Nε-carboxymethyllysine-modified proteins are unable to bind to RAGE and activate an inflammatory response

被引：70

作者：

Buetler, Timo M. ^{[1
]}

Leclerc, Estelle ^{[2
]}

Baumeyer, Alexandra ^{[1
]}

Latado, Helia ^{[1
]}

Newell, John ^{[1
]}

Adolfsson, Oskar ^{[1
]}

Parisod, Veronique ^{[1
]}

Richoz, Janique ^{[1
]}

Maurer, Sarah ^{[1
]}

Foata, Francis ^{[1
]}

Piguet, Dominique ^{[1
]}

Junod, Sylviane ^{[1
]}

Heizmann, Claus W. ^{[3
]}

Delatour, Thierry ^{[1
]}

机构：

[1] Nestle Res Ctr, CH-1000 Lausanne 26, Switzerland

[2] Florida Atlantic Univ, Dept Chem & Biochem, Boca Raton, FL 33431 USA

[3] Univ Childrens Hosp, Div Clin Chem & Biochem, Zurich, Switzerland

来源：

MOLECULAR NUTRITION & FOOD RESEARCH | 2008年 / 52卷 / 03期

关键词：

carboxymethyllysine; inflammation; lactoglobulin; Maillard reaction; RAGE;

D O I：

10.1002/mnfr.200700101

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Advanced glycation endproducts (AGEs) containing carboxymethyllysine (CML) modifications are generally thought to be ligands of the receptor for AGEs, RAGEs. It has been argued that this results in the activation of pro-inflammatory pathways and diseases. However, it has not been shown conclusively that a CML-modified protein can interact directly with RAGE. Here, we have analyzed whether beta-lactoglobulin (bLG) or human serum albumin (HSA) modified chemically to contain only CML (10-40% lysine modification) can (i) interact with RAGE in vitro and (ii) interact with and activate RAGE in lung epithelial cells. Our results show that CML-modified bLG or HSA are unable to bind to RAGE in a cell-free assay system (Biacore). Furthermore, they are unable to activate pro-inflammatory signaling in the cellular system. Thus, CML probably does not form the necessary structure(s) to interact with RAGE and activate an inflammatory signaling cascade in RAGE-expressing cells.

引用

页码：370 / 378

页数：9

共 39 条

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