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Evidence for the presence of N‐CAM 180 on astrocytes from rat cerebellum and differences in glycan structures between N‐CAM 120 and N‐CAM 140
Author(s) -
Sasaki Tasuku,
Endo Tamao
Publication year - 1999
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/(sici)1098-1136(199912)28:3<236::aid-glia7>3.0.co;2-#
Subject(s) - gene isoform , glycan , astrocyte , biology , epitope , neural cell adhesion molecule , lectin , monoclonal antibody , biochemistry , glycosylation , microbiology and biotechnology , glycoprotein , cell , antibody , cell adhesion , immunology , neuroscience , gene , central nervous system
Differences in the N‐linked oligosaccharides on isoforms of the neural cell adhesion molecule (N‐CAM) on astrocytes were found using a lectin, namely, Datura stramonium agglutinin (DSA). Integral proteins of astrocytes prepared from newborn rat cerebella were solubilized with Nonident P‐40 and then separated into two fractions, an unbound fraction and a bound fraction, by a DSA‐agarose column. Both fractions thus obtained were subjected to immunoblotting using an anti‐N‐CAM monoclonal antibody. In the DSA‐bound fraction, N‐CAM 180 was found as well as N‐CAM 120 and N‐CAM 140. On the other hand, N‐CAM 180 was not detected in the unbound fraction, whereas N‐CAM 120 and N‐CAM 140 were. Furthermore, N‐CAM 180 did not carry the HNK‐1 epitope, whereas the other two isoforms did. Although the presence of N‐CAM 180 on astrocytes was controversial until recently, the results shown here indicate that N‐CAM 180 exists on rat astrocytes and exclusively carries a glycan structure reacting with DSA. This is the first demonstration of the production of N‐CAM glycoforms carrying different oligosaccharides by a homogeneous astrocyte preparation. These results suggest that the glycosylation of each N‐CAM isoform might be regulated independently. Whether each N‐CAM with different glycans participates in different functions remains to be established. GLIA 28:236–243, 1999. © 1999 Wiley‐Liss, Inc.