Release of elastase from purified human lung mast cells and basophils. Identification as a Hageman factor cleaving enzyme

• Published in: Inflammation 1989-06, Vol.13 (3), p.295-308
• Main Authors: MEIER, H. L, SCHULMAN, E. S, HECK, L. W, MACGLASHAN, D, NEWBALL, H. H, KAPLAN, A. P
• Format: Article
• Language: English
• Subjects: Autoradiography; Basophils - enzymology; Biological and medical sciences; Cells, Cultured; Factor XII - metabolism; Factor XIIa; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunobiology; Immunoglobulin E - physiology; Lung - enzymology; Mast Cells - enzymology; Molecular Weight; Monocytes, macrophages; Myeloid cells: ontogeny, maturation, markers, receptors; Neutrophils - enzymology; Pancreatic Elastase - metabolism; Serine Endopeptidases - metabolism
• ISSN: 0360-3997; 1573-2576
• DOI: 10.1007/BF00914396

Elastase, a serine protease, is capable of inducing severe lung destruction in experimental animal models. We now report that this proteinase exists preformed in neutrophil-free sonicates of purified human lung mast cells (greater than 98% purity) and in circulating peripheral blood basophils (greater than 97% purity). The elastase levels in both cell types (41-174 ng/10(6) cells) 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.