Blockade of receptor for advanced glycation endproducts: A new target for therapeutic intervention in diabetic complications and inflammatory disorders

Barry I. Hudson, Loredana G. Bucciarelli, Thoralf Wendt, Taichi Sakaguchi, Evanthia Lalla, Wu Qu, Yan Lu, Larisse Lee, David M. Stern, Yoshifumi Naka, Ravichandran Ramasamy, Shi Du Yan, Shi Fang Yan, Vivette D'Agati, Ann Marie Schmidt

Research output: Contribution to journalReview articlepeer-review

147 Scopus citations

Abstract

The glycation and oxidation of proteins/lipids leads to the generation of a new class of biologically active moieties, the advanced glycation endproducts (AGEs). Recent studies have elucidated that carboxymethyllysine (CML) adducts of proteins/lipids are a highly prevalent AGE in vivo. CML-modified adducts are signal transduction ligands of the receptor for AGE (RAGE), a member of the immunoglobulin superfamily. Importantly, CML-modified adducts accumulate in diverse settings. In addition to enhanced formation in settings of high glucose, these adducts form in inflammatory milieu. Studies performed both in vitro and in vivo have suggested that the proinflammatory/tissue destructive consequences of RAGE activation in the diabetic/inflamed environment may be markedly attenuated by blockade of the ligand-RAGE axis. Here, we will summarize the known consequences of RAGE activation in the tissues and highlight novel areas for therapeutic intervention in these disease states.

Original languageEnglish (US)
Pages (from-to)80-88
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume419
Issue number1
DOIs
StatePublished - Nov 1 2003
Externally publishedYes

Keywords

  • Diabetes
  • Glycation
  • Inflammation
  • Oxidation
  • RAGE
  • Receptors

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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