Charcot Leyden Crystal Protein (CLC)

LGALS10; LPPL; Eosinophil Lysophospholipase; Lysolecithin Acylhydrolase; Galectin 10

Charcot Leyden Crystal Protein (CLC)

CLC protein is a unique constituent of eosinophils and basophils. This protein forms the hexagonal bipyramidal crystals observed in tissues at sites of eosinophil accumulations, possesses lysophospholipase activity, and comprises an estimated 7% to 10% of total eosinophil protein. The ultrastructural localization of CLC protein was studied in mature peripheral blood eosinophils from normal donors and from patients with the idiopathic hypereosinophilic syndrome. Subcellular localization was evaluated by immunoelectron microscopy using eosinophils, both from buffy coat and purified cell suspensions, that were fixed by a variety of methods. Immunochemical detection of CLC protein employed rabbit antiserum to eosinophil CLC protein, affinity chromatography-purified monospecific IgG antibodies, and postembedding immunogold techniques.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)