Neurocan and brevican are related chondroitin sulfate proteoglycans which a
re mainly expressed in the central nervous system. Neurocan and the secrete
d brevican variant are composed of globular N-terminal hyaluronan binding d
omains, central O-linked oligosaccharide attachment regions, and globular C
-terminal domains. Interaction studies of mouse brain proteoglycans reveale
d that neurocan, but not brevican, was retained on a heparin affinity matri
x. Also a recombinantly produced C-terminal fragment of neurocan, expressed
by HEK 293 cells, was retained by the heparin affinity matrix. The substit
ution of this fragment with a chondroitin sulfate chain did not inhibit bin
ding to the heparin affinity matrix at physiological NaCl concentrations, b
ut decreased the NaCl concentration necessary for elution. Two potential co
nsequences of the heparin binding ability of neurocan are an enforcement of
the interaction with other heparin binding molecules and a directed secret
ion by polarized cells. (C) 2000 Academic Press.