Noguchi M, Adachi H, Sato S, Honda T, Ohnishi S, Aoki E, Torizuka K
Department of Nuclear Medicine and Radiology, Kyoto University School of Medicine, Japan.
Endocrinol Jpn. 1987 Oct;34(5):727-36. doi: 10.1507/endocrj1954.34.727.
We investigated cholecystokinin (CCK) receptors on isolated gastric chief cells from guinea pig. CCK stimulated pepsinogen secretion from chief cells at the same efficacy as that induced by carbamylcholine. Binding of 125I-labeled CCK-33 (125I-CCK) to chief cells was temperature-dependent, and was saturable and reversible at 37 degrees C. Hofstee plots of the ability of CCK-8 to inhibit binding of 125I-CCK showed a linear regression line, suggesting that CCK receptors possessed one binding site. The dissociation constant of the binding site was calculated to be 3.8 x 10(-10) M. The dose-response curve of CCK for pepsinogen secretion was superimposed on that for the binding to its receptors. These results indicated that gastric chief cells from the guinea pig possess CCK receptors that relate closely to the action of CCK involved in pepsinogen secretion.
我们研究了豚鼠分离的胃主细胞上的胆囊收缩素(CCK)受体。CCK刺激主细胞分泌胃蛋白酶原的效力与氨甲酰胆碱诱导的效力相同。125I标记的CCK-33(125I-CCK)与主细胞的结合是温度依赖性的,在37℃时是可饱和且可逆的。CCK-8抑制125I-CCK结合能力的霍夫斯泰因图显示出一条线性回归线,表明CCK受体具有一个结合位点。结合位点的解离常数经计算为3.8×10(-10)M。CCK对胃蛋白酶原分泌的剂量反应曲线与其与受体结合的剂量反应曲线重叠。这些结果表明,豚鼠的胃主细胞具有与参与胃蛋白酶原分泌的CCK作用密切相关的CCK受体。