POSSIBLE INTERACTIONS BETWEEN THE FC-EPSILON RECEPTOR AND A NOVEL MAST-CELL FUNCTION-ASSOCIATED ANTIGEN
POSSIBLE INTERACTIONS BETWEEN THE FC-EPSILON RECEPTOR AND A NOVEL MAST-CELL FUNCTION-ASSOCIATED ANTIGEN
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DOI:
10.1093/intimm/3.4.333
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发表时间:
1991-04-01
影响因子:
4.4
通讯作者:
PECHT, I
中科院分区:
文献类型:
--
作者:
ORTEGA, E;SCHNEIDER, H;PECHT, I
We have recently described a monoclonal antibody, mAb G63, which identifies a novel membrane component of mast cells. This antigen is a glycoprotein with an apparent molecular mass of 28 - 40 kd, and is present on the surface of rat mucosal and serosal mast cells. Its density on cells of the mucosal mast cell line RBL-2H3 is 1 - 2 x 10(4) copies per cell. Crosslinking of this membrane protein by the intact mAb G63 results in a pronounced inhibition of the Fc-epsilon-RI-mediated secretion of RBL-2H3 cells. Here we show that crosslinking this novel membrane component inhibits biochemical processes initiated by Fc-epsilon-RI aggregation, such as the hydrolysis of phosphatidylinositides, the influx of Ca2+ ions, and the synthesis and release of de novo formed inflammatory mediators. Furthermore, by fluorescence microscopy, we show that crosslinking of Fc-epsilon-RI-IgE complexes by multivalent antigen results in redistribution of the membrane component recognized by G63, leading to its co-localization with the aggregated Fc-epsilon-RI. This localization is inhibited by NaN3, but not by colchicine or cytochalasin D. Fc-epsilon-RI crosslinking also promotes internalization of this novel membrane component. Taken together these data suggest that the mast cell membrane component recognized by mAb G63 is involved in the Fc-epsilon-RI-mediated stimulation of these cells, and thus can be considered a mast cell function-associated antigen (MAFA).