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Journal of Neuroscience, Vol 15, 6419-6432, Copyright © 1995 by Society for Neuroscience
Biochemical properties and subcellular distribution of the neuronal class E calcium channel alpha 1 subunit
CT Yokoyama, RE Westenbroek, JW Hell, TW Soong, TP Snutch and WA Catterall
Department of Pharmacology, University of Washington, Seattle 98195, USA.
Anti-peptide antibodies specific for the neuronal calcium channel alpha 1E
subunit (anti-CNE1 and anti-CNE2) were produced to study the biochemical
properties and subcellular distribution of the alpha 1E polypeptide from
rat brain. Immunoblotting identified a single size form of 245-255 kDa
which was a substrate for phosphorylation by cAMP- dependent protein
kinase, protein kinase C, cGMP-dependent protein kinase, and
calcium/calmodulin-dependent protein kinase II. Ligand- binding studies of
alpha 1E indicate that it is not a high affinity receptor for the
dihydropyridine isradipine or the peptide toxins omega- conotoxin GVIA or
omega-conotoxin MVIIC at concentrations which elicit high affinity binding
to other channel types in the same membrane preparation. The alpha 1E
subunit is widely distributed in the brain with the most prominent
immunocytochemical staining in deep midline structures such as
caudate-putamen, thalamus, hypothalamus, amygdala, cerebellum, and a
variety of nuclei in the ventral midbrain and brainstem. Staining is
primarily in the cell soma but is also prominent in the dendritic field of
a discrete subset of neurons including the mitral cells of the olfactory
bulb and the distal dendritic branches of the cerebellar Purkinje cells.
Our observations indicate that the 245- 255 kDa alpha 1E subunit is
localized in cell bodies, and in some cases in dendrites, of a broad range
of central neurons and is potentially modulated by multiple second
messenger-activated protein kinase.
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