食管癌中的肿瘤蛋白水解活性

Tumor Proteolytic Activity in Esophageal Cancer.

作者信息

Goufman E I, Tikhonova N B, Gershkovich K B, Aleksankin A P, Stepanov A A, Nizyaeva N V, Bochkov V V, Mikhaleva L M, Kovaleva O V, Stilidi I S, Kushlinskii N E

机构信息

Petrovsky National Research Centre of Surgery, Moscow, Russia.

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.

出版信息

Bull Exp Biol Med. 2025 Apr;178(6):774-777. doi: 10.1007/s10517-025-06415-w. Epub 2025 May 30.

DOI:10.1007/s10517-025-06415-w

PMID:40445536

Abstract

The growth of malignant tumors is accompanied by an increase in plasmin activity, one of the key enzymes in oncogenesis. IgG proteolysis by plasmin yields fragments with exposed C-terminal lysine residues that can bind to plasmin heavy chain. Highly purified plasminogen (plasmin precursor) and heavy chains containing lysine-binding sites were isolated. The formation of IgG fragments as a result of their proteolysis by plasmin in solution was shown. Using ELISA with immobilized heavy chains, we found increased concentration of IgG fragments in the sera of patients with esophageal cancer in comparison with healthy donors. The test had high sensitivity (91%) and specificity (85%).

摘要

恶性肿瘤的生长伴随着纤溶酶活性的增加，纤溶酶是肿瘤发生过程中的关键酶之一。纤溶酶对IgG的蛋白水解产生具有暴露的C末端赖氨酸残基的片段，这些片段可以与纤溶酶重链结合。分离出了高度纯化的纤溶酶原（纤溶酶前体）和含有赖氨酸结合位点的重链。结果表明，溶液中的纤溶酶对IgG进行蛋白水解会形成IgG片段。使用固定化重链的ELISA方法，我们发现与健康供体相比，食管癌患者血清中IgG片段的浓度有所增加。该检测具有高灵敏度（91%）和特异性（85%）。