胆囊收缩素对大鼠胰腺中环磷酸腺苷依赖性蛋白激酶激活的特性研究
Characterization of cAMP-dependent protein kinase activation by CCK in rat pancreas.
作者信息
Marino C R, Leach S D, Schaefer J F, Miller L J, Gorelick F S
机构信息
Department of Medicine, Yale University School of Medicine, New Haven, CT 06510.
出版信息
FEBS Lett. 1993 Jan 18;316(1):48-52. doi: 10.1016/0014-5793(93)81734-h.
This study reports on the use of a new sensitive assay of cAMP-dependent protein kinase activity to examine the effect of cholecystokinin (CCK) on the cAMP second messenger cascade in rat pancreatic acini. Treatment of acini with both low (pM) and high (nM) concentrations of CCK was associated with an increase in cAMP-dependent protein kinase activity. The increases in kinase activity were detected in the absence of phosphodiesterase inhibition, a condition required to detect a measurable increase in cellular cAMP in these cells. Furthermore, the cAMP cascade was dissociated from the secretory effects of CCK, since the CCK analogue, OPE, mediates enzyme secretion but does not increase cellular cAMP levels or kinase activity.
本研究报告了一种新的检测环磷酸腺苷（cAMP）依赖性蛋白激酶活性的灵敏方法的应用，该方法用于检测胆囊收缩素（CCK）对大鼠胰腺腺泡中cAMP第二信使级联反应的影响。用低浓度（皮摩尔）和高浓度（纳摩尔）的CCK处理胰腺腺泡，均与cAMP依赖性蛋白激酶活性增加有关。在没有磷酸二酯酶抑制的情况下检测到激酶活性增加，而在这些细胞中检测到细胞内cAMP有可测量的增加需要这种条件。此外，cAMP级联反应与CCK的分泌效应无关，因为CCK类似物OPE介导酶分泌，但不增加细胞内cAMP水平或激酶活性。
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