Do vanadium ions exert any specific effect on brain protein phosphorylation.

It has been shown previously (1) that vanadate stimulates phosphorylation of the overall proteins from the synaptic membranes of rat cerebral cortex. The aim of the present experiments was to investigate whether the action of vanadate and also of vanadyl ions could exert any specific effect on endogenous phosphorylation of proteins from subcellular fractions of the rat brain cortex. Both vanadate and vanadyl ions stimulate phosphorylation of the overall proteins from synaptic membranes and to lesser extent from mitochondria. An attempt was made to estimate the contribution of inhibition of ATPase activity to nonspecific stimulation of phosphate labeling in the synaptic membrane fraction. A band of Mr approx. 37 kDa from synaptic membranes was particularly sensitive to vanadate. In mitochondria both vanadate and vanadyl caused a marked, concentration dependent inhibition of phosphorylation of a band corresponding to Mr approx. 34 kDa. The effect was confined exclusively to the mitochondrial fractions (total, perikaryal and two synaptic types). It was absent in all subcellular fractions tested, including the nuclear one. Phosphorylation of the mitochondrial 34 kDa band is not influenced by cyclic AMP, Ca-calmodulin, shift of pH from 6.6 to 8.1. Alkaline hydrolysis removed almost all phosphate-labeled bands of mitochondria, including that of 34 kDa.