Endogenous cyclic AMP-stimulated phosphorylation of a Wolfgram protein component in rabbit central-nervous-system myelin.

Cyclic AMP-stimulated phosphorylation of membrane proteins in central-nervous-system myelin was investigated, with rabbit brain myelin. Subfractionation of a myelin membrane preparation by sucrose-density-gradient centrifugation produced a rapidly sedimenting population of membrane vesicles containing 5'-nucleotidase and acetylcholinesterase, a light membrane fraction containing myelin basic protein and 2',3'-cyclic nucleotide 3'-phosphodiesterase, and an intermediate membrane fraction containing the highest specific activity of 2',3'-cyclic nucleotide 3'-phosphodiesterase and a small proportion of myelin basic protein. Cyclic AMP stimulation of protein phosphorylation was confined to a protein of Mr 49 700, which co-electrophoresed with the upper component of the Wolfgram protein doublet. Cyclic AMP did not affect the phosphorylation of myelin basic protein. Cyclic AMP-stimulated phosphorylation of this protein followed 2',3'-cyclic nucleotide 3'-phosphodiesterase activity on subcellular fractionation and was correspondingly high in the intermediate or 'myelin-like' fraction on sucrose-density-gradient centrifugation.