Herron G S, Werb Z, Dwyer K, Banda M J
J Biol Chem. 1986 Feb 25;261(6):2810-3.
We have characterized the biosynthesis of two metalloproteinases, procollagenase and prostromelysin, by rabbit brain capillary endothelial cells (RBCE) by means of immunochemical, biosynthetic, and functional assays. Unstimulated RBCE secreted no detectable metalloproteinases. Secretion of both procollagenase and prostromelysin was induced within 6 h by treating the cells with 50 ng/ml 12-O-tetradecanoylphorbol-13-acetate. In treated cells, the two proenzymes accounted for up to 20% of the [35S]methionine-labeled secreted proteins; about 15 micrograms of each protein was secreted in 48 h by 10(6) RBCE. Although RBCE secreted approximately as much procollagenase and prostromelysin as did rabbit fibroblasts, virtually no enzyme activity could be measured in RBCE-conditioned medium, even after activation of the proenzymes by trypsin or an organomercurial agent.
我们通过免疫化学、生物合成和功能测定，对兔脑毛细血管内皮细胞（RBCE）合成两种金属蛋白酶（前胶原酶和前基质溶解素）的过程进行了表征。未受刺激的RBCE不分泌可检测到的金属蛋白酶。用50 ng/ml 12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯处理细胞后，6小时内即可诱导前胶原酶和前基质溶解素的分泌。在经处理的细胞中，这两种酶原占[35S]甲硫氨酸标记的分泌蛋白的比例高达20%；10(6)个RBCE在48小时内可分泌约15微克的每种蛋白。尽管RBCE分泌的前胶原酶和前基质溶解素的量与兔成纤维细胞分泌的大致相同，但即使在用胰蛋白酶或有机汞试剂激活酶原后，在RBCE条件培养基中几乎检测不到酶活性。
