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Journal of Neuroscience, Vol 6, 850-858, Copyright © 1986 by Society for Neuroscience
Novel monoclonal antibodies provide evidence for the in situ existence of a nonphosphorylated form of the largest neurofilament subunit
VM Lee, MJ Carden and JQ Trojanowski
We have obtained five monoclonal antibodies to the Mr 200,000 neurofilament
component (NF200) after immunization with polypeptides purified from
enzymatically dephosphorylated bovine neurofilaments. In immunoblots of
untreated neurofilament protein and protein from filaments exposed to
phosphatase, these antibodies recognize nonphosphorylated or
dephosphorylated, but not phosphorylated, forms of NF200. The epitopes
recognized by these new monoclonal antibodies reside in the carboxyterminal
domain of the NF200 polypeptide as defined by immunoreaction with limited
chymotryptic fragments. Immunohistochemical studies of bovine cerebellum,
spinal cord, trigeminal ganglion, and trigeminal nerve with these new
monoclonal antibodies demonstrate immunoreactivity primarily in neuronal
perikarya; axons and dendrites are weakly or infrequently immunostained.
After enzymatic dephosphorylation of these tissues, a more extensive
distribution of immunoreactivity is seen, especially in axons and
dendrites. Immunostaining of cultured rat sympathetic neurons is restricted
to cell bodies. These data provide evidence for the in situ existence of
NF200 epitopes that are not phosphorylated in some classes of neurons or
regions of a neuron, but are modified by phosphorylation in other neurons
or neuronal domains. These new monoclonal antibodies are distinctly
different from those in a large library (over 100) raised to, and specific
for, phosphorylated neurofilament proteins. They are novel tools for
probing neurofilament distribution, metabolism, structure, and possibly
function.
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