A. Faissner et al., ISOLATION OF A NEURAL CHONDROITIN SULFATE PROTEOGLYCAN WITH NEURITE OUTGROWTH-PROMOTING PROPERTIES, The Journal of cell biology, 126(3), 1994, pp. 783-799
Proteoglycans are expressed in various tissues on cell surfaces and in
the extracellular matrix and display substantial heterogeneity of bot
h protein and carbohydrate constituents. The functions of individual p
roteoglycans of the nervous system are not well characterized, partly
because specific reagents which would permit their isolation are missi
ng. We report here that the monoclonal antibody 473HD, which binds to
the surface of early differentiation stages of murine astrocytes and o
ligodendrocytes, reacts with the chondroitin sulfate/dermatan sulfate
hybrid epitope DSD-1 expressed on a central nervous system chondroitin
sulfate proteoglycan designated DSD-1-PG. When purified from detergen
t-free postnatal days 7 to 14 mouse brain extracts, DSD-1-PG displays
an apparent molecular mass between 800-1,000 kD with a prominent core
glycoprotein of 350-400 kD. Polyclonal anti-DSD-1-PG antibodies and mo
noclonal antibody 473HD react with the same molecular species as shown
by immunocytochemistry and sequential immunoprecipitation performed o
n postnatal mouse cerebellar cultures, suggesting that the DSD-1 epito
pe is restricted to one proteoglycan. DSD-1-PG promotes neurite outgro
wth of embryonic day 14 mesencephalic and embryonic day 18 hippocampal
neurons from rat, a process which can be blocked by monoclonal antibo
dy 473HD and by enzymatic removal of the DSD-1-epitope. These results
show that the hybrid glycosaminoglycan structure DSD-1 supports the mo
rphological differentiation of central nervous system neurons.