title: Role of galectin-3 as a receptor for advanced glycosylation end products.
abstract: The advanced glycosylation end product (AGE)-binding proteins identified so far include the components of the AGE-receptor complex p60, p90 and galectin-3, receptor for advanced glycosylation end products (RAGE), and the macrophage scavenger receptor types I and II. Galectin-3 interacts with beta-galactoside residues of several cell surface and matrix glycoproteins through the carbohydrate recognition domain and is also capable of peptide-peptide associations mediated by its N-terminus domain. These structural properties enable galectin-3 to exert multiple functions, including the modulation of cell adhesion, the control of cell cycle, and the mRNA splicing activity. Moreover, in macrophages, astrocytes, and endothelial cells, galectin-3 has been shown to exhibit a high-affinity binding for AGEs; the lack of a transmembrane anchor sequence or signal peptide suggests that it associates with other AGE-receptor components rather than playing an independent role as AGE-receptor. In tissues that are targets of diabetic vascular complications, such as the mesangium and the endothelium, galectin-3 is not expressed or only weakly expressed under basal conditions, at variance with p90 and p60 but becomes detectable with aging and is induced or up-regulated by the diabetic milieu, which only slightly affects the expression of p90 or p60. This (over)expression of galectin-3 may in turn modulate AGE-receptor-mediated events by modifying the function of the AGE-receptor complex, which could play a role in the pathogenesis of target tissue injury. Up-regulated galectin-3 expression may also exert direct effects on tissue remodeling, independently of AGE ligands, by virtue of its adhesive and growth regulating properties.
authors.affiliation: Department of Clinical Sciences, La Sapienza University, Rome, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Pricci
authors.forename: G
authors.initials: G
authors.lastname: Leto
authors.forename: L
authors.initials: L
authors.lastname: Amadio
authors.forename: C
authors.initials: C
authors.lastname: Iacobini
authors.forename: G
authors.initials: G
authors.lastname: Romeo
authors.forename: S
authors.initials: S
authors.lastname: Cordone
authors.forename: R
authors.initials: R
authors.lastname: Gradini
authors.forename: P
authors.initials: P
authors.lastname: Barsotti
authors.forename: F T
authors.initials: FT
authors.lastname: Liu
authors.forename: U
authors.initials: U
authors.lastname: Di Mario
authors.forename: G
authors.initials: G
authors.lastname: Pugliese
mesh_terms: D000818:Animals; D000943:Antigens, Differentiation / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D002448:Cell Adhesion; D002453:Cell Cycle; D048909:Diabetes Complications; D037502:Galectin 3; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D006801:Humans; D012326:RNA Splicing
chemical_list: D000943:Antigens, Differentiation; D037502:Galectin 3; D017127:Glycation End Products, Advanced