Inflammatory responses of human eosinophils to cockroach are mediated through protease-dependent pathways

• Published in: Journal of allergy and clinical immunology Vol. 126; no. 1; pp. 169 - 172.e2
• Main Authors: Wada, Kota, MD, Matsuwaki, Yoshinori, MD, PhD, Yoon, Juhan, PhD, Benson, Linda M., BS, Checkel, James L, Bingemann, Theresa A., MD, Kita, Hirohito, MD
• Format: Journal Article
• Language: English
• Published: New York, NY Mosby, Inc 01.07.2010; Elsevier; Elsevier Limited
• Subjects: Allergy and Immunology; Animals; Asthma; Asthma - etiology; Biological and medical sciences; Cockroaches; Cockroaches - immunology; Eosinophils - physiology; Fluorides; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunopathology; Kinases; Ligands; Medical sciences; Peptides; Proteases; Receptor, PAR-2 - physiology; Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis; Human; Cockroach; Immunopathology; Peptidases; Immunology; Enzyme; Granulocyte; Hydrolases; Inflammation; Eosinophil
• ISSN: 0091-6749; 1097-6825
• DOI: 10.1016/j.jaci.2010.04.007

Pretreatment of German and Oriental cockroach extracts with pepstatin AÂ inhibited production of the S37LIGKdD peptide fragment by about 50% to 70%. [...]these cockroach extracts likely contain pepstatin A-sensitive proteases, which cleave PAR-2 peptide similarly to the authentic PAR-2 ligand, trypsin. While none of the well characterized cockroach allergens showed proteolytic activity, the midgut of cockroaches contains trypsin, chymotrypsin, subtilisin, and cysteine proteaselike proteases.9 Typically, PAR-2 is cleaved and activated by serine proteases, such as trypsin.7 However, in a human epithelial cell line stimulated with German cockroach extract, the aspartate protease inhibitor, pepstatin A, and the cysteine protease inhibitor, E64, inhibited phospho-p44 mitogen-activated protein kinase levels, suggesting a role for cysteine proteases or aspartate proteases.