Glycobiology Advance Access published online on April 27, 2005
Glycobiology, doi:10.1093/glycob/cwi068
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1 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences; Laboratory of Animal Cell Function, Bioscience and Biotechnology Center
* To whom correspondence should be addressed. Acute-phase serum proteins increase in response to inflammatory stimuli. Most of those proteins are glycoproteins that often contain sialic acids (Sia). It is unknown, however, how the expression of Sia in these glycoproteins changes during inflammation. The present study demonstrates changes in the
Received September 28, 2004
Revised April 10, 2005
Accepted April 24, 2005
Article
Inflammation-dependent changes in
2,3-, 2,6-, and 2,8-sialic acid glycotopes on serum glycoproteins in mouse
2 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences; Institute for Advanced Research, Nagoya University, Nagoya 464-8601, JAPAN
3 Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences; Laboratory of Animal Cell Function, Bioscience and Biotechnology Center; Institute for Advanced Research, Nagoya University, Nagoya 464-8601, JAPAN
Ken Kitajima, E-mail: kitajima{at}agr.nagoya-u.ac.jp
Abstract 
2,3-, 2,6-, and 2,8-Sia glycotopes on serum glycoproteins in response to turpentine oil-induced inflammation, based on lectin- and immunoblot analyses using sialyl linkage-specific lectins, Maackia amurensis for the 2,3-Sia glycotope and Sambucus sieboldiana for the 2,6-Sia glycotopes, and monoclonal antibody 2-4B recognizing the di- and oligomers of the 2,8-Neu5Gc residue. There was an increase in a limited number of sialoglycoproteins containing the 2,3-, 2,6-, or 2,8-Sia glycotopes. Reverse transcription-polymerase chain reaction analysis of the expression profiles of mRNAs for the known sialyltransferases in mouse liver during inflammation indicated upregulated expression of 
-galactoside 2,3-sialyltransferases (ST3Gal I, and ST3Gal III), and -N-acetylgalactosaminide 2,6-sialyltransferase (ST6GalNAc VI) as well as -galactoside 2,6-sialyltransferase (ST6Gal I) mRNAs. Notably, ST3Gal I and III and ST6GalNAc VI, are involved in the synthesis of the 2,3- and 2,6-Sia glycotopes on O-glycan chains and possibly on gangliosides, while ST6Gal I is specific for N-glycan chains. These results provide an evidence for the inflammation-induced expression of sialyl glycotopes in serum glycoproteins. We demonstrated that inflammation significantly increased the expression of an unknown 32-kDa glycoprotein containing the 2,8-Sia glycotope. The mechanism for the increase in glycoprotein in inflamed mouse serum remains to be examined, as mRNA expression for all of the 2,8-sialyltransferases (ST8Sia I-VI) was unchanged during inflammation.
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