A panel of monoclonal antibodies specific of alpha-tubulin (TU-01, TU-
09) and beta-tubulin (TU-06, TU-13) subunits was used to study the loc
ation of N-terminal structural domains of tubulin in adult mouse brain
. The specificity of antibodies was confirmed b immunoblotting experim
ents. Immunohistochemical staining of vi bratome sections from cerebra
l cortex, cerebellum, hippocampus, and corpus callosum showed that ant
ibodies TU-01, TU-09, and TU13 reacted with neuronal and glial cells a
nd their processes, whereas the TU-06 antibody stained only the perika
rya. Dendrites and axons were either unstained or their staining was v
ery weak. As the TU-06 epitope is located on the N-terminal structural
domain of beta-tubulin, the observed staining pattern cannot be inter
preted as evidence of a distinct subcellular localization of beta-tubu
lin isotypes or known post-translational modifications. The limited di
stribution of the epitope could, rather, reflect differences between t
he conformations of tubulin molecules in microtubules of somata and ne
urites or, alternatively, a specific masking of the corresponding regi
on on the N-terminal domain of beta-tubulin by interacting protein(s)
in dendrites and axons.