| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Published online before print May 18, 2007
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,1
* Department of Medicine, Yale University School of Medicine, New Haven, Connecticut, USA; and Departments of
Surgery and
Medicine, Columbia University Medical Center, New York, New York, USA
1 Correspondence: Division of Surgical Science, Department of Surgery, Columbia University Medical Center, 630 West 168th Street, P&S 17-501, New York, NY 10032, USA. E-mail: ams11{at}columbia.edu
ABSTRACT
The multiligand receptor for advanced glycation end products (RAGE) of the Ig superfamily transduces the biological impact of discrete families of ligands, including advanced glycation end products, certain members of the S100/calgranulin family, high mobility group box-1, Mac-1 (
Mβ2, CD11b/CD18), and amyloid-β peptide and β-sheet fibrils. Although structurally dissimilar, at least at the monomeric level, recent evidence suggests that oligomeric forms of these RAGE ligands may be especially apt to activate the receptor and up-regulate a program of inflammatory and tissue injury-provoking genes. The challenge in probing the biology of RAGE and its impact in acute responses to stress and the potential development of chronic disease is to draw the line between mechanisms that evoke repair versus those that sustain inflammation and tissue damage. In this review, we suggest the concept that the ligands of RAGE comprise a primal program in the acute response to stress. When up-regulated in environments laden with oxidative stress, inflammation, innate aging, or high glucose, as examples, the function of these ligand families may be transformed from ones linked to rapid repair to those that drive chronic disease. Identification of the threshold beyond which ligands of RAGE mediate repair versus injury is a central component in delineating optimal strategies to target RAGE in the clinic.
Key Words: inflammation • immunity
This article has been cited by other articles:
|
|
 |
|
  G. Bode, A. Luken, C. Kerkhoff, J. Roth, S. Ludwig, and W. Nacken Interaction between S100A8/A9 and Annexin A6 Is Involved in the Calcium-induced Cell Surface Exposition of S100A8/A9 J. Biol. Chem., November 14, 2008; 283(46): 31776 - 31784. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Raucci, S. Cugusi, A. Antonelli, S. M. Barabino, L. Monti, A. Bierhaus, K. Reiss, P. Saftig, and M. E. Bianchi A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10) FASEB J, October 1, 2008; 22(10): 3716 - 3727. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. A. Manfredi, A. Capobianco, A. Esposito, F. De Cobelli, T. Canu, A. Monno, A. Raucci, F. Sanvito, C. Doglioni, P. P. Nawroth, et al. Maturing Dendritic Cells Depend on RAGE for In Vivo Homing to Lymph Nodes J. Immunol., February 15, 2008; 180(4): 2270 - 2275. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Seth, J. Cui, E. To, M. Kwee, and J. Matsubara Complement-Associated Deposits in the Human Retina Invest. Ophthalmol. Vis. Sci., February 1, 2008; 49(2): 743 - 750. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
