title: Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-sialic acid glycotopes on serum glycoproteins in mice.
abstract: 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 alpha2,3-, alpha2,6-, and alpha2,8-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 alpha2,3-Sia glycotope and Sambucus sieboldiana for the alpha2,6-Sia glycotopes, and monoclonal antibody 2-4B (mAb.2-4B) recognizing the di- and oligomers of the alpha2,8-Neu5Gc residue. There was an increase in a limited number of sialoglycoproteins containing the alpha2,3-, alpha2,6-, or alpha2,8-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 beta-galactoside alpha2,3-sialyltransferases (ST3Gal I and ST3Gal III) and beta-N-acetylgalactosaminide alpha2,6-sialyltransferase (ST6GalNAc VI) as well as beta-galactoside alpha2,6-sialyltransferase (ST6Gal I) mRNAs. Notably, ST3Gal I and III and ST6GalNAc VI are involved in the synthesis of the alpha2,3- and alpha2,6-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 alpha2,8-Sia glycotope. The mechanism for the increase in glycoprotein in inflamed mouse serum remains to be examined, as mRNA expression for all of the alpha2,8-sialyltransferases (ST8Sia I-VI) was unchanged during inflammation.
authors.affiliation: Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan.
authors.forename: Zenta
authors.initials: Z
authors.lastname: Yasukawa
authors.forename: Chihiro
authors.initials: C
authors.lastname: Sato
authors.forename: Ken
authors.initials: K
authors.lastname: Kitajima
mesh_terms: D000209:Acute-Phase Proteins / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D005786:Gene Expression Regulation; D006023:Glycoproteins / Q000097:blood / Q000737:chemistry* / Q000235:genetics; D007249:Inflammation / Q000097:blood / Q000139:chemically induced / Q000235:genetics; D051379:Mice; D012794:Sialic Acids / Q000097:blood / Q000737:chemistry* / Q000235:genetics
chemical_list: D000209:Acute-Phase Proteins; D006023:Glycoproteins; D012794:Sialic Acids