Role of galectin-3 as a receptor for advanced glycosylation end products

F. Pricci, G. Leto, L. Amadio, C. Iacobini, G. Romeo, S. Cordone, R. Gradini, P. Barsotti, F. T. Liu, U. Di Mario, G. Pugliese

Research output: Contribution to journalArticle

72 Citations (Scopus)

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 β-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.

Original languageEnglish
JournalKidney international. Supplement
Volume58
Issue number77
Publication statusPublished - 2000

Fingerprint

Galectin 3
Advanced Glycosylation End Products
Scavenger Receptors
Diabetic Angiopathies
Galactosides
Peptides
Membrane Glycoproteins
Protein Sorting Signals
Cell Cycle Checkpoints
Advanced Glycosylation End Product-Specific Receptor
Cell Adhesion
Astrocytes
Adhesives
Endothelium
Carrier Proteins
Endothelial Cells
Macrophages
Carbohydrates
Ligands
Messenger RNA

Keywords

  • AGE-receptor
  • Cell adhesion
  • Diabetic complications
  • Nonenzymatic glycation

ASJC Scopus subject areas

  • Nephrology

Cite this

Pricci, F., Leto, G., Amadio, L., Iacobini, C., Romeo, G., Cordone, S., ... Pugliese, G. (2000). Role of galectin-3 as a receptor for advanced glycosylation end products. Kidney international. Supplement, 58(77).

Role of galectin-3 as a receptor for advanced glycosylation end products. / Pricci, F.; Leto, G.; Amadio, L.; Iacobini, C.; Romeo, G.; Cordone, S.; Gradini, R.; Barsotti, P.; Liu, F. T.; Di Mario, U.; Pugliese, G.

In: Kidney international. Supplement, Vol. 58, No. 77, 2000.

Research output: Contribution to journalArticle

Pricci, F, Leto, G, Amadio, L, Iacobini, C, Romeo, G, Cordone, S, Gradini, R, Barsotti, P, Liu, FT, Di Mario, U & Pugliese, G 2000, 'Role of galectin-3 as a receptor for advanced glycosylation end products', Kidney international. Supplement, vol. 58, no. 77.
Pricci F, Leto G, Amadio L, Iacobini C, Romeo G, Cordone S et al. Role of galectin-3 as a receptor for advanced glycosylation end products. Kidney international. Supplement. 2000;58(77).
Pricci, F. ; Leto, G. ; Amadio, L. ; Iacobini, C. ; Romeo, G. ; Cordone, S. ; Gradini, R. ; Barsotti, P. ; Liu, F. T. ; Di Mario, U. ; Pugliese, G. / Role of galectin-3 as a receptor for advanced glycosylation end products. In: Kidney international. Supplement. 2000 ; Vol. 58, No. 77.
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AU - Iacobini, C.

AU - Romeo, G.

AU - Cordone, S.

AU - Gradini, R.

AU - Barsotti, P.

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AU - Pugliese, G.

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