Naito K, Nakajima S, Kanbayashi N, Okuyama A, Goto M
Tsukuba Research Institute, Banyu Pharmaceutical Co. Ltd., Japan.
Agents Actions. 1993 Jul;39(3-4):182-6. doi: 10.1007/BF01998972.
The effect of a new metalloproteinase (MP) inhibitor [BE16627B; L-N-(N-hydroxy-2-isobutylsuccinamoyl)-seryl-L-valine, MW: 375.2] isolated from Streptomyces sp. was evaluated by using primary cultures of synovial cells from rheumatoid arthritis patients. BE16627B selectively inhibited MPs such as human stromelysin and 92 kD gelatinase. After the cells were cultured with BE16627B for 5 days, BE16627B inhibited MP activity in the primary culture supernatants from synovial cells in a dose-dependent fashion without showing apparent cytotoxicity or affecting the production and secretion of MPs. Its IC50 for active collagenolysis before activation by trypsin was 25 microM.
从链霉菌属中分离出的一种新型金属蛋白酶（MP）抑制剂[BE16627B；L-N-（N-羟基-2-异丁基琥珀酰基）-丝氨酰-L-缬氨酸，分子量：375.2]的作用，通过使用类风湿性关节炎患者滑膜细胞的原代培养物进行了评估。BE16627B选择性抑制诸如人基质溶素和92kD明胶酶等金属蛋白酶。在用BE16627B培养细胞5天后，BE16627B以剂量依赖性方式抑制滑膜细胞原代培养上清液中的MP活性，而未表现出明显的细胞毒性，也未影响金属蛋白酶的产生和分泌。其在被胰蛋白酶激活前对活性胶原溶解的IC50为25微摩尔。
