Kanagasuntheram P, Teo T S
Biochem Int. 1983 Oct;7(4):511-8.
Calmodulin present in rat parotid homogenates activated cyclic AMP phosphodiesterase activity by 8 to 10 fold. The activation was Ca2+-dependent and reversed by trifluoperazine. Half-maximal inhibition required 12 microM trifluoperazine. Incubation of parotid slices with up to 40 microM trifluoperazine had no effect on the basal rate of amylase and K+ release or on cellular ATP content. Isoproterenol stimulated glucose utilization and substance P stimulated amylase secretion were also unaffected by 40 microM trifluoperazine. 20 or 40 microM Trifluoperazine however inhibited amylase secretion induced by isoproterenol, dibutyryl cyclic AMP, carbamoylcholine or phenylephrine. The possible involvement of calmodulin in regulating enzyme secretion following stimulation of the parotid gland with the various types of agonists is discussed.
大鼠腮腺匀浆中的钙调蛋白可使环磷酸腺苷磷酸二酯酶活性激活8至10倍。这种激活依赖于Ca2+,并可被三氟拉嗪逆转。半数最大抑制浓度需要12微摩尔三氟拉嗪。用高达40微摩尔三氟拉嗪孵育腮腺切片,对淀粉酶和钾离子的基础释放速率或细胞内ATP含量没有影响。异丙肾上腺素刺激的葡萄糖利用以及P物质刺激的淀粉酶分泌也不受40微摩尔三氟拉嗪的影响。然而,20或40微摩尔三氟拉嗪可抑制由异丙肾上腺素、二丁酰环磷酸腺苷、氨甲酰胆碱或去氧肾上腺素诱导的淀粉酶分泌。本文讨论了钙调蛋白在腮腺受到各种类型激动剂刺激后调节酶分泌过程中可能的作用。