Charcot-Leyden crystals (CLC), formed in vitro from human eosinophils, were recently shown to contain a protein identical in physicochemical characteristics to human eosinophil lysophospholipase. Monospecific antisera, prepared against homogeneous, chromatographically purified eosinophil lysophospholipase and against CLC formed in vitro, yielded precipitin lines fusing in a pattern of immunochemical identity on Ouchterlony analysis with disrupted eosinophils, purified lysophospholipase, and solubilized CLC protein. With antisera to the purified lysophospholipase, CLC present in vivo in human feces were demonstrated by indirect immunofluorescence to contain eosinophil lysophospholipase. Fecal CLC, purified by sequential gradient centrifugation, contained a single protein migrating identically to eosinophil lysophospholipase on SDS polyacrylamide gel electrophoresis. Solubilized fecal CLC were recrystallized to form characteristically-shaped CLC. Thus, naturally occurring CLC are formed solely of human eosinophil lysophospholipase.
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Article Synopsis
- Charcot-Leyden crystals (CLCs) are associated with eosinophilic diseases like asthma, and the study reveals that reduced glutathione (GSH) disrupts CLCs by inhibiting the crystallization of human galectin-10 (Gal-10).
- GSH does not affect CLCs from monkeys, indicating that the human Gal-10 variant's unique cysteine (Cys57) is likely key to GSH's effects, as it doesn't disrupt crystallization of Gal-10 variants without this residue.
- The research also shows that human Gal-10 interacts with tubulin and is influenced by GSH, GTP, and Mg, suggesting potential pharmaceutical applications of GSH in treating diseases related to C
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