Watanabe M, Isobe T, Okuyama T, Ichimura T, Kuwano R, Takahashi Y, Kondo H
Department of Anatomy, Tohoku University School of Medicine, Sendai, Japan.
Brain Res Mol Brain Res. 1991 May;10(2):151-8. doi: 10.1016/0169-328x(91)90105-7.
Activation of tyrosine and tryptophan hydroxylases, key enzymes for the catecholamine and serotonin biosynthesis, requires Ca2+/calmodulin-dependent protein kinase II and 14-3-3 protein which comprises a family of, at least, seven polypeptides in the bovine. Here we show that the amino acid sequence of the rat 14-3-3 eta chain deduced from the nucleotide sequence is completely identical to that of bovine counterpart. Using in situ hybridization the expression of mRNA for this protein is detected not only in the monoamine-synthetic neurons but also in many other discrete nuclei which synthesize neither catecholamine nor serotonin. The highly conservative structure between mammalian species and wider expression of this protein than expected in the central nervous system suggest that the 14-3-3 protein exerts some, though yet to be defined, functions fundamental to neuronal activities other than activation of the monoamine biosynthesis.
