Identification of human eosinophil lysophospholipase as the constituent of Charcot-Leyden crystals.

Abstract

Since the initial descriptions of Charcot-Leyden crystals more than 100 years ago, the presence of these slender, dipyramidal crystals in human tissues and biologic fluids has become a hallmark of eosinophilic leukocyte infiltration, especially in association with allergic and helminthic diseases. The formation of these crystals in vitro after disruption of human eosinophils, but not of other cell types, in hypotonic saline or detergent established the eosinophil as the unique cellular source of the crystalline protein. Charcot-Leyden crystals have now been found to express lysophospholipase activity (lysolecithin acylhydrolase, EC 3.1.1.5), and the solubilized Charcot-Leyden crystal protein presents a single stained protein band that is coincident with the lysophospholipase activity eluted from replicate gels on alkaline polyacrylamide gel electrophoresis. On sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the solubilized Charcot-Leyden crystal protein migrates with a molecular weight of 17,400, which is comparable to that of eosinophil lysophospholipase purified chromatographically to homogeneity; further, on combination, the two proteins comigrate as a single staining band. Finally, the chromatographically purified eosinophil lysophospholipase in hypotonic buffer forms dipyramidal crystals morphologically identical to Charcot-Leyden crystals. The findings that chromatographically purified, homogeneous eosinophil lysophospholipase and Charcot-Leyden crystal protein express the same enzymatic activity, are of the same size and charge, and form crystals of identical morphology indicate that human eosinophil lysophospholipase is the constituent of Charcot-Leyden crystals.

Ultrastructure of Mycobacterium marinum granuloma in striped bass Morone saxatilis

“…Charcot-Leyden crystals (CLCs) are commonly described in human conditions of eosinophilia, such as allergy, parasitic infection, eosinophilic granuloma and various neoplasms (Charcot & Robin 1853, Dvorak et al 1990, Carson et al 1992. CLCs are composed of the enzyme lysophospholipase (lysolecithin acylhydrolase, EC 3.1.1.5) (Weller et al 1982), which spontaneously forms regular geometric structures, usually hexagonal bipyramids, when released from damaged or degranulating eosinophils (El-Hashimi 1971). Crystalline inclusions are also found in the core of most intact human eosinophil granules (Miller et al 1966), although lysophospholipase has been ultrastructurally localized to a subpopulation of granules without crystalline cores (Dvorak et al 1988).…”

Expression of myeloid-specific genes in childhood acute lymphoblastic leukemia – a cDNA array study

“…[14][15][16][17] Since we compared whole bone marrow to a B cell reference, it was possible that the over-expression originated from the myeloid cells in the patient samples. However, by calculating an area under a ROC curve and performing a randomization experiment, we showed that the small amount of myeloid cells (1-15%) did not affect the results.…”

Los cristales de Charcot-Leyden

“…La composición única de los cristales es lisofosfolipasa (8). Esta enzima, purificada por electroforesis a partirde eosinófilos sanguíneos, origina típicos cristales de Charcot-Leyden (8,9).…”

“…Esta enzima, purificada por electroforesis a partirde eosinófilos sanguíneos, origina típicos cristales de Charcot-Leyden (8,9). Los cristales de Charcot-Leyden obtenidos de las heces reaccionan positivamente con un anticuerpo producido contra lisofosfolipasa (8,9).…”