Glycobiology Advance Access originally published online on April 11, 2006
Glycobiology 2006 16(7):651-665; doi:10.1093/glycob/cwj112
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Identification of disialic acid-containing glycoproteins in mouse serum: a novel modification of immunoglobulin light chains, vitronectin, and plasminogen
3 Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, and 4 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan; and 5 Department of Advanced BioSciences, Graduate School of Humanities and Sciences, Ochanomizu University, Tokyo 112-8610, Japan
1 To whom correspondence should be addressed; e-mail: chi{at}agr.nagoya-u.ac.jp
2 To whom correspondence should be addressed; e-mail: kitjaima{at}agr.nagoya-u.ac.jp
Received on January 28, 2006; revised on March 31, 2006; accepted on April 4, 2006
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 
2,8-linkage. In a previous study, we demonstrated that four components in mouse serum contain 2,8-linked disialic acid (diSia), based on immunoreactivity with monoclonal antibody 2-4B, which is specific to N-glycolylneuraminic acid (Neu5Gc)2
(8Neu5Gc2)n–1, n 
2 [Yasukawa et al., (2005) Glycobiology, 15, 827–837]. In this study, we purified three components, 30-, 70-, and 120-kDa gp, and identified them as an immunoglobulin (Ig) light chain, vitronectin, and plasminogen, respectively, using matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy analyses. Modifications of these proteins with 2,8-linked diSia 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 2,8-linked diSia. In addition, both mouse and rat vitronectin contained diSia, and the amount of disialylation in vitronectin dramatically decreased after hepatectomy. These results indicate that a novel diSia modification of serum glycoproteins is biologically important for immunologic events and fibrinolysis.
Key words: disialic acid / immunoglobulin light chain / plasminogen / serum glycoprotein / vitronectin
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