The protein encoded by this gene is a soluble beta-galactoside binding lectin. The encoded protein is found as a homodimer and can bind to lymphotoxin-alpha. A single nucleotide polymorphism in an intron of this gene can alter the transcriptional level of the protein, with a resultant increased risk of myocardial infarction.
The Galectin family of proteins 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. 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 tandem repeat 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. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.
Galectin-3(LGALS3) is also known as Galactose-specific lectin 3; Mac-2 antigen; Carbohydrate-binding protein 35; Laminin-binding protein and Galactoside-binding protein. LGALS3 is highly expressed in early stages of papillary carcinoma; and lowly during tumor progression. LGALS3 is probably forms homo- or heterodimers and secreted by a non-classical secretory pathway and associates with the cell surface. LGALS3 plays an important role during the acquisition of vasculogenic mimicry and angiogenic properties. LGLAS3 takes part in an immune regulator to inhibit T-cell immune responses and promote tumor growth; as a result providing a new mechanism for tumor immune tolerance.
Leukotriene A-4 hydrolase; also known as LTA-4 hydrolase; Leukotriene A (4) hydrolase; LTA4H and LTA4; is cytoplasm protein which belongs to thepeptidase M1 family. LTA4H hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). This enzyme also has some peptidase activity. The leukotrienes (LTs) are a class of structurally related lipid mediators involved in the development and maintenance of inflammatory and allergic reactions. In the biosynthesis of LTs; arachidonic acid was converted into the unstable intermediate epoxide LTA4; which may in turn be conjugated with glutathione to form the spasmogenic LTC4; or hydrolyzed into the proinflammatory lipid mediator LTB4 in a reaction catalyzed by Leukotriene A4 hydrolase (LTA4H). LTB4 is a classical chemoattractant of human neutrophils and triggers adherence and aggregation of leukocytes to vascular endothelium; and also modulates immune responses. As a bifunctional zinc metalloenzyme; LTA4H also exhibits an anion-dependant arginyl aminopeptidase activity of high efficiency and specificity in addition to its epoxide hydrolase activity. LTA4H is regarded as a therapeutic target for inflammation.
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