Galectin-3 (Galectin 3) is a Protein Coding gene. This gene encodes a member of the galectin family of carbohydrate-binding proteins. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. Galectin-3 is a beta-galactoside-binding lectin and plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion, and T-cell regulation. Galectin-3 has an important role in tumor progression throμgh inhibition of apoptosis. Galectin-3 expression is associated with neoplastic transformation and with differentiation of monocytes to macrophages. Elevated expression of Galectin-3 has been demonstrated in the synovium of rheumatoid arthritis (RA). Diseases associated with Galectin-3 include Follicular Adenoma and Papillary Carcinoma.
Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions.
The Galectin family of proteins; with specificity for Nacetyllactosamine containing glycoproteins; consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs).They also possess hemagglutination activity; which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide; they can be secreted by one or more as yet unidentified non-classical secretory pathways. They have diverse effects on many cellular functions including adhesion; migration; polarity; chemotaxis; proliferation; apoptosis; and differentiation. Galectins may play a key role in many pathological states; including autoimmune diseases; allergic reactions; inflammation; tumor cell metastasis; atherosclerosis; and diabetic complications.
LGALS7; also known as Galectin-7; is a member of the galectins family. The galectins are a family of beta-galactoside-binding proteins. There are at least 14 identified members in this family. Galectins share similarities in the CRD (the carbohydrate recognition domain). They are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide; galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are implicated in modulating cell-cell and cell-matrix interactions. LGALS7 contains 1 galectin domain and is mainly expressed in stratified squamous epithelium. Galectin-7 could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. LGALS7 is a pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly.
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