Letters to the Editor |
Department of Medicine, Kurume University School of Medicine, Kurume, Japan
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
To the Editor:
I have read two interesting papers about endogenous C-truncated splice isoform of secretory receptor for advanced glycation end products (esRAGE), which were recently published in your journal.1,2 The findings that esRAGE levels are correlated with serum pentosidine and carboxymethyllysine in type 1 diabetes by Miura et al1 are consistent with our and Tans previous observations that serum levels of total soluble form of RAGE (sRAGE) were positively, but not inversely, correlated with circulating AGE levels in nondiabetic and type 2 diabetic subjects, respectively.3,4 These observations suggest that endogenous esRAGE or sRAGE levels are not sufficient to eliminate circulating AGEs efficiently in vivo. However, Koyama et al2,5 recently reported in ATVB that decreased levels of esRAGE were associated with comorbidity including the metabolic syndrome and atherosclerosis and with cardiovascular mortality in end-stage renal disease patients. Therefore, it is unlikely that esRAGE protects against these devastating disorders by working as a decoy receptor for AGEs in vivo. Indeed, they also claimed in their article that pentosidine level was positively, but not inversely, associated with esRAGE.
In contrast to the case of esRAGE, circulating sRAGE levels are increased, rather than decreased, in both type 1 and type 2 diabetic patients.4,6,7 Further, the following evidence supports the concept that circulating sRAGE may be elevated in response to serum AGE levels and reflect tissue RAGE expression in diabetes, thereby acting as a negative feedback agent against the AGE-elicited vascular injury: (1) RAGE belongs to the same immunoglobulin superfamily as intercellular adhesion molecule-1
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