Gordon S G
J Histochem Cytochem. 1981 Mar;29(3A Suppl):457-63. doi: 10.1177/29.3.457.
There is increased deposition and lysis of fibrin in cancer, but little is known about the causes of this abnormal fibrin formation. This article reviews research on cancer procoagulant and presents some preliminary immunohistochemical studies. Cancer procoagulant was purified from a rabbit V2 carcinoma. It was a single polypeptide cysteine protease with a molecular weight of 68,000 daltons and an isoelectric point of 4.8-4.9. It initiates coagulation by directly activating factor X within the coagulation cascade. Its physical, chemical, and enzymatic properties distinguish it from serine proteases within the coagulation cascade and suggest that it is a protein from neoplastic cells. To determine whether cancer procoagulant was unique to the malignant state, procoagulant activity was assayed in extracts of normal and malignant tissue and serum-free medium from normal and transformed fibroblasts. Normal tissue and cells had procoagulant activity with characteristics similar to tissue factor, while malignant tissue and transformed cells had a procoagulant with the characteristics of cancer procoagulant, suggesting that cancer procoagulant is unique to the malignant state. An antibody to cancer procoagulant was used for horseradish peroxidase immunohistochemical staining fo cultured rabbit V2 carcinoma cells. These preliminary results support the concept that malignant cells produce the cancer procoagulant antigen.
癌症中纤维蛋白的沉积和溶解增加，但对于这种异常纤维蛋白形成的原因知之甚少。本文回顾了有关癌促凝素的研究，并展示了一些初步的免疫组织化学研究。癌促凝素是从兔V2癌中纯化出来的。它是一种单链多肽半胱氨酸蛋白酶，分子量为68,000道尔顿，等电点为4.8 - 4.9。它通过直接激活凝血级联反应中的因子X来启动凝血。其物理、化学和酶学特性使其与凝血级联反应中的丝氨酸蛋白酶不同，并表明它是一种来自肿瘤细胞的蛋白质。为了确定癌促凝素是否是恶性状态所特有的，对正常和恶性组织提取物以及正常和转化成纤维细胞的无血清培养基中的促凝活性进行了检测。正常组织和细胞具有与组织因子相似特征的促凝活性，而恶性组织和转化细胞具有癌促凝素特征的促凝素，这表明癌促凝素是恶性状态所特有的。一种针对癌促凝素的抗体用于对培养的兔V2癌细胞进行辣根过氧化物酶免疫组织化学染色。这些初步结果支持了恶性细胞产生癌促凝素抗原这一概念。
