Ager-1,2,3 bind AGEs

Stable Identifier
R-NUL-879372
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
plasma membrane, extracellular region
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Ager-1,2,3 bind AGEs
In addition to AGER/RAGE, several other proteins have been identified as AGE-binding proteins. AGE binding proteins p60 and p90 (Yang et al. 1991) were subsequently identified as the Oligosaccharyl transferase 48 kDa subunit (Ost-48) and Glucosidease-2 subunit beta (Li et al. 1996). A third member was identified as Galectin-3 (Vlassara et al. 1995). These 3 proteins have been shown to be present on the plasma membrane of many cell types including vascular endothelium (Stitt et al. 1999). They have been designated AGE-R1, -R2 and -R3. Their suggested function is the removal and degradation of AGEs, but AGER-1 was found to negatively regulate AGER/RAGE (Lu et al. 2004), with kinetics that suggested a more complex interaction than simple competition for the same ligand.
Literature References
PubMed ID Title Journal Year
8529130 Identification of galectin-3 as a high-affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex

Cerami, A, Imani, F, Liu, FT, Yang, Z, Wojciechowicz, D, Vlassara, H, Li, YM

Mol Med 1995
1651976 Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

Brunelle, S, Suthanthiran, M, Cerami, A, Makita, Z, Yang, Z, Vlassara, H, Sehajpal, P, Horii, Y

J Exp Med 1991
Participants
Input
Output
Orthologous Events
AGER-1,2,3 bind AGEs (Homo sapiens)
Authored
Jupe, S  (2010-06-17)
Reviewed
Yan, SD  (2010-11-09)
Created
Jupe, S  (2010-06-17)
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