人嗜中性粒细胞的阳离子蛋白：增强金黄色葡萄球菌蛋白 A-IgG 复合物的吞噬作用。
Cationic proteins of human granulocytes: Enhancement of phagocytosis ofStaphylococcus protein A-IgG complexes.
机构信息
Departments of Internal Medicine and Clinical Chemistry, University Hospital, Uppsala, Sweden.
出版信息
Inflammation. 1976 Jun;1(3):237-46. doi: 10.1007/BF00917865.
The antibacterial chymotrypsin-like cationic protein of human granulocytes is shown to enhance the phagocytosis ofStaphylococcus protein A-IgG complexes by human granulocytes. The enhancement is time- and dose-dependent, and it is inhibited by heat inactivation of the chymotrypsin-like cationic protein. Granulocyte elastase and trypsin give a similar enhancement. The chymotrypsin-like cationic protein-mediated enhancement is poorly inhibited byα 1-antitrypsin. There is a need for approximately 20 molα 1-antitrypsin to inhibit 1 mol chymotrypsin-like cationic protein. Elastase is effectively inhibited at a 1∶1 molar relationship. Kinetic studies suggest that phagocytosis enhancement by chymotrypsin-like cationic protein may be due to modification of the Fc-receptor with concomitantly increased affinhy of the protein A-IgG complex.
人嗜中性白细胞的抗菌胰凝乳蛋白酶样阳离子蛋白被证实可增强人嗜中性白细胞对葡萄球菌蛋白 A-IgG 复合物的吞噬作用。这种增强作用具有时间和剂量依赖性，并可被胰凝乳蛋白酶样阳离子蛋白的热失活所抑制。粒细胞弹性蛋白酶和胰蛋白酶也有类似的增强作用。α1-抗胰蛋白酶对人嗜中性白细胞的胰凝乳蛋白酶样阳离子蛋白介导的增强作用抑制作用较差。大约需要 20 摩尔的α1-抗胰蛋白酶才能抑制 1 摩尔的胰凝乳蛋白酶样阳离子蛋白。弹性蛋白酶在 1∶1 的摩尔比例下可被有效抑制。动力学研究表明，胰凝乳蛋白酶样阳离子蛋白的吞噬作用增强可能是由于 Fc 受体的修饰，同时增加了蛋白 A-IgG 复合物的亲和力。
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