Protein phosphorylation in the blood-brain barrier. Possible presence of marcks in brain microvessels

The protein phosphorylation in rat brain microvessels has been examined; the major phosphorylated proteins correspond to a doublet of molecular weight 134–141 kDa, and four proteins of approx. 25, 55, 80 and 200 kDa. TPA (12- O-tetradecanoylphorbol-13-acetate) enhanced, in a few minutes, the phosphorylation of three major protein substrates with apparent molecular weights of 17.5, 44.5 and 80 kDa. These effects are inhibited by staurosporine. The 80 kDa protein resulted to be myristoylated alanine-rich C kinase substrate (MARCKS). This work demonstrates that protein kinase C plays an important role in protein phosphorylation in blood-brain barrier (BBB).