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Journal of Neuroscience, Vol 3, 2324-2335, Copyright © 1983 by Society for Neuroscience
Nerve fiber growth in culture on fibronectin, collagen, and glycosaminoglycan substrates
S Carbonetto, MM Gruver and DC Turner
In an initial report (Carbonetto, S. T., M. M. Gruver, and D. C. Turner
(1982) Science 216: 897-899) we described the use of 2-
hydroxyethylmethacrylate (HEMA) in preparing defined culture substrates for
studying nerve fiber growth. In those studies fibronectin and collagen were
conspicuous, among a variety of HEMA-embedded proteins, in supporting fiber
growth of embryonic neurons from chick dorsal root ganglia. Here we further
document and extend our preliminary studies, especially with regard to the
interaction of growing nerve fibers with fibronectin. HEMA substrates were
prepared with proteolytic fragments of fibronectin, each of which had one
or more of the functional sites of the intact molecule. Only those
fragments of fibronectin that retained the region of the molecule known to
mediate myoblast attachment were active in supporting nerve fiber growth.
When added in excess to the culture medium, the smallest of the active
fragments inhibited fiber growth on substrates that contained intact
fibronectin. In culture medium depleted of serum fibronectin, HEMA gels
containing collagens purified from connective tissues (types I and III) or
from basement membranes (type IV) were about as effective as HEMA
substrates containing fibronectin in supporting fiber growth. Nerve fiber
growth on collagen substrates proceeded in the absence of fibronectin in
the culture medium. Several glycosaminoglycans (heparin, chondroitin
sulfate, hyaluronic acid) were ineffective as substrates for fiber growth.
Treatment of HEMA/ fibronectin gels with heparin or incorporation of
heparin along with fibronectin in the gel profoundly diminished the
efficacy of fibronectin in supporting nerve fiber growth. Our studies
suggest that the growth of nerve fibers on fibronectin substrates results
from direct interaction with a specific portion of the fibronectin molecule
and that this interaction can be inhibited by heparin and possibly other
glycosaminoglycans.
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