Abstract
Galectins are a family of lectins that bind β-galactose-containing glycoconjugates and are characterized by carbohydrate-recognition domains (CRDs). Galectins exploit several biological functions, including angiogenesis, regulation of immune cell activities and cell adhesion, in both physiological and pathological processes, as tumor progression. Multiple myeloma (MM) is a plasma cell (PC) malignancy characterized by the tight adhesion between tumoral PCs and bone marrow (BM) microenvironment, leading to the increase of PC survival and drug resistance, MM-induced neo-angiogenesis, immunosuppression and osteolytic bone lesions. In this review, we explore the expression profiles and the roles of galectin-1, galectin-3, galectin-8 and galectin-9 in the pathophysiology of MM. We focus on the role of these lectins in the interplay between MM and BM microenvironment cells showing their involvement in MM progression mainly through the regulation of PC survival and MM-induced angiogenesis and osteoclastogenesis. The translational impact of these pre-clinical pieces of evidence is supported by recent data that indicate galectins could be new attractive targets to block MM cell growth in vivo and by the evidence that the expression levels of LGALS1 and LGALS8, genes encoding for galectin-1 and galectin-8 respectively, correlate to MM patients’ survival.
Highlights
Galectins are a family of lectins, evolutionarily conserved and with the ability to bind glycans [1]
We focus on the role of these lectins in the interplay between MM and bone marrow (BM) microenvironment cells showing their involvement in MM progression mainly through the regulation of plasma cell (PC) survival and MM-induced angiogenesis and osteoclastogenesis
Based on the number and the structure of carbohydrate-recognition domains (CRDs), galectins are divided in three groups: prototype that have only a CRD that can associate in dimer, tandem repeat-type that carry two CRDs linked by a short peptide linker, and chimera-type that has a CRD connected to a non-lectin amino-terminal region that allow the oligomerization into pentamers [1,2,4]
Summary
Galectins are a family of lectins, evolutionarily conserved and with the ability to bind glycans [1]. Galectins can bind to cell surface glycoconjugates, bearing the N-acetyl-lactosamine (Galβ(1-4)GlcNAc; LacNAc) disaccharide, forming a galectin–glycan structure called lattice, and mediating an intracellular signal transduction [1,6,7,8]. They can bind to some glycoproteins of the extracellular matrix, such as laminin, fibronectin and elastin [9]. Each member of the galectin family exhibits preferences in different glycan binding [10], which could explain their differences in biological and pathophysiological functions and the wide range of identified receptors on cell surfaces [2,11].
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