GALECTIN-3

Official Full Name

galectin 3

Organism

Homo sapiens

Gene ID

3958

Background

This gene encodes a member of the galectin family of carbohydrate binding proteins. Members of this protein family have an affinity for beta-galactosides. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. This protein can self-associate through the N-terminal domain allowing it to bind to multivalent saccharide ligands. This protein localizes to the extracellular matrix, the cytoplasm and the nucleus. This protein plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion and T-cell regulation. The protein exhibits antimicrobial activity against bacteria and fungi. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Oct 2014]

Synonyms

L31; GAL3; MAC2; CBP35; GALBP; GALIG; LGALS2

Protein Sequence

MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI

Open

Disease

Hypertension, Idiopathic interstitial pneumonitis, Melanoma, Non-alcoholic fatty liver disease, Psoriasis

Approved Drug

Clinical Trial Drug

2 +

Discontinued Drug

Clones

Cat.No.	Product Name	Price
CDCL184359	Human Galectin-3 ORF clone(NM_002306.3)	Inquiry
CDCL184360	Rat Galectin-3 ORF clone(NM_031832.1)	Inquiry

Detailed Information

Galectin-3 is a β-galactoside-binding protein with a molecular weight of 31,000. Its structure primarily consists of repeat sequences rich in proline and glycine, an amino-terminal domain, and a carboxy-terminal domain that can bind carbohydrates. Its structure mostly comprises an amino-terminal domain, repetitive sequences rich in proline and glycine, and a carboxy-terminal region capable of binding carbohydrates. It is also part of the Galectins family. Formed by the fusion of a carbohydrate recognition domain (CRD) with a collagen-like repeat domain, Galectin-3 is an intracellular and extracellular lectin that may interact with cell surface molecules, intracellular glycoproteins, and components of the extracellular matrix. Especially notably influencing the function of CD8+ T cells in HPV-positive head and neck squamous cell carcinoma, it performs several intracellular and extracellular activities supporting tumor angiogenesis, interacting with cell growth, adhesion, apoptosis, inflammation, immune control, tumor transformation, metastasis, and tumor progression.

Figure 1 describes the structure of Galectin-3 and its key functions in inflammation and fibrosis, illustrating its interaction sites and involvement in pathological processes. Figure 1. Galectin-3: structure and key functions in inflammation and fibrosis. (Bouffette S, et al., 2023)

Galectin-3 is very avid for β-galactose and significantly affects cell-to-cell and cell-to-matrix interactions as well as mRNA splicing. A multifunctional protein, galectin-3 has many biological activities. Activated macrophages, basophils, epithelial cells, and some sensory neurons show the maximum expression of it. Though it may also be found in the nucleus, cell surface, or extracellular area, it is mostly located in the cytoplasm. Widely spread throughout nature, particularly in mammals, members of the Galectin family help control immunological responses, cell adhesion, tumor development, and inflammation in many physiological and pathological contexts. Galectins are famous for their capacity to precisely identify and bind beta-galactosides. Mediating cell adhesion requires galectin-3, which also participates in cell-to-cell and cell-to-matrix adhesion. Using interactions with laminin, fibronectin, Mac-2 binding protein, and other matrix components, promotes adhesion and spreading, therefore indirectly boosting the growth and motility of many cells. Immune regulation and inflammation are also significantly influenced by galectins. Binding to cell surface glycol-complexes, they start a chain of intracellular signaling events that affect immune cell activation and function.

The following describes galectin-3 production, transport, and secretion: 1) there is no signal peptide; 2) free ribosomes in the cytoplasm create it; 3) it can be moved to organelles including the nucleus and mitochondria; 4) it can be released into the extracellular area.

Tumor cells, macrophages, epithelial cells, fibroblasts, and activated T cells mostly express Galectin-3 on their surface. Though expressed at modest levels in the brain, heart, and pancreas of mice, it is rather prevalent in the liver, ileum, kidneys, and adrenal glands; it also displays significant expression in the lungs, spleen, stomach, colon, uterus, and ovaries. Moreover, activated macrophages, basophils, epithelial cells, and some sensory neurons show greatest expression of Galectin-3.

Galectin-3 shows substantial variation in expression in various organs. It is weakly expressed in the heart and pancreas but strongly expressed in the liver, ileum, kidneys, and adrenal glands; it also exhibits high expression in the lungs, spleen, stomach, colon, uterus, and ovaries. The development of certain malignant tumors, including those in the stomach, intestines, central nervous system, and thyroid, is also linked to Galectin-3 expression in tumor cells.

References:

Bouffette S, Botez I, De Ceuninck F. Targeting galectin-3 in inflammatory and fibrotic diseases. Trends Pharmacol Sci. 2023 Aug;44(8):519-531.
Mackinnon AC, Tonev D, et al. Galectin-3: therapeutic targeting in liver disease. Expert Opin Ther Targets. 2023;27(9):779-791.
Procyk G, Czapla A, et al. The role of galectin-3 in atrial fibrillation. J Mol Med (Berl). 2023;101(12):1481-1492.

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