An endogenous factor which interacts with synaptosomal membrane Na+, K+ ATPase activation by K+

G. RODRÍGUEZ DE LORES ARNAIZ (

NEUROCHEMICAL RESEARCH

SPRINGER/PLENUM PUBLISHERS

Lugar: New York; Año: 1993 vol. 18 p. 655 - 662

0364-3190

In previous papers, the isolation of brain soluble fractions able to modify neuronal Na+, K+-ATPase activity has been described. One of those fractions-peak I-stimulates membrane Na+, K+-ATPase while another-peak II-inhibits this enzyme activity, and has other ouabain-like properties. In the present study, synaptosomal membrane Na+, K+-ATPase was analyzed under several experimental conditions, using ATP orp-nitrophenylphosphate (p-NPP) as substrate, in the absence and presence of cerebral cortex peak II. Peak II inhibited K+-p-NPPase activity in a concentration dependent manner. Double reciprocal plots indicated that peak II uncompetitively inhibits K+-p-NPPase activity regarding substrate, Mg2+ and K+ concentration. Peak II failed to block the known K+-p-NPPase stimulation caused by ATP plus Na+. At various K+ concentrations, percentage K+-p-NPPase inhibition by peak II was similar regardless of the ATP plus Na+ presence, indicating lack of correlation with enzyme phosphorylation. Na+, K+-ATPase activity was decreased by peak II depending on K+ concentration. It is postulated that the inhibitory factor(s) present in peak II interfere(s) with enzyme activation by K+.