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Glycobiology Advance Access published online on April 11, 2006
Glycobiology, doi:10.1093/glycob/cwj112
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org. The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org
Received January 28, 2006
Revised March 31, 2006
Accepted April 4, 2006

Article

Identification of disialic acid-containing glycoproteins in mouse serum: A novel modification of immunoglobulin light chains, vitronectin, and plasminogen

Zenta Yasukawa 1, Chihiro Sato 1 *, Kotone Sano 2, Haruko Ogawa 2, and Ken Kitajima 1 *

1 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, JAPAN; Laboratory of Animal Cell Function, Bioscience and Biotechnology Center
2 Department of Advanced BioSciences, Graduate School of Humanities and Sciences, Ochanomizu University, Tokyo 112-8610, JAPAN

* To whom correspondence should be addressed.
Chihiro Sato, E-mail: chi{at}agr.nagoya-u.ac.jp
Ken Kitajima, E-mail: kitjaima{at}agr.nagoya-u.ac.jp


  Abstract

Serum glycoproteins are involved in various biologic activities, such as the removal of exogenous antigens, fibrinolysis, and metal transport. Some of them are also useful markers of inflammation and disease. Although the amount of sialic acid increases following inflammation, little attention has been paid to the presence of linkage-specific epitopes in serum, especially the {alpha}2,8-linkage. In a previous study, we demonstrated that four components in mouse serum contain {alpha}2,8-linked disialic acid, based on immunoreactivity with monoclonal antibody 2-4B (mAb.2-4B), which is specific to Neu5Gc {alpha}2->(8Neu5Gc {alpha}2->)n-1, n≥2 [Yasukawa, Z. et al. (2005) Glycobiology 15, 827-837]. In this study, we purified three components, 30 kDa-gp, 70 kDa-gp, and 120 kDa-gp, and identified them as an immunoglobulin light chain, vitronectin, and plasminogen, respectively, using matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy analyses. Modifications of these proteins with {alpha}2,8-linked disialic acid were chemically confirmed by fluorometric C7/C9 analyses and mild acid hydrolysates-fluorometric anion exchange chromatography analyses. We also demonstrated that the IgG, IgM and IgE light chains are commonly modified with {alpha}2,8-linked disialic acid. In addition, both mouse and rat vitronectin contained disialic acid and the amount of disialylation in vitronectin dramatically decreased after hepatectomy. These results indicate that a novel disialic acid-modification of serum glycoproteins is biologically important for immunologic events and fibrinolysis.

Keywords: disialic acid/serum glycoprotein/immunoglobulin light chain/vitronectin/plasminogen.
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