Steven F S, Anees M, Booth N A
Division of Biochemistry, School of Biological Sciences, University of Manchester, U.K.
Anticancer Res. 1995 Jan-Feb;15(1):205-10.
The interaction of plasminogen activator-inhibitor (PAI-1) with a cell surface protease, guanidinobenzoatase (GB), has been studied in free solution and on the surface of colonic epithelial cells. It has been demonstrated that PAI-1 recognises and inhibits the iso enzymic form of GB associated with colonic carcinoma cells but fails to bind to the iso enzymic form of GB associated with normal donor colonic epithelial cells. This interaction is mediated by a lysyl binding site on the GB: complex formation prevents GB binding to fibrin fibrils which also involves lysyl binding sites.
已在游离溶液和结肠上皮细胞表面研究了纤溶酶原激活物抑制剂（PAI-1）与细胞表面蛋白酶胍基苯甲酸酶（GB）的相互作用。已证明PAI-1可识别并抑制与结肠癌细胞相关的GB同工酶形式，但无法与正常供体结肠上皮细胞相关的GB同工酶形式结合。这种相互作用由GB上的一个赖氨酰结合位点介导：复合物的形成阻止了GB与也涉及赖氨酰结合位点的纤维蛋白原纤维结合。
