Release of Elastase from Purified Human Lung Mast Cells and Basophils. Identification as a Hageman Factor Cleaving Enzyme
Abstract
Elastase, a serine protease, is capable of inducing severe lung destruction in experimental animal models. We now report that this proteinase exists performed in neutrophil-free sonicates of purified human lung mast cells (>98% purity) and in circulating peripheral blood basophils (>97% purity). The elastase levels in both cell types represents approximately 3-20% of those found in human neutrophils; both cell types released their elastase following anti-IgE and ionophore A23187 challenge. The apparent molecular size of the mast cell enzyme on Sephadex G-100 gel filtration, as well as its inhibition profile, was identical to that of purified human neutrophil elastase. This mast cell elastase is identical to our previously reported mast cell-derived Hageman factor cleaving activity. Mast cell-, basophil-, and neutrophil-derived elastases cleave Hageman factor into fragments of 52,000 and 28,000 Da; cleavage by all three enzymes is inhibited by preincubation with polyclonal antibodies directed against human neutrophil elastase. Reprints.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1989
- Accession Number
- ADA228378
Entities
People
- Donald Macglashan
- Edward S. Schulman
- Harold H. Newball
- Henry L. Meier
- Louis W. Heck
Organizations
- United States Army Medical Research Institute of Chemical Defense