作者: A. J. Wardlaw , G. M. Walsh , A. B. Kay , A. R. E. Anwar , O. Cromwell
DOI:
关键词: Bovine serum albumin 、 Fibronectin 、 Monoclonal antibody 、 Allergic inflammation 、 Eosinophil 、 Chemistry 、 Integrin 、 Alpha chain 、 Molecular biology 、 Cell–cell interaction 、 Immunology
摘要: Human peripheral blood eosinophils adhered specifically to microtitre plates coated with plasma fibronectin (Fn) in a dose- and time-dependent fashion. Adhesion was optimal at 60 min concentration of 100 micrograms/ml. Adherence Fn up-regulated by platelet-activating factor (PAF; optimum 10(-6) M) significantly inhibited polyclonal anti-Fn antibody (P 250 micrograms/ml); (3) significant inhibition eosinophil adherence achieved monoclonal antibodies (mAb) against the alpha chain VLA-4 but not mAb CD45 or mouse myeloma as negative controls. After adhesion Fn, were investigated for their capacity release leukotriene C4 response stimulation suboptimal calcium ionophore (2 x M). Significant enhancement detected Fn-coated control bovine serum albumin (BSA) < 0.01). Furthermore, this 4 beta 1 HP2/1 0.05) an anti-CD45 mAb. From these studies we conclude that (1) (VLA-4) integrin is major receptor on human (2) may prime mediator during allergic inflammation.