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J Biol Chem, Vol. 273, Issue 5, 2575-2582, January 30, 1998
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From the The occurrence of the Department of Biophysics and Biochemistry,
Graduate School of Science, University of Tokyo, Hongo-7, Tokyo 113, Japan, the ¶ Department of Applied Biological Sciences, School of
Agricultural Sciences, Nagoya University, Chikusa, Nagoya 464-01, Japan, and the Institute of Biological Chemistry, Academia
Sinica, Nankang, Taipei 115, Taiwan
2
8-linked oligomeric
form of N-glycolylneuraminic acid (oligo-Neu5Gc) residues
in mammalian glycoproteins was unequivocally demonstrated using a newly
developed anti-oligo/poly-Neu5Gc monoclonal antibody as well as by
chemical and biochemical methods. First, the antibody, designated
mAb.2-4B, which specifically recognized oligo/poly-Neu5Gc with a
degree of polymerization of >2, was developed by establishing a
hybridoma cell line from P3U1 myeloma cells fused with splenocytes from
an MRL autoimmune mouse immunized with
dipalmitoylphosphatidylethanolamine-conjugated oligo/poly-Neu5Gc. Second, oligo-Neu5Gc was shown to occur in glycoproteins derived from
pig spleen by Western blot analysis using mAb.2-4B, which was also
confirmed by fluorometric high performance liquid chromatographic analysis of the product of periodate oxidation/reduction/acid hydrolysis of the purified glycopeptide fractions and by TLC and 600-MHz 1H NMR spectroscopic analysis of their mild acid
hydrolysates. Finally, the ubiquitous occurrence of oligo-Neu5Gc chains
as glycoproteinaceous components in Wistar rat tissue was
immunochemically indicated. This is the first example demonstrating the
diversity in oligo/poly-Sia structure in mammalian glycoproteins, where
only poly-N-acetylneuraminic acid is known to occur. Such
diversity in oligo/poly-Sia structure also implicates a diverged array
of biological functions of this glycan unit in glycoproteins.
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