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Journal of Neuroscience, Vol 13, 2863-2873, Copyright © 1993 by Society for Neuroscience
A heparan sulfate proteoglycan in developing avian axonal tracts
W Halfter
Department of Neurobiology, University of Pittsburgh, Pennsylvania 15261.
A neuronal heparan sulfate proteoglycan was identified by a panel of four
monoclonal antibodies. The antibodies were generated from mice immunized
with embryonic chick retina basal lamina (clones 3A12, 3A3, and 9E10) and
embryonic chick optic tract (clone 6D2). Cross-reactivity of all four
antibodies with the purified proteoglycan confirmed that the antibodies
were directed to the same antigen. Antibodies to heparan sulfate
proteoglycan from embryonic chick muscle or EHS mouse tumor (perlecan) did
not cross-react with the neuronal heparan sulfate proteoglycan, suggesting
that the two proteoglycans are not related. In Western blots, the
proteoglycan had a molecular weight of 600 kDa that dropped to 250 kDa when
the samples were treated with heparitinase or nitric acid.
Immunocytochemistry showed that in early stages of chick and quail
development, the proteoglycan was exclusively localized in basal laminae
and had a distribution similar to that of laminin. During further
development, a strong labeling was also found in the extracellular
environment of nerve tracts, such as the optic nerve and white matter areas
of the brain and spinal cord. The labeling of axonal tracts declined from
embryonic day 10 onward, while labeling in basal laminae persisted.
Antibodies to muscle heparan sulfate proteoglycan or to perlecan did not
label nerve fibers. The data show that embryonic neuronal tissue expresses
a new type of heparan sulfate proteoglycan.
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