The Immunobiology of the Serine Protease Allergens from the House Dust

Geoffrey Stewart, S.M. Boyd, C.H. Bird, K.D. Krska, M.R. Kollinger, P.J. Thompson

    Research output: Contribution to journalArticle

    34 Citations (Scopus)

    Abstract

    Extracts of Dermatophagoides pteronyssinus and D. farinae were shown to contain a variety of 30 kDA serine proteases, including trypsin, chymotrypsin, and an elastase-like enzyme. The mite trypsin, unlike chymotrypsin and the elastase enzyme, was heterogeneous with regard to charge. The enzymes were shown to be present at higher concentration in fecally enriched extracts than in whole mite extracts. The proteases were shown to induce vascular permeability and to detach cells in tissue culture. Further study showed that the mite elastase induced non-IgE mediated rat mast cell degranulation. Such properties may contribute to immunogenicity. (C) 1994 Wiley-Liss, Inc.
    Original languageEnglish
    Pages (from-to)105-107
    JournalAmerican Journal of Industrial Medicine
    Volume25
    DOIs
    Publication statusPublished - 1994

    Fingerprint

    Mites
    Pancreatic Elastase
    Serine Proteases
    Dust
    Allergens
    Dermatophagoides pteronyssinus
    Cell Degranulation
    Capillary Permeability
    Enzymes
    Mast Cells
    Trypsin
    Peptide Hydrolases

    Cite this

    Stewart, G., Boyd, S. M., Bird, C. H., Krska, K. D., Kollinger, M. R., & Thompson, P. J. (1994). The Immunobiology of the Serine Protease Allergens from the House Dust. American Journal of Industrial Medicine, 25, 105-107. https://doi.org/10.1002/ajim.4700250128
    Stewart, Geoffrey ; Boyd, S.M. ; Bird, C.H. ; Krska, K.D. ; Kollinger, M.R. ; Thompson, P.J. / The Immunobiology of the Serine Protease Allergens from the House Dust. In: American Journal of Industrial Medicine. 1994 ; Vol. 25. pp. 105-107.
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    abstract = "Extracts of Dermatophagoides pteronyssinus and D. farinae were shown to contain a variety of 30 kDA serine proteases, including trypsin, chymotrypsin, and an elastase-like enzyme. The mite trypsin, unlike chymotrypsin and the elastase enzyme, was heterogeneous with regard to charge. The enzymes were shown to be present at higher concentration in fecally enriched extracts than in whole mite extracts. The proteases were shown to induce vascular permeability and to detach cells in tissue culture. Further study showed that the mite elastase induced non-IgE mediated rat mast cell degranulation. Such properties may contribute to immunogenicity. (C) 1994 Wiley-Liss, Inc.",
    author = "Geoffrey Stewart and S.M. Boyd and C.H. Bird and K.D. Krska and M.R. Kollinger and P.J. Thompson",
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    Stewart, G, Boyd, SM, Bird, CH, Krska, KD, Kollinger, MR & Thompson, PJ 1994, 'The Immunobiology of the Serine Protease Allergens from the House Dust' American Journal of Industrial Medicine, vol. 25, pp. 105-107. https://doi.org/10.1002/ajim.4700250128

    The Immunobiology of the Serine Protease Allergens from the House Dust. / Stewart, Geoffrey; Boyd, S.M.; Bird, C.H.; Krska, K.D.; Kollinger, M.R.; Thompson, P.J.

    In: American Journal of Industrial Medicine, Vol. 25, 1994, p. 105-107.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - The Immunobiology of the Serine Protease Allergens from the House Dust

    AU - Stewart, Geoffrey

    AU - Boyd, S.M.

    AU - Bird, C.H.

    AU - Krska, K.D.

    AU - Kollinger, M.R.

    AU - Thompson, P.J.

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    AB - Extracts of Dermatophagoides pteronyssinus and D. farinae were shown to contain a variety of 30 kDA serine proteases, including trypsin, chymotrypsin, and an elastase-like enzyme. The mite trypsin, unlike chymotrypsin and the elastase enzyme, was heterogeneous with regard to charge. The enzymes were shown to be present at higher concentration in fecally enriched extracts than in whole mite extracts. The proteases were shown to induce vascular permeability and to detach cells in tissue culture. Further study showed that the mite elastase induced non-IgE mediated rat mast cell degranulation. Such properties may contribute to immunogenicity. (C) 1994 Wiley-Liss, Inc.

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    M3 - Article

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    JO - American Journal of Industrial Medicine

    JF - American Journal of Industrial Medicine

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    ER -