کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2833323 1163866 2007 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Monomeric and polymeric IgA show a similar association with the myeloid FcαRI/CD89
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Monomeric and polymeric IgA show a similar association with the myeloid FcαRI/CD89
چکیده انگلیسی

IgA is found in both mucosal secretions and serum and is the dominant immunoglobulin isotype produced in humans. It exists in different molecular forms, namely monomeric IgA, dimeric IgA, polymeric IgA and secretory IgA, all exhibiting interactions with FcαRI/CD89 to some extent. CD89 is an activating, γ-chain associated, Fc receptor for IgA expressed on myeloid cells. Here, we investigated the interaction of monomeric and polymeric IgA purified from human serum with CD89 using surface plasmon resonance. The results demonstrate a similar association for monomeric and polymeric IgA with CD89. In contrast, monomeric IgA dissociated more rapidly from CD89 than polymeric IgA. Removal of N-glycans from mIgA resulted is an increased association with CD89, whereas the dissociation was more rapid, resulting in binding comparable to that of untreated monomeric IgA. We conclude that the initial interaction of monomeric and polymeric IgA with CD89 is similar, whereas monomeric IgA dissociates more rapidly from CD89. In view of the large excess of monomeric IgA in serum, monomeric IgA will compete for CD89 interaction with polymeric IgA, thereby preventing cell activation initiated by receptor aggregation contributing to the anti-inflammatory role of IgA.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular Immunology - Volume 44, Issue 5, February 2007, Pages 966–973
نویسندگان
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