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Minimum stable structure of the receptor for advanced glycation end product possesses multi ligand binding ability.

Abstract：

:The receptor for advanced glycation end products (RAGE) is a multi-ligand receptor involved in the development of diabetic complications. Although the soluble form of the extracellular domain maintains the ability to bind multi-ligands, it is unstable and degrades into several peptide species during storage. Proteolysis with thrombin or factor Xa revealed several protease sensitive sites. Most sensitive site is located between Arg228 and Val229, and peptide bond next to Arg216, Arg116, Arg114 and Trp271 are also cleaved. Seven truncated extracellular domains of RAGE were engineered in order to obtain a stable soluble fragment. RAGE 143 (Ala23-Thr143) is not only protease resistant but also shows the same ligand-binding ability as that of the full-length extracellular domain. The resultant minimum RAGE 143 works as a stable recognition devise to detect advanced glycation end products (AGEs).

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kumano-Kuramochi M,Ohnishi-Kameyama M,Xie Q,Niimi S,Kubota F,Komba S,Machida S

doi

10.1016/j.bbrc.2009.05.142

subject

Has Abstract

pub_date

2009-08-14 00:00:00

pages

130-4

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)01120-6

journal_volume

386

pub_type

杂志文章

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