Roncaglioni M C, Falanga A, D'Alessandro A P, Alessio M G, Casali B, Donati M B
Haematologica. 1989 Mar-Apr;74(2):143-7.
Rabbit V2 carcinoma tissue is the tumor in which cancer procoagulant activity (CP) was first described, purified and identified as a cysteine proteinase able to activate F X directly. In the present study we show that CP of V2 carcinoma extracts is depressed in its biological activity (although the antigen is present) by warfarin treatment. The biochemical basis for this effect is offered by the identification of Vit.K-dependent gamma-carboxylase in the microsomal fraction of the tumor tissue. V2 carcinoma tissue had very low endogenous substrate(s) of tumor carboxylase in basal conditions but this increased threefold after warfarin. The accumulation of endogenous substrate(s) and the depression of the CP activity by warfarin raises the possibility that CP represents at least one of the substrates for gamma-glutamyl carboxylase in this experimental tumor tissue.
兔V2癌组织是首次描述、纯化并鉴定出癌促凝活性（CP）的肿瘤，该活性是一种能够直接激活因子X的半胱氨酸蛋白酶。在本研究中，我们发现华法林处理可降低V2癌提取物中CP的生物活性（尽管抗原存在）。肿瘤组织微粒体部分中维生素K依赖性γ-羧化酶的鉴定为这种效应提供了生化基础。在基础条件下，V2癌组织的肿瘤羧化酶内源性底物非常低，但华法林处理后增加了三倍。内源性底物的积累以及华法林对CP活性的抑制增加了一种可能性，即CP在该实验性肿瘤组织中代表γ-谷氨酰羧化酶的至少一种底物。
