Perez H D, Ong R R
Inflammation. 1984 Sep;8(3):277-85. doi: 10.1007/BF00916416.
Polymorphonuclear leukocyte (PMN) surface membrane glycoproteins very likely are involved in the phenomenon of stimulus-response coupling. Previously, we have shown that subagglutinating concentrations of the plant lectin, wheat germ agglutinin (WGA) specifically and irreversibly inhibited N-formyl-methionyl-leucyl-phenyl-alanine (FMLP)-mediated PMN chemotaxis. WGA did not affect the binding of [3H]FMLP to its receptor on the PMN plasma membrane. We have examined the possibility that cross-linking of WGA binding sites may elicit PMN degranulation. We have found that multivalent, but not bivalent, cross-linking of WGA bound to PMNs elicits release of lysosomal constituents. This phenomenon was specific for WGA since it did not occur when concanavalin A (Con A), instead of WGA, was used. It is intriguing to speculate that WGA may attach to a "physiologic" receptor for FMLP on the PMN membrane and that redistribution (cross-linking) of this receptor might be an early event in the activation of PMNs by FMLP.
多形核白细胞（PMN）表面膜糖蛋白很可能参与刺激-反应偶联现象。此前，我们已表明植物凝集素麦胚凝集素（WGA）的亚凝集浓度能特异性且不可逆地抑制N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸（FMLP）介导的PMN趋化作用。WGA不影响[3H]FMLP与其在PMN质膜上的受体的结合。我们研究了WGA结合位点交联可能引发PMN脱颗粒的可能性。我们发现，与PMN结合的WGA的多价而非二价交联会引发溶酶体成分的释放。这种现象对WGA具有特异性，因为当使用伴刀豆球蛋白A（Con A）而非WGA时不会发生。有趣的是，可以推测WGA可能附着于PMN膜上FMLP的“生理性”受体，并且该受体的重新分布（交联）可能是FMLP激活PMN的早期事件。
