ABSTRACT
Charcot-Leyden crystals (CLC) were first described in 1853 by Charcot and C. Robin in the postmortem spleen and blood of a leukemia patient; a later report by Leyden described them in the sputum of asthmatics. These distinctive hexagonal, bipyramidal crystals have classically been observed in tissues and secretions from sites of eosinophil-associated inflammatory reactions in asthma, myeloid leukemias, allergic, parasitic and other diseases. Expression of recombinant CLC protein was evaluated both by Western blot and radioimmunoassay inhibition analyses of COS and Chinese hamster ovary cell extracts and by indirect immunofluorescent staining and ultrastructural immunogold analyses of intact cells. Transfection of the CLC cDNA into COS cells directed the expression of considerable lysophospholipase enzyme activity, confirming that the native eosinophil CLC protein functions as a lysophospholipase. The recombinantly expressed CLC protein was found to be immunochemically indistinguishable from native eosinophil-derived CLC protein as determined by radioimmunoassay inhibition analyses.
