title: Galectin-3: an emerging all-out player in metabolic disorders and their complications.
abstract: Galectin-3 has been increasingly recognized as an important modulator of several biological functions, by interacting with several molecules inside and outside the cell, and an emerging player in numerous disease conditions. Galectin-3 exerts various and sometimes contrasting effects according to its location, type of injury or site of damage. Strong evidence indicates that galectin-3 participates in the pathogenesis of diabetic complications via its receptor function for advanced glycation end-products (AGEs) and advanced lipoxidation end-products (ALEs). AGEs/ALEs are produced to an increased extent in target organs of complications, such as kidney and vessels; here, lack of galectin-3 impairs their removal, leading to accelerated damage. In contrast, in the liver, AGE/ALE tissue content and injury are decreased, because lack of galectin-3 results in reduced uptake and tissue accumulation of these by-products. Some of these effects can be explained by changes in the expression of receptor for AGEs (RAGE), associated with galectin-3 deletion and consequent changes in AGE/ALE tissue levels. Furthermore, galectin-3 might exert AGE/ALE- and RAGE-independent effects, favoring resolution of inflammation and modulating fibrogenesis and ectopic osteogenesis. These effects are mediated by intracellular and extracellular galectin-3, the latter via interaction with N-glycans at the cell surface to form lattice structures. Recently, galectin-3 has been implicated in the development of metabolic disorders because it favors glucose homeostasis and prevents the deleterious activation of adaptive and innate immune response to obesogenic/diabetogenic stimuli. In conclusion, galectin-3 is an emerging all-out player in metabolic disorders and their complications that deserves further investigation as the potential target of therapeutic intervention.
authors.affiliation: Department of Clinical and Molecular Medicine, "La Sapienza" University, Via di Grottarossa, 1035-1039, Rome 00189, Italy giuseppe.pugliese@uniroma1.it.
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Pugliese
authors.affiliation: Department of Clinical and Molecular Medicine, "La Sapienza" University, Via di Grottarossa, 1035-1039, Rome 00189, Italy.
authors.forename: Carla
authors.initials: C
authors.lastname: Iacobini
authors.affiliation: DINOGMI, University of Genoa Medical School, Genoa 16132, Italy.
authors.forename: Carlo M
authors.initials: CM
authors.lastname: Pesce
authors.affiliation: Department of Clinical and Molecular Medicine, "La Sapienza" University, Via di Grottarossa, 1035-1039, Rome 00189, Italy.
authors.forename: Stefano
authors.initials: S
authors.lastname: Menini
mesh_terms: D000818:Animals; D037502:Galectin 3 / Q000502:physiology*; D006801:Humans; D007249:Inflammation / Q000378:metabolism; D008659:Metabolic Diseases / Q000276:immunology / Q000378:metabolism*; D000067759:Receptor for Advanced Glycation End Products / Q000378:metabolism
chemical_list: C000593871:AGER protein, human; D037502:Galectin 3; D000067759:Receptor for Advanced Glycation End Products
keywords: advanced glycation end-products; advanced lipoxidation end-products; galectin-3; metabolic disorders; receptor for AGEs