Erratum: Carboxylated N‐glycans on RAGE promote S100A12 binding and signaling, in Journal of Cellular Biochemistry, by Srikrishna et al.
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ABSTRACT: The receptor for advanced glycation end products (RAGE) is a signaling receptor protein of the immunoglobulin superfamily implicated in multiple pathologies. It binds a diverse repertoire of ligands, but the structural basis for the interaction of different ligands is not well understood. We earlier showed that carboxylated glycans on the V-domain of RAGE promote the binding of HMGB1 and S100A8/A9. Here we study the role of these glycans on the binding and intracellular signaling mediated by another RAGE ligand, S100A12. S100A12 binds carboxylated glycans, and a subpopulation of RAGE enriched for carboxylated glycans shows more than 10-fold higher binding potential for S100A12 than total RAGE. When expressed in mammalian cells, RAGE is modified by complex glycans predominantly at the first glycosylation site (N25IT) that retains S100A12 binding. Glycosylation of RAGE and maximum binding sites for S100A12 on RAGE are also cell type dependent. Carboxylated glycan-enriched population of RAGE forms higher order multimeric complexes with S100A12, and this ability to multimerize is reduced upon deglycosylation or by using non-glycosylated sRAGE expressed in E. coli. mAbGB3.1, an antibody against carboxylated glycans, blocks S100A12-mediated NF-kappaB signaling in HeLa cells expressing full-length RAGE. These results demonstrate that carboxylated N-glycans on RAGE enhance binding potential and promote receptor clustering and subsequent signaling events following oligomeric S100A12 binding.Journal of Cellular Biochemistry 06/2010; 110(3):645-59. · 3.06 Impact Factor
Erratum: Carboxylated N-glycans on RAGE promote
S100A12 binding and signaling, in Journal of Cellular
Biochemistry, by Srikrishna et al.
Subsequent to the publication of Srikrishna et al. the following
inaccuracies were discovered:
Dr. Achim Temme’s affiliation should have been: Department of
Neurosurgery, University Hospital Carl Gustav Carus, TU Dresden,
01307 Dresden, Germany
Dr. Bernd Weigle’s affiliation should have been: Institute of
The funding source for Drs. Dorit Hanein and Neils Volkmann,
Department of Defense Office of the Congressionally Directed
Medical Research Programs Proposal; Grant Number: 09082003,
should have been National Institutes of Health Cell Migration
Consortium; Grant Number: U54 GM64346 (D.H. and N.V.). This
change is applicable to both the grant sponsors listed on the lead
page and also within the acknowledgement section.
Further, in light of these post-publication corrections the online
version of the originally published article has been updated
accordingly. Please consider this revised version to be the version
Srikrishna G, Nayak J, Weigle B, Temme A, Foell D, Hazelwood L, Olsson A,
Volkmann N, Hanein D, Freeze HH. 2010. Carboxylated N-glycans on RAGE
promote S100A12 binding and signaling. J Cell Biochem. 110:645–659.
Journal of Cellular
Journal of Cellular Biochemistry 111:248 (2010)
DOI 10.1002/jcb.22746 ? ? 2010 Wiley-Liss, Inc.
Published online 12 July 2010 in Wiley Online Library (wileyonlinelibrary.com).