KMD Bioscience Co., Ltd.
400-621-6806
2023-08-03 Hits(431)
The galectin family consists of carbohydrate (glycan) binding proteins that are expressed by a wide variety of cells and bind to galactose-containing glycans. Galectins can be located in the nucleus or the cytoplasm, or can be secreted into the extracellular space. They can modulate innate and adaptive immune cells by binding to glycans on the surface of immune cells or intracellularly via carbohydrate-dependent or carbohydrate-independent interactions. Galectins expressed by immune cells can also participate in host responses to infection by directly binding to microorganisms or by modulating antimicrobial functions such as autophagy. Here we explore the diverse ways in which galectins have been shown to impact immunity and discuss the opportunities and challenges in the field.
Canonical pathways of immune regulation involve ligand–receptor interactions that transmit predicable signalling outcomes. The discrete nature of such ligand–receptor pairs, including the specific signalling pathways they engage, lends well to genetic and pharmacological approaches to define their biological functions. However, another level of essential immune regulation involves interactions of greater complexity. Mammals express various carbohydrate (glycan) binding proteins (GBPs) that recognize glycosylated proteins and glycosylated lipids (glycoconjugates). The targeted modifications on these glycoconjugates are highly variable. Glycan modifications cannot be predicted based on the amino acid sequence of a given glycoprotein but, instead, are dictated by the repertoire of glycosyltransferases and substrates responsible for their synthesis. As a result, the same protein (or lipid) can be decorated by different carbohydrate modifications depending on the type, differentiation and overall activation state of a given cell. In this way, the nature and abundance of glycans of a given glycoconjugate, not protein or lipid levels alone, can dictate how well a given GBP binds. As different glycoconjugates may express the same glycan structure, different proteins or lipids on a cell surface may be engaged by a given GBP, allowing GBPs to potentially modulate or activate various distinct receptors. Thus, the role of GBPs in immune signalling and regulation fundamentally differs from other immune regulators, such as cytokine-receptor pathways.
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