Deutsch D G, Chin S A
Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, NY 11794.
Biochem Pharmacol. 1993 Sep 1;46(5):791-6. doi: 10.1016/0006-2952(93)90486-g.
Enzymatic activities have been identified which catalyze both the hydrolysis and synthesis of arachidonylethanolamide (anandamide). Anandamide was taken up by neuroblastoma and glioma cells in culture, but it did not accumulate since it was rapidly degraded by an amidase activity that resided mainly in the membrane fractions. This amidase activity was expressed in brain and the majority of cells and tissues tested. Phenylmethylsulfonyl fluoride (PMSF) was found to be a potent inhibitor of this amidase. A catalytic activity for the biosynthesis of anandamide from ethanolamine and arachidonic acid was readily apparent in incubations of rat brain homogenates. The stability of anandamide in serum and its rapid breakdown in cells and tissues are consistent with the observation that it is active when administered systemically, and its duration of action will be regulated by its rate of degradation in cells.
已经鉴定出催化花生四烯酸乙醇酰胺（阿南达米德）水解和合成的酶活性。阿南达米德被培养中的神经母细胞瘤和胶质瘤细胞摄取，但由于它被主要存在于膜组分中的酰胺酶活性迅速降解，所以并未积累。这种酰胺酶活性在脑以及大多数测试的细胞和组织中都有表达。发现苯甲基磺酰氟（PMSF）是这种酰胺酶的有效抑制剂。在大鼠脑匀浆孵育中，从乙醇胺和花生四烯酸生物合成阿南达米德的催化活性很明显。阿南达米德在血清中的稳定性及其在细胞和组织中的快速分解与以下观察结果一致：它在全身给药时具有活性，其作用持续时间将由其在细胞中的降解速率调节。
