AGER-1,2,3 bind AGEs

Stable Identifier
R-HSA-879358
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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
1651976 Two novel rat liver membrane proteins that bind advanced glycosylation endproducts: relationship to macrophage receptor for glucose-modified proteins

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

J Exp Med 1991
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

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

Mol Med 1995
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