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Journal of Neuroscience, Vol 6, 714-722, Copyright © 1986 by Society for Neuroscience
Immunocytochemical localization of tubulin and microtubule-associated protein 2 during the development of hippocampal neurons in culture
A Caceres, GA Banker and L Binder
In dissociated-cell cultures prepared from the embryonic rat hippocampus,
neurons establish both axons and dendrites, which differ in geometry, in
ultrastructure, and in synaptic polarity. We have used immunocytochemistry
with monoclonal antibodies to study the regional distribution of
beta-tubulin and micro-tubule-associated protein 2 (MAP2) in hippocampal
cultures and their localization during early stages of axonal and dendritic
development. After development for a week or more in culture, when axons
and dendrites were well- differentiated, the distribution of these two
proteins was quite different. Beta-tubulin was present throughout the nerve
cell, in soma, dendrites, and axon. It was also present in all classes of
non-neuronal cells, astrocytes, fibroblasts, and a presumptive glial
progenitor cell. In contrast, MAP2 was preferentially localized to nerve
cells; within neurons, MAP2 was present in soma and dendrites, but little
or no immunostaining was detectable in axons. Both beta-tubulin and MAP2
were present in nerve cells at the time of plating. From the earliest
stages of process extension, beta-tubulin was present in all neuronal
processes, both axons and dendrites. Surprisingly, MAP2 was also initially
present in both axons and dendrites, extending as far as the axonal growth
cone. With subsequent development, MAP2 staining was selectively lost from
the axon so that after 1 week in vitro little or no axonal staining
remained. Taken together with earlier results (Caceres et al., 1984a),
these data indicate that the establishment of neuronal polarity, as
manifested by the molecular differentiation of the axonal and dendritic
cytoskeleton, occurs largely under endogenous control, even under culture
conditions in which cell interactions are greatly restricted.(ABSTRACT
TRUNCATED AT 250 WORDS)
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