LGALS3

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LGALS3

A gene on chromosome 14q22.3 that encodes a galectin family-type carbohydrate-binding protein, which can self-associate through the N-terminal domain, bind to multivalent saccharide ligands and localise to the extracellular matrix, cytoplasm and nucleus. The LGALS3 protein product plays a role in various cell functions including apoptosis, innate
immunity, cell adhesion and T-cell regulation.
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To date, 15 different members have been identified, which are classified according to their biochemical structure into three groups: (a) prototype galectins, including galectin- (Gal-) 1, -2, -5, -7,10, -11, -13, -14, and -15, display one carbohydrate-recognition domain (CRD) and can dimerize; (b) tandem-repeat galectins, including Gal-4, -6, -8, -9, and -12, exhibit two CRDs associated with a linker peptide; and (c) the unique chimera-type Gal-3 contains one CRD and an additional nonlectin domain and can oligomerize [1].
However, in broad contrast to Gal-3, Gal1 expression was not increased over time.
The novel cardiac biomarker galectin-3 (Gal-3) is a beta galactoside binding lectin involved in fibrogenesis and inflammatory response in the failing heart.
Out of the 272 patients, 67 (24.6%) patients had RODCM and 57 (85%) patients with RODCM had Gal-3 measured at baseline with complete follow-up data and were thus included in the present analysis (Figure 1).
Background: Galectin-3 (Gal-3) plays a role in the mechanisms underlying ocular venous malformation.
Galectin-3 (Gal-3), a member of the lectin family, is involved in several cellular processes such as cell adhesion, proliferation, apoptosis, and messenger RNA (mRNA) splicing.[sup][7] However, it remains unclear whether Gal-3 is involved in the pathogenesis of ocular venous malformation.
Galectin-3 (Gal-3) has also been suggested as a critical mediator of immunomodulatory actions of human MSC [4, 5].
Based on staining intensities of Gal1 and Gal-3 antibodies in ovarian tissue sections, staining results were graded as negative (-), weak (+), moderate (++) and intense (+++) (Vaskivuo et al, 2002).
Galectins have been subdivided into three groups (Figure 1(a)) based on their structure and the number of CRD: (a) prototype Gals are constituted by a single CRD (Gals-1, -2, -5, -7, -10, -11, -13, and -14); (b) tandem-repeat Gals, by 2 different but homologous CRDs, connected by a linker region (Gals-4, -6, -8, -9, and -12); (c) chimera-Gals, represented by a unique member: Gal-3, consisted by a single CRD fused to a tail of short tandem repeats.
Galectin-3 (Gal-3), a protein member of the lectinfamily, binds to [beta]-galactosides and is widely expressed in epithelial and immune cells.
Galectin-3 (Gal-3) is a multifunctional [beta]-galactoside-binding lectin highly expressed in a variety of inflammatory and epithelial cells [17].
They can be structurally classified into three groups: prototype galectins (Galectins 1, 2, 5, 7, 10, 11, 13, 14, and 15) that have a single CRD; tandem galectins (Galectins 4,6, 8, 9, and 12), with 2 distinct but homologous CRDs; and the chimera-type group, of which Galectin-3 (Gal-3) is the only member, with a C-terminal CRD and a large N-terminal (NT) protein-binding domain (reviewed in [3]).