一种肿瘤相关胰蛋白酶抑制剂与凝血及肿瘤侵袭相关丝氨酸蛋白酶的反应
Reaction of a tumour-associated trypsin inhibitor with serine proteinases associated with coagulation and tumour invasion.
作者信息
Turpeinen U, Koivunen E, Stenman U H
机构信息
Department I of Obstetrics and Gynaecology, Helsinki University Central Hospital, Finland.
出版信息
Biochem J. 1988 Sep 15;254(3):911-4. doi: 10.1042/bj2540911.
Abstract
The inhibition of six serine proteinases by a tumour-associated trypsin inhibitor (TATI) was studied using synthetic peptide substrates. Physiological concentrations of TATI inhibited the amidolytic activities of trypsin, plasmin, urokinase and tissue plasminogen activator (tPA). Chymotrypsin, kallikrein and thrombin were also inhibited, but by much higher concentrations of TATI. The ability of TATI to inhibit trypsin, plasmin, urokinase and tPA suggests that it has a role in proteolytic processes in vivo involving these enzymes.
摘要
使用合成肽底物研究了肿瘤相关胰蛋白酶抑制剂（TATI）对六种丝氨酸蛋白酶的抑制作用。生理浓度的TATI抑制了胰蛋白酶、纤溶酶、尿激酶和组织纤溶酶原激活剂（tPA）的酰胺水解活性。胰凝乳蛋白酶、激肽释放酶和凝血酶也受到抑制，但所需的TATI浓度要高得多。TATI抑制胰蛋白酶、纤溶酶、尿激酶和tPA的能力表明，它在体内涉及这些酶的蛋白水解过程中发挥作用。
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