Substrate preference profiles of proteases released by allergenic pollens
| Autor: | Robert George Whittaker, Rakesh K. Kumar, F Widmer, P J Hayes |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Ragweed Serine protease Proteases Protease biology medicine.medical_treatment Immunology food and beverages Cynodon dactylon biology.organism_classification medicine.disease_cause Allergen Enzyme Biochemistry chemistry otorhinolaryngologic diseases medicine biology.protein Immunology and Allergy Ambrosia |
| Zdroj: | Clinical & Experimental Allergy. 30:571-576 |
| ISSN: | 0954-7894 |
| Popis: | Background Pollens are important triggers for allergic asthma and seasonal rhinitis. We have recently reported that proteases released by major allergenic pollens can injure airway epithelial cells in vitro. Disruption of epithelial integrity by proteases released following deposition of pollens on mucosal surfaces could promote sensitization and induce inflammation. Objective To compare protease activities released by allergenic pollens of various genera. Methods We used a rapid microassay which quantifies cleavage of dipeptide ester substrates to characterize the substrate preference profiles of serine proteases in diffusates of the pollens of perennial ryegrass (Lolium perenne), Kentucky blue grass (Poa pratensis), Bermuda grass (Cynodon dactylon), Western ragweed (Ambrosia spp.), white birch (Betula spp.) and Sydney golden wattle (Acacia longifolia). Results Comparison of the profiles revealed notable differences as well as similarities between serine protease activities released by these pollens. Diffusates of Kentucky blue grass pollen exhibited very high substrate preference for arginine and lysine. For other pollens, cleavage of the cysteine substrate was usually the most rapid and was associated with marked preference for leucine and methionine. There was considerable variation between these pollens in the rates of cleavage of the histidine substrate. In addition, we observed high rates of cleavage of arginine and lysine substrates by Acacia pollen diffusate. Conclusion At least two dominant patterns of substrate preference are identifiable in the mixtures of proteases released by hydrated pollens. Purification of the proteases responsible for these patterns of activity will facilitate investigation of their role in airway epithelial injury and allergic disease. |
| Databáze: | OpenAIRE |
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