Adhesion to fibronectin primes eosinophils via alpha 4 beta 1 (VLA-4).

作者: A. J. Wardlaw , G. M. Walsh , A. B. Kay , A. R. E. Anwar , O. Cromwell

DOI:

关键词: Bovine serum albuminFibronectinMonoclonal antibodyAllergic inflammationEosinophilChemistryIntegrinAlpha chainMolecular biologyCell–cell interactionImmunology

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.

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