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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2007;27:e33.)
© 2007 American Heart Association, Inc.

Letters to the Editor

Assaying Soluble Forms of Receptor for Advanced Glycation End Products

Yasuhiko Yamamoto; Junnosuke Miura; Shigeru Sakurai; Takuo Watanabe; Hideto Yonekura; Hironori Tamei; Hirokazu Matsuki; Ken-ichi Obata; Yasuko Uchigata; Yasuhiko Iwamoto; Hidenori Koyama; Hiroshi Yamamoto

Department of Biochemistry and Molecular Vascular Biology (Y.Y., S.S., T.W., H. Yamamoto), Kanazawa University Graduate School of Medical Science, Kanazawa; Diabetes Center (J.M., Y.U., Y.I.), Tokyo Women’s Medical University School of Medicine, Tokyo; Department of Biochemistry (H. Yonekura), Kanazawa Medical University, Kanazawa; Research Laboratory (H.T., H.M., K.O.), Daiichi Fine Chemical Co Ltd, Takaoka; Department of Metabolism, Endocrinology, and Molecular Medicine (H.K.), Osaka City University Graduate School of Medicine, Osaka, Japan.

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In response:

Yamagishi and Imaizumi speculate that kinetics and role of circulating total soluble form of receptor for advanced glycation endproducts (soluble receptor for AGE, sRAGE) may be different from those of endogenous secretory RAGE (esRAGE) in diabetes. They also suggest an alternative interpretation that serum sRAGE level may reflect tissue membrane form of RAGE expression.

Currently, 2 different types of sandwich enzyme-linked immunosorbent assays (ELISAs) are commercially available and used for measurement of circulating soluble RAGE proteins: [1] esRAGE ELISA from B-Bridge Int. esRAGE is a splice variant form of RAGE lacking transmembrane domain and secreting into extracellular space and the circulation.¹ Sakurai et al developed its specific detection system using a capture monoclonal antibody (Ab) recognizing RAGE-extracellular domain and a detection polyclonal Ab for the esRAGE-specific C-terminal 16 amino acid sequence.² This ELISA system is not influenced by coexistence of AGE ligands.² [2] sRAGE ELISA from R&D Systems, which detects heterogenous population of total sRAGE proteins including (1) esRAGE, (2) (3) cleavage forms by metalloproteinases³ of membrane-bound full-length RAGE and esRAGE, and (4) other splice variant forms of RAGE. Similar to RAGE, esRAGE protein also has the common digestion site recognized by the proteinases, yielding deletion of the C-terminal sequence characteristic to esRAGE. These 2 assay systems are, however, constituted by individual Ab and different standard proteins. Indeed, plasma esRAGE levels in healthy subjects were found to be 5-fold less than plasma sRAGE.⁴ To precisely compare plasma sRAGE and esRAGE level, we developed another total sRAGE ELISA system . . . [Full Text of this Article]