| Literature DB >> 17239818 |
Norihiko Sasaki1, Hideki Yoshida, Takashi J Fuwa, Akiko Kinoshita-Toyoda, Hidenao Toyoda, Yoshio Hirabayashi, Hideki Ishida, Ryu Ueda, Shoko Nishihara.
Abstract
The GalNAcbeta1,4GlcNAc (LacdiNAc or LDN) structure is a more common structural feature in invertebrate glycoconjugates when compared with the Galbeta1,4GlcNAc structure. Recently, beta1,4-N-acetylgalactosaminyltransferase (beta4GalNAcT) was identified in some invertebrates including Drosophila. However, the LDN structure has not been reported in Drosophila, and the biological function of LDN remains to be determined. In this study, we examined acceptor substrate specificity of Drosophila beta4GalNAcTA by using some N- and O-glycans on glycoproteins and neutral glycosphingolipids (GSLs). GalNAc was efficiently transferred toward N-glycans, O-glycans, and the arthro-series GSLs. Moreover, we showed that dbeta4GalNAcTA contributed to the synthesis of the LDN structure in vivo. The dbeta4GalNAcTA mRNA was highly expressed in the developmental and adult neuronal tissues. Thus, these results suggest that dbeta4GalNAcTA acts on the terminal GlcNAc residue of some glycans for the synthesis of LDN, and the LDN structure may play a role in the physiological or neuronal development of Drosophila.Entities:
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Year: 2007 PMID： 17239818 DOI： 10.1016/j.bbrc.2007.01.015
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575