Human leukocyte elastase, cathepsin G, and lactoferrin: family of neutrophil granule glycoproteins that bind to an alveolar macrophage receptor.
Human leukocyte elastase, cathepsin G, and lactoferrin: family of neutrophil granule glycoproteins that bind to an alveolar macrophage receptor.
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人白细胞弹性蛋白酶、组织蛋白酶 G 和乳铁蛋白:与肺泡巨噬细胞受体结合的中性粒细胞颗粒糖蛋白家族。
DOI:
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发表时间:
1982
影响因子:
11.1
通讯作者:
E. Campbell
中科院分区:
文献类型:
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作者:
E. Campbell
Interactions between polymorphonuclear neutrophils and mononuclear phagocytes are potentially of great importance in a variety of inflammatory processes. As part of a continuing effort to elucidate the physiologic importance of human alveolar macrophage receptor-mediated binding of neutrophil (leukocyte) elastase, I have studied the binding of leukocyte elastase and two other neutrophil granule glycoproteins, cathepsin G and lactoferrin, to human alveolar macrophages. Saturable binding of all three ligands at 0 degrees C was observed, with equilibrium dissociation constants of 4.0 x 10(-7), 2.0 x 10(-7), and 1.7 x 10(-6) M, respectively. All bound to a similar number (54-73 x 10(6)) of sites per cell. Binding of all three ligands was inhibited by the polysaccharide fucoidin, and extensive cross-inhibition of their binding to macrophages was observed. The results indicate that alveolar macrophages possess a relatively low-affinity, high-volume receptor for a family of neutrophil granule glycoproteins, which would be ideally suited for clearing released neutrophil granule contents from the extracellular space in inflamed tissues.