N(epsilon)-carboxymethyllysine-modified proteins are unable to bind to RAGE and activate an inflammatory response.
Mol Nutr Food Res
; 52(3): 370-8, 2008 Mar.
Article
em En
| MEDLINE
| ID: mdl-18320574
ABSTRACT
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Albumina Sérica
/
Receptores Imunológicos
/
Inflamação
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Lactoglobulinas
/
Lisina
Limite:
Humans
Idioma:
En
Revista:
Mol Nutr Food Res
Assunto da revista:
CIENCIAS DA NUTRICAO
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
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