The Galectin family is a group of proteins that can specifically bind to β-galactosides such as N-acetyl lactosamine, the protein, and the glycosyl group are bound by either N-linkage or O-linkage. Galectins are an evolutionarily conserved family, and all Galectins contain a conserved carbohydrate recognition domain (CRD) of approximately 130 amino acids. Previously, galactose lectins were also referred to as S-type lectins because some galactose lectins are disulfide-dependent for binding to carbohydrates. Based on the special ability of Galectins, they can be used in Glycobiology Microarray Analysis, especially Lectin Microarray Assay.
Fig.1 Structure of human Galectin-9 in complex with N-acetyllactosamine dimer. (Wikipedia)
16 mammalian Galectins have been identified so far and 12 of which are expressed in humans. These Galectins are classified into three main types based on the number and arrangement of CRDs, and all three types of Galectins have well-defined CRDs with highly conserved amino acid sequences and β-sandwich structures.
Galectin-1, -2, -5, -7, -10, -11, -13, -14, -15, -16.
Prototype Galectins contain a single domain for recognizing CRD. Each Galectin has a distinct affinity for binding carbohydrates.
In mammals, there is only one chimeric Galectin, termed Galectin-3. It has also known by the names Mac-2 antigen, CBP35, and CBP30.
In different tissues and subcellular locations, Galectins have different functions and can bind carbohydrate-specific properties allowing them to play a key role in several intracellular and extracellular processes that bind to glycosylated proteins and lipids. Outside the cell, Galectins bind to the cell surface and extracellular matrix glycans, thus affecting a variety of cellular processes. Galectin can also be present in the cytoplasm and nucleus and may affect cellular functions through protein interactions with other cytoplasmic and nuclear proteins, such as intracellular signaling pathways and pre-mRNA shearing, etc. Galectins can be expressed by many different immune and inflammatory cells and are important regulators of immune and inflammatory responses. The response of immune cells to Galectin is also dependent on the specific glycosylation of surface glycoproteins to produce Galectin ligands. Selective and powerful Inhibitors for Galectins will be useful tools to research the biological activities of various Galectins due to their crucial roles in biology and to better understand the mechanism of action of Galectins in pertinent therapeutics.
Fig.2 Galectins in the MM BM microenvironment. (Storti, et al., 2017)
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