NAD(P)H-DEPENDENT PRODUCTION OF OXYGEN REACTIVE SPECIES BY THE SALIVARY-GLANDS OF THE MOSQUITO ANOPHELES-ALBIMANUS

Salivary gland homogenates of the adult female mosquito Anopheles albi manus, but not those of Aedes aegypti, induced light production in the presence of NADPH and luminol, indicating a NADPH oxidase activity pr oducing reactive oxygen species (superoxide anion) by the anopheline s alivary homogenate. Superoxide production by the anopheline salivary h omogenate was also confirmed by the NADPH-dependent, superoxide dismut ase inhibitable, reduction of cytochrome c. The NADPH oxidase reaction measured by light production in the presence of luminol was inhibited by superoxide dismutase and catalase, Both NADH and NADPH were substr ates for the production of oxygen reactive species by the salivary hom ogenate. Activity, as measured by luminol-dependent light emission, wa s enhanced one order of magnitude in the presence of 1.6 mg/ml of eith er phosphatidylserine or bovine serum albumin, Molecular sieving and h ydroxyapatite chromatography of the salivary homogenate showed coeluti on of the NADPH oxidase activity with the previously reported salivary peroxidase activity. It is suggested that the salivary peroxidase of Anopheles albimanus has the ability of producing superoxide in the pre sence of NADPH, and this may provide the peroxidase with substrates ne cessary for peroxidation of vasoconstrictor amines such as serotonin, released by aggregating platelets at the site of mosquito probing and feeding. Copyright (C) 1996 Elsevier Science Ltd.