The mechanism by which dietary AGEs are a risk to human health is via their interaction with RAGE: Arguing against the motion
- 13 September 2007
- journal article
- review article
- Published by Wiley in Molecular Nutrition & Food Research
- Vol. 51 (9) , 1116-1119
- https://doi.org/10.1002/mnfr.200600284
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 multifunctional Receptor for Advanced Glycation Endproducts (RAGE). Introduction: http://dx.doi.org/10.1002/mnfr.200700017 Pro arguments: http://dx.doi.org/10.1002/mnfr.200700008Keywords
Funding Information
- Nestec
This publication has 23 references indexed in Scilit:
- An update of the S100 nomenclatureBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2006
- Expression and purification of recombinant human receptor for advanced glycation endproducts in Escherichia coliProtein Expression and Purification, 2006
- Association of Advanced Glycation End Products with A549 Cells, a Human Pulmonary Epithelial Cell Line, Is Mediated by a Receptor Distinct from the Scavenger Receptor Family and RAGEThe Journal of Biochemistry, 2006
- The Importance of Calcium-Binding Proteins in Childhood DiseasesThe Journal of Pediatrics, 2005
- Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammationGlycobiology, 2005
- S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature)Biochemical and Biophysical Research Communications, 2004
- Effect of advanced glycation end products on endotoxin-induced TNF-a, IL-1b and IL-8 in human peripheral blood mononuclear cellsClinical Nephrology, 2004
- Calcium signalling: dynamics, homeostasis and remodellingNature Reviews Molecular Cell Biology, 2003
- RAGE Mediates a Novel Proinflammatory Axis: A Central Cell Surface Receptor for S100/Calgranulin PolypeptidesPublished by Elsevier ,1999
- A soluble protein characteristic of the nervous systemBiochemical and Biophysical Research Communications, 1965