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Galectin-10 is a member of the galectin family, encoded by the CLC gene, and is the principal constituent of Charcot-Leyden crystals found in eosinophilic inflammatory conditions such as asthma[1][3][4]. It functions as a lectin and lysophospholipase, hydrolyzing lysophosphatidylcholine, and participates in immune regulation, notably within regulatory T-cells. Galectin-10 forms homodimers with a unique structure distinct from other prototype galectins and is found in the cytoplasm and extracellular space of eosinophils and basophils[1][4]. It interacts with tubulin α-1B and may have low-affinity carbohydrate binding activity. Disruption of CLCs by reduced glutathione or anti-Gal-10 antibodies suggests Galectin-10 is a viable target for novel therapies for eosinophilic diseases, though targeting must carefully balance immune functions[1][4].
Reduced glutathione chemically modifies Gal-10 (Cys57), disrupting CLCs. Colchicine targets Gal-10-tubulin interaction, preventing crystal formation.
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