Alloantibody bipolar bridging; a new mechanism of cell surface activation.
Bipolar bridging of cellular membrane receptors and epitopes by alloantibodies (Fab bridging the MHC antigens and Fc the Fc receptors) has been shown on a murine mast cell model to be a way of cell signaling and activation. In order to test a possible general significance of this phenomenon, another model was studied, namely guinea pig neutrophils. It was found l(1) that neutrophils from S2, S13 and BIO-AD strains both express class I (B) and class II (Ia) antigens on their surface, as detected by a Prot.A-SRBC rosetting method, after cell incubation with related alloantibodies; (2) that Fc receptors for IgG (Fc gamma R) were specific for IgG2 subclass, as determined by the same rosetting method after binding of preformed immune complexes (IgG1, IgG2 and F(ab')2 anti-DNP-DNP25 BSA); and (3) that specific alloantibodies of IgG2 subclass were able to specifically activate the neutrophil oxidative metabolism as shown by superoxide anion (O2-) release, detected by the luminol-dependent chemiluminescence method. Neither the IgG1 nor F(ab')2 portion were able to trigger O2- release. This demonstrates a second situation of a cell membrane activation through alloantibody bipolar bridging.
D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D006649:Histocompatibility Antigens; D007518:Isoantibodies; D009504:Neutrophils / Q000032:analysis; D011961:Receptors, Fc / Q000032:analysis; D011971:Receptors, Immunologic / Q000502:physiology*; D012397:Rosette Formation
D006649:Histocompatibility Antigens; D007518:Isoantibodies; D011961:Receptors, Fc; D011971:Receptors, Immunologic