Galectin-3

1A3K, 1KJL, 1KJR, 2NMN, 2NMO, 2NN8, 2XG3, 3AYA, 3AYC, 3AYD, 3AYE, 3T1L, 3T1M, 3ZSJ, 3ZSK, 3ZSL, 3ZSM, 4BLI, 4BLJ, 4BM8, 4JC1, 4JCK, 4LBJ, 4LBK, 4LBL, 4LBM, 4LBN, 4LBO, 4R9A, 4R9B, 4R9C, 4R9D, 4RL7, 4XBN, 5H9R, 5H9P395816854ENSG00000131981ENSMUSG00000050335P17931P16110NM_001177388NM_002306NM_001357678NM_001145953NM_010705NP_002297NP_001344607n/aGalectin-3 is a protein that in humans is encoded by the LGALS3 gene. Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified.1a3k: X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION1kjl: High Resolution X-Ray Structure of Human Galectin-3 in complex with LacNAc1kjr: Crystal Structure of the human galectin-3 CRD in complex with a 3'-derivative of N-Acetyllactosamine2nmn: Crystal structure of human galectin-3 carbohydrate-recognising domain at 2.45 angstrom resolution2nmo: Crystal structure of human galectin-3 carbohydrate-recognition domain at 1.35 angstrom resolution2nn8: Crystal structure of human galectin-3 carbohydrate-recognition domain with lactose bound, at 1.35 angstrom resolution Galectin-3 is a protein that in humans is encoded by the LGALS3 gene. Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified. Galectin-3 is approximately 30 kDa and, like all galectins, contains a carbohydrate-recognition-binding domain (CRD) of about 130 amino acids that enable the specific binding of β-galactosides. Galectin-3 (Gal-3) is also a member of the beta-galactoside-binding protein family that plays an important role in cell-cell adhesion, cell-matrix interactions, macrophage activation, angiogenesis, metastasis, apoptosis. Galectin-3 is encoded by a single gene, LGALS3, located on chromosome 14, locus q21–q22. Galectin-3 is expressed in the nucleus, cytoplasm, mitochondrion, cell surface, and extracellular space. Galectin-3 has an affinity for beta-galactosides and exhibits antimicrobial activity against bacteria and fungi. This protein has been shown to be involved in the following biological processes: cell adhesion, cell activation and chemoattraction, cell growth and differentiation, cell cycle, and apoptosis. Given galectin-3's broad biological functionality, it has been demonstrated to be involved in cancer, inflammation and fibrosis, heart disease, and stroke. Studies have also shown that the expression of galectin-3 is implicated in a variety of processes associated with heart failure, including myofibroblast proliferation, fibrogenesis, tissue repair, inflammation, and ventricular remodeling. Galectin-3 associates with the primary cilium and modulates renal cyst growth in congenital polycystic kidney disease. A correlation between galectin-3 expression levels and various types of fibrosis has been found. Galectin-3 is upregulated in cases of liver fibrosis, renal fibrosis, and idiopathic pulmonary fibrosis (IPF). In several studies with mice deficient in or lacking galectin-3, conditions that caused control mice to develop IPF, renal, or liver fibrosis either induced limited fibrosis or failed to induce fibrosis entirely. Companies have developed galectin modulators that block the binding of galectins to carbohydrate structures. The galectin-3 inhibitor, TD139 and GR-MD-02 have the potential to treat fibrosis. Elevated levels of galectin-3 have been found to be significantly associated with higher risk of death in both acute decompensated heart failure and chronic heart failure populations. In normal human, murine, and rat cells galectin-3 levels are low. However, as heart disease progresses, significant upregulation of galectin-3 occurs in the myocardium.