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J Biol Chem, Vol. 275, Issue 20, 15422-15431, May 19, 2000

Frequent Occurrence of Pre-existing 28-Linked Disialic and Oligosialic Acids with Chain Lengths Up to 7 Sia Residues in Mammalian Brain Glycoproteins
PREVALENCE REVEALED BY HIGHLY SENSITIVE CHEMICAL METHODS AND ANTI-DI-, OLIGO-, AND POLY-Sia ANTIBODIES SPECIFIC FOR DEFINED CHAIN LENGTHS^*

Chihiro Sato, Hideyuki Fukuoka, Kaoru Ohta, Tsukasa Matsuda, Rika Koshino^§, Kazukiyo Kobayashi^§, Frederic A. Troy II^¶, and Ken Kitajima

From the  Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, the ^§ Department of Biotechnology, Graduate School of Engineering, Nagoya University, Nagoya 464-8601, Japan and the ^¶ Department of Biological Chemistry, University of California School of Medicine, Davis, California 95616

The pre-existence of 28-linked disialic acid (di-Sia) and oligosialic acid (oligo-Sia) structures with up to 7 Sia residues was shown to occur on a large number of brain glycoproteins, including neural cell adhesion molecules (N-CAMs), by two highly sensitive chemical methods (Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1998) Anal. Biochem. 261, 191-197; Sato, C., Inoue, S., Matsuda, T., and Kitajima, K. (1999) Anal. Biochem. 266, 102-109). This unexpected finding was also confirmed using a newly developed antibody prepared using a copolymer of 28-linked N-acetylneuraminyl p-vinylbenzylamide and acrylamide as an immunogen and known antibodies whose immunospecificities were determined to be di- and oligo-Sia residues with defined chain lengths. The major significance of the new finding that di- and oligo-Sia chains exist on a large number of brain glycoproteins is 2-fold. First, it reveals a surprising diversity in the number and M_r of proteins distinct from N-CAM that are covalently modified by these short sialyl glycotopes. Second, it suggests that synthesis of di- and/or oligo-Sia units may be catalyzed by 28-sialyltransferase(s) that are distinct from the known polysialyltransferases, STX and PST, which are partially responsible for polysialylation of N-CAM.

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^* This work was supported in part by grants-in-aid for International Scientific Research, Joint Research, for Scientific Research on Priority Areas, for Scientific Research (C) (to K. Kitajima), the Japan Society for the Promotion of Science Research Fellow from the Ministry of Education, Science, Sports and Culture, Hayashi Memorial Foundation for Female Natural Science (to C. S.), and United States Public Health Service National Institutes of Health Grant GM55703 (to F. A. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Fax: 81-52-789-4128; E-mail: kitajima@agr.nagoya-u.ac.jp.

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Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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