Tissue localization of bovine dander allergen Bos d 2

JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY

卷:101

Article

Rautiainen, J ; Rytkönen, M ; Syrjänen, K ; Pentikäinen, J ; Zeiler, T ; Virtanen, T ; Mäntyjärvi, R

关键词: allergen;    Bos d 2;    bovine;    calycin;    cow;    immunohistochemistry;    lipocalin;    RT-PCR;   

DOI  :  10.1016/S0091-6749(98)70247-7

来源: Elsevier

【 摘 要 】

Background: Domestic mammals are important sources of indoor allergens. However, the origin at the tissue level and the biologic function of mammalian allergens are largely unknowm. Objective: The aim of this study was to localize the source of the major bovine dander allergen, Bos d 2, in bovine tissues. Methods: Samples from several organs were tested for the presence of mRNA encoding Bos d 2 and Bos d 2 protein by using the reverse transcriptase polymerase chain reaction and immunohistochemical staining, respectively. Results: Skin proved to be the only tissue where mRNA encoding Bos d 2 was detected. This observation was confirmed by immunohistochemistry with a monoclonal anti-Bos d 2 antibody as the primary antibody. In the skin sections, Bos d 2 was found in the secretory cells of apocrine sweat glands and the basement membranes of the epithelium and hair follicles. Bos d 2 belongs to the family of lipocalins comprising a number of pheromone carrier proteins that are present, for example, in the secretions of the apocrine sweat glands. Conclusion: Together with earlier data, our findings suggest that Bos d 2 is produced in sweat glands and transported to the skin surface as a carrier of the pheromone ligand. Because dander allergens of a number of mammalian species are lipocalins, the common biologic function of being pheromone carriers seems to be a common feature of an important group of aeroallergens.

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