Inflammatory responses of human eosinophils to cockroach are mediated through protease-dependent pathways
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, tryps...
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Published in | Journal of allergy and clinical immunology Vol. 126; no. 1; pp. 169 - 172.e2 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
New York, NY
Mosby, Inc
01.07.2010
Elsevier Elsevier Limited |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | SourceType-Other Sources-1 ObjectType-Article-2 content type line 63 ObjectType-Correspondence-1 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0091-6749 1097-6825 |
DOI: | 10.1016/j.jaci.2010.04.007 |