Steven F S, Griffin M M, Mangel W F, Maier H, Altmannsberger M
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, U.K.
J Enzyme Inhib. 1988;2(3):209-14. doi: 10.3109/14756368809040727.
Guanidinobenzoatase is a proteolytic enzyme capable of degrading fibronectin and is a tumour associated enzyme. Guanidinobenzoatase has been shown to be an arginine selective protease and is distinct from trypsin, plasmin and thrombin, the latter enzymes can be assayed with bis(carbobenzyloxycarbonyl-L-argininamido)-Rhodamine or BZAR. Guanidinobenzoatase is inhibited by BZAR when the enzyme is assayed in free solution and when the enzyme is cell-bound in frozen sections of tumour containing tissues. It is proposed that BZAR and its analogues may be of value in inhibiting tumour cell invasion in vivo and also that the selectivity of BZAR may be used to direct cytotoxic drugs to tumour cells possessing active guanidinobenzoatase.
胍基苯甲酸酶是一种能够降解纤连蛋白的蛋白水解酶，是一种肿瘤相关酶。胍基苯甲酸酶已被证明是一种精氨酸选择性蛋白酶，与胰蛋白酶、纤溶酶和凝血酶不同，后几种酶可用双（苄氧羰基-L-精氨酰胺基）-罗丹明或BZAR进行检测。当在游离溶液中检测该酶以及在含有肿瘤组织的冰冻切片中该酶与细胞结合时，胍基苯甲酸酶都能被BZAR抑制。有人提出，BZAR及其类似物可能在体内抑制肿瘤细胞侵袭方面具有价值，而且BZAR的选择性可用于将细胞毒性药物导向具有活性胍基苯甲酸酶的肿瘤细胞。
