patients but not for sera of normal volunteers or for patients with disorders other than cancer. Like those from sera, the activities from urine were resistant to heat and to digestion with proteinase K. Two different fractions with capsaicin-responsive NADH oxidase activities were obtained by FPLC. One fraction in which the 33-kDa band was the major component exhibited NADH oxidase activity stimulated by capsaicin. Another fraction in which 66-kDa and 45-kDa bands were major components exhibited NADH oxidase activities inhibited by capsaicin. A monoclonal antibody generated to a ca 34-kDa form of the NADH oxidase from sera reacted with a urine protein of a ca 33-kDa band in the capsaicin-stimulated fraction. The 33-kDa protein was of low abundance and was estimated to be present in amounts between 5 and 100 μg/L, depending on the particular patient.
