Si. Sano et al., DIFFERENT SUBSETS OF CNS NEURONS EXPRESS DIFFERENT GLYCOSAMINOGLYCAN EPITOPES ON LARGE PERINEURONAL PROTEOGLYCANS, Brain research, 630(1-2), 1993, pp. 65-74
Proteoglycans are known to occur in the central nervous tissue, but th
eir function is not well understood. We made a biochemical study of fo
ur perineuronal antigens on different subsets of rat brain neurons and
found that three antigens recognized by antibodies against glycosamin
oglycan epitopes were large proteoglycans. Molecular masses estimated
by immunoblotting were 700 kDa for 473, 376 and 1B5 antigens and 600 k
Da for the 374 antigen. Reactivities of the antigens on immunoblots to
monoclonal antibodies (MAbs) 473 and 376 were lost, and that to MAb 1
B5 uncovered, after chondroitinase ABC treatment as in the brain secti
ons. The elution profiles from ion-exchange and gel-filtration column
chromatography of 473, 376 and 1B5 antigens were quite similar, but th
ose of 374 antigen were slightly different. The immunoaffinity-purifie
d 473 antigen migrated at 700 kDa on sodium dodecylsulfate gel electro
phoresis, and chondroitinase ABC treatment decreased the molecular mas
s to 600 kDa. The 473 antigen was recognized by MAbs 376 and 1B5 altho
ugh these MAbs also reacted with 473-negative 700 kDa molecules. These
results suggest that neuronal subset-specific glycosylation may occur
on the 700 kDa proteoglycans, and that the glycosaminoglycan structur
es may be involved in the pericellular diversity of CNS neurons.