Debanne M T, Bell R, Dolovich J
Biochim Biophys Acta. 1975 Dec 5;411(2):295-304. doi: 10.1016/0304-4165(75)90309-8.
Complexes of labelled proteinases (subtilopeptidase A, trypsin) with serum alpha 1-macroglobulin or alpha 2-macroglobulin are rapidly taken up in vitro by rabbit alveolar macrophages and peritoneal macrophages but not by mixed rabbit peripheral blood leukocytes. Enzyme, not bound to alpha 1- or alpha 2-macroglobulin, does not become associated with alveolar macrophages. Chemically inactivated subtilopeptidase A does not bind to alpha 1- or alpha 2-macroglobulin; chemically inactivated subtilopeptidase A in mixtures with alpha 1 - or alpha 2-microglobulin, does not interact with alveolar macrophages. Blocking experiments confirmed that the interaction of proteinase with alveolar macrophages is complex specific; uptake of labelled complex was prevented by the simultaneous addition of macroglobulin complexes formed with non-labelled subtilopeptidase A, subtilopeptidase B, trypsin or chymotrypsin but not by macroglobulin alone. The findings demonstrate a complex-specific interaction between proteinase-alpha-macroglobulin complexes and macrophages.
标记的蛋白酶(枯草杆菌蛋白酶A、胰蛋白酶)与血清α1-巨球蛋白或α2-巨球蛋白形成的复合物在体外能被兔肺泡巨噬细胞和腹膜巨噬细胞迅速摄取,但兔外周血混合白细胞则不能摄取。未与α1-或α2-巨球蛋白结合的酶不会与肺泡巨噬细胞结合。化学灭活的枯草杆菌蛋白酶A不会与α1-或α2-巨球蛋白结合;化学灭活的枯草杆菌蛋白酶A与α1-或α2-微球蛋白混合时,不会与肺泡巨噬细胞相互作用。阻断实验证实,蛋白酶与肺泡巨噬细胞的相互作用具有复合物特异性;同时加入由未标记的枯草杆菌蛋白酶A、枯草杆菌蛋白酶B、胰蛋白酶或糜蛋白酶形成的巨球蛋白复合物可阻止标记复合物的摄取,但单独加入巨球蛋白则不能。这些发现表明蛋白酶-α-巨球蛋白复合物与巨噬细胞之间存在复合物特异性相互作用。