title: Detection of serine proteases in extracts of the domestic mite Blomia tropicalis.
abstract: Previous studies have shown that the domestic mites Dennatophagoides pteronyssinus and D. farinae contain allergens with serine protease activity. These proteolytic allergens include trypsin, chymotrypsin, elastase, kallikrein, and C3/C5 convertase. However, it is not known whether the domestic mite Blomia tropicalis shares with other mite species the serine protease activities. The enzymatic activity present in extracts obtained from food-free B. tropicalis was investigated using specific substrates and inhibitors. Based upon the concentration response and inhibition profiles, and the digestion of specific substrates our data demonstrate that extracts from B. tropicalis exhibit several serine-protease-like activities. The enzyme activities detected in the B. tropicalis extracts are trypsin, elastase, chymotrypsin, kallikrein, C3/C5 convertase, and mast cell protease. Our results also demonstrate that kallikrein and C3/C5 convertase-like activities were not significantly affected by the alpha1-antiprotease, a naturally occurring serine protease inhibitor which protects lung mucosa from the enzymatic action. These data strongly suggest that the Echymyopodidae mite B. tropicalis shares at least five serine proteases with members of other mite families, the Glycyphagidae and Pyroglyphidae. In addition, our data demonstrate the potential use of biochemical methods to detect serine proteases for evaluation of mite growth in viitro, or to detect environmental exposures to these enzymes.
authors.affiliation: Ponce School of Medicine, Puerto Rico 00732, USA. asthma@coqui.net
authors.forename: Federico
authors.initials: F
authors.lastname: Montealegre
authors.forename: Carmen
authors.initials: C
authors.lastname: Quiñones
authors.forename: Nanette
authors.initials: N
authors.lastname: Torres
authors.forename: Kirsteen
authors.initials: K
authors.lastname: Goth
mesh_terms: D000818:Animals; D002364:Caseins / Q000378:metabolism; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000378:metabolism; D050577:Complement C3-C5 Convertases / Q000037:antagonists & inhibitors / Q000378:metabolism; D007477:Ions; D007610:Kallikreins / Q000037:antagonists & inhibitors / Q000378:metabolism; D008670:Metals; D008925:Mites / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity; D014020:Tissue Extracts; D014357:Trypsin / Q000378:metabolism; D000515:alpha 1-Antitrypsin / Q000378:metabolism
chemical_list: D002364:Caseins; D007477:Ions; D008670:Metals; D011480:Protease Inhibitors; D014020:Tissue Extracts; D000515:alpha 1-Antitrypsin; D050577:Complement C3-C5 Convertases; D007610:Kallikreins; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin