LGALS10 Human

The Charcot-Leyden Crystal Protein (CLC-P), also known as Galectin-10, is a protein predominantly found in human eosinophils and basophils . It is named after the distinctive Charcot-Leyden crystals, which are hexagonal bipyramidal structures formed by the crystallization of this protein . These crystals are often observed in tissues and secretions associated with eosinophilic inflammation, such as in conditions like asthma, allergic reactions, and parasitic infections .

The discovery of Charcot-Leyden crystals dates back to the mid-19th century. Friedrich Albert von Zenker first noticed these crystals in 1851, and they were later described by Jean-Martin Charcot and Charles-Philippe Robin in 1853 . Ernst Viktor von Leyden further studied these crystals in 1872, contributing to the understanding of their association with eosinophilic diseases .

CLC-P is a lysophospholipase, an enzyme that hydrolyzes lysophospholipids to release free fatty acids . It has been shown to possess lysophospholipase activity, releasing palmitate from lysopalmitoylphosphatidylcholine . Additionally, CLC-P functions as an acyl-protein thioesterase (APT), which catalyzes the removal of thioester-linked fatty acids from cysteine residues of proteins . This activity is crucial for the regulation of protein palmitoylation, a post-translational modification that affects membrane localization, vesicular transport, and secretion .

Charcot-Leyden crystals are indicative of eosinophilic inflammation and are commonly found in conditions such as asthma, bronchitis, allergic rhinitis, and parasitic infections . The presence of these crystals in tissues and secretions serves as a marker for eosinophil-rich inflammatory conditions . Recent studies have shown that CLC-P can activate the NLRP3 inflammasome, leading to IL-1β-driven inflammation . This highlights the potential role of CLC-P in promoting pro-inflammatory activities in eosinophilic disorders.

Human recombinant CLC-P is produced using recombinant DNA technology, which involves inserting the gene encoding CLC-P into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in research to study the biochemical properties and functions of CLC-P, as well as its role in eosinophilic inflammation and related diseases .