ABSTRACT
The tendency of charcot-Leyden crystals (CLC) protein to form the distinctive bipyramidal crystals at sites of eosinophil infiltration has generated significant interest in the biochemical properties of this protein. However, although CLC protein comprises an estimated 7–10% of total eosinophil protein and possesses lysophospholipase activity, its role in eosinophil and basophil function remains obscure. The structure of the CLC gene has been examined using Southern blot analysis of restriction digests of total genomic DNA isolated from unseparated peripheral blood leukocytes of normal donors. Asthma is characterized by impaired respiratory function and airways inflammation. Lung pathology in many patients with moderate to severe asthma is marked by the infiltration and degranulation of eosinophils as well as microatelectasis. The principal substrate of eosinophil lysophospholipase, lysophosphatidylcholine, is an important, albeit minor, component of pulmonary surfactant. Surfactant is primarily composed of phospholipids, the predominant one being 1,2-dipalmitoyl phosphatidylcholine.
