A NOVEL MEMBER OF THE INTEGRIN RECEPTOR FAMILY MEDIATES ARG-GLY-ASP STIMULATED NEUTROPHIL PHAGOCYTOSIS
A NOVEL MEMBER OF THE INTEGRIN RECEPTOR FAMILY MEDIATES ARG-GLY-ASP STIMULATED NEUTROPHIL PHAGOCYTOSIS
复制标题
DOI：
10.1083/jcb.108.5.1935
复制
发表时间：
1989-05-01
影响因子：
7.8
通讯作者：
BROWN, EJ
中科院分区：
文献类型：
--
作者：
GRESHAM, HD;GOODWIN, JL;BROWN, EJ
人中性粒细胞(PMN)表达一种异二聚体受体，该受体与许多黏附蛋白中的Arg-Gly-Asp(RGD)序列具有配基结合特异性。与该受体结合的单抗B6H12既能抑制RGD介导的配体结合，又能抑制纤维连接蛋白、纤维蛋白原、玻璃体连接蛋白、S因子和IV型胶原对免疫球蛋白G介导的吞噬作用的刺激。通过这种受体结合的配体被PMN的髓过氧化物酶-过氧化氢-卤化物系统的产物迅速失活。我们的结论是，这种受体，我们建议将其命名为白细胞反应整合素，是PMN上的一个信号转导分子，可能在炎症部位的PMN功能的调节中具有重要的早期作用。
Human neutrophils (PMN) express a heterodimeric receptor that has ligand binding specificity for the Arg-Gly-Asp (RGD) sequence within many adhesive proteins. A monoclonal antibody, B6H12, which binds to this receptor, inhibits both RGD-mediated ligand binding and stimulation of IgG-mediated phagocytosis by fibronectin, fibrinogen, vitronectin, von Willebrand''s factor, and collagen type IV. By several criteria this receptor is neither a known very late antigen, a known cytoadhesin (gp IIb/IIIa-vitronectin receptor), nor a member of the LFA-1, Mac-1, p150,95 group of integrin receptors. Ligand binding via this receptor is rapidly inactivated by products of the myeloperoxidase-hydrogen peroxide-halide system of PMN. We conclude that this receptor, for which we propose the name leukocyte response integrin, is a signal-transducing molecule on PMN which may have a significant early role in modulation of PMN function at inflammatory sites.