Journal article
Purified Human Mast Cells and Basophils Release Human Elastase and Cathepsin G by an IgE-Mediated Mechanism
International Archives of Allergy and Immunology, v 77(1-2), pp 179-183
1985
PMID: 3924838
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Abstract
Human lung mast cells and human peripheral basophils were purified and examined for their content of proteolytic enzymes similar to lung Hageman factor activator (LHFA) previously found to be released from chopped human lung by an IgE-mediated mechanism. It was found that both cell types contained elastase and cathepsin G-like enzymes, and that elastase appeared to be responsible for LHFA activity. The enzymes, as well as histamine, were released in a dose-dependent manner from these cells by anti-IgE antibody and by ionophore A 23187. It appears that stimulation by either anti-IgE or ionophore increases the amount of both enzymes extractable from these cells. The release of these proteases may explain some of the inflammation and observed defects in coagulation which occur as a result of anaphylaxis.
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Details
- Title
- Purified Human Mast Cells and Basophils Release Human Elastase and Cathepsin G by an IgE-Mediated Mechanism
- Creators
- Henry Louis Meier - United States ArmyLou W Heck - University of Alabama at BirminghamEdward S Schulman - Thomas Jefferson UniversityDonald W MacGlashan, Jr
- Publication Details
- International Archives of Allergy and Immunology, v 77(1-2), pp 179-183
- Number of pages
- 5
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Pulmonary, Critical Care, and Sleep (Medicine)
- Web of Science ID
- WOS:A1985AJS2400035
- Scopus ID
- 2-s2.0-0021836810
- Other Identifier
- 9783318001433; 3318001430; 991019295190304721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Allergy
- Immunology