Glycobiology Advance Access originally published online on April 27, 2005
Glycobiology 2005 15(9):827-837; doi:10.1093/glycob/cwi068
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Inflammation-dependent changes in 
2,3-, 2,6-, and 2,8-sialic acid glycotopes on serum glycoproteins in mice
2 Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan; 3 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan; and 4 Institute for Advanced Research, Nagoya University, Nagoya 464-8601, Japan
1 To whom correspondence should be addressed; e-mail: kitajima{at}agr.nagoya-u.ac.jp
Received on September 28, 2004; revised on April 10, 2005; accepted on April 24, 2005
The expression of acute-phase serum proteins increases in response to inflammatory stimuli. Most of these proteins are glycoproteins that often contain sialic acids (Sia). It is unknown, however, how the expression of Sia in these glycoproteins changes during inflammation. This study demonstrates changes in the 
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 by 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 (mAb.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 (RT–PCR) analysis of the expression profiles of mRNAs for the known sialyltransferases in mouse liver during inflammation indicated the up-regulated expression of ß-galactoside 2,3-sialyltransferases (ST3Gal I and ST3Gal III) and ß-N-acetylgalactosaminide 2,6-sialyltransferase (ST6GalNAc VI) as well as ß-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, whereas ST6Gal I is specific for N-glycan chains. These results provide 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.
Key words: disialic acid / inflammation / oligosialic acid / serum glycoprotein / sialyltransferase
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