Journal of Neuroscience, Vol 6, 199-207, Copyright © 1986 by Society for Neuroscience
Heterogeneous localization of protein kinase C in rat brain: autoradiographic analysis of phorbol ester receptor binding
PF Worley, JM Baraban and SH Snyder
Protein kinase C is a calcium- and phospholipid-stimulated enzyme present
in high concentration in the brain. Phorbol esters are potent tumor
promoters that bind to specific receptors with high affinity. Several lines
of evidence indicate that the phorbol ester receptor is identical to
protein kinase C. To determine the distribution of protein kinase C, we
have localized phorbol ester receptors in the rat brain by autoradiography,
using [3H]phorbol 12,13-dibutyrate ([3H]PDBu) and have performed a variety
of lesions to assess the nature of the cellular elements possessing the
binding sites. The [3H]PDBu binding sites in the rat brain are discretely
localized and primarily associated with neurons. Evidence is presented for
localization to intrinsic neurons of the cortex and hippocampus, terminals
of the striatonigral projection, a projection to the molecular layer of the
dentate gyrus, and to dendrites of Purkinje cells.