## Abstract We are interested in the regulation of intracellular calcium and the various diseases associated with an altered regulation of this second messenger. More recently, we also became interested in pathologies involving the Ca2+‐binding S100 proteins and AGEs and their association with the
Dietary AGEs and ALEs and risk to human health by their interaction with the receptor for advanced glycation endproducts (RAGE) – an introduction
✍ Scribed by Paul J. Thornalley
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 202 KB
- Volume
- 51
- Category
- Article
- ISSN
- 1613-4125
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The receptor for advanced glycation endproducts (RAGE) has a well‐substantiated role in cell dysfunction and mechanisms of inflammatory disease. The physiological agonists of RAGE are less certain: S100/calgranulin proteins, high mobility group‐1 protein HMGB1 and other proteins are candidate agonists. It increasingly appears unlikely proteins modified by advanced glycation endproducts are effective agonists in vivo. In the following debate, Professors Ann Marie Schmidt and Claus Heizmann gave arguments and evidences for and against the motion. Recent evidence suggesting the activation of RAGE impairs the enzymatic defence against glycation provided by glyoxalase 1 (Glo 1) suggests that studies of RAGE will continue to be of importance to our understanding of the physiological significance of protein glycation.
Pro arguments: http://dx.doi.org/10.1002/mnfr.200700008
Contra arguments: http://dx.doi.org/10.1002/mnfr.200600284
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