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灵长类动物脊髓中125I-胆囊收缩素的结合位点属于CCK-A亚类。

Binding sites for 125I-cholecystokinin in primate spinal cord are of the CCK-A subclass.

作者信息

Hill D R, Shaw T M, Woodruff G N

机构信息

Merck Sharp and Dohme Research Laboratories, Neuroscience Research Centre, Harlow, Essex, U.K.

出版信息

Neurosci Lett. 1988 Jun 29;89(2):133-9. doi: 10.1016/0304-3940(88)90369-2.

Abstract

Cholecystokinin (CCK) receptor binding was measured in sections of human, monkey and rat spinal cord using autoradiographical techniques. In each species, high levels of specific 125I-Bolton-Hunter CCK binding were detected in the superficial layers of the dorsal horn (the substantia gelatinosa). In monkey and human but not rat spinal cord, 125I-CCK binding was dose-dependently inhibited by low concentrations of the selective CCK-A antagonist L-364,718. Binding of [3H]L-364,718, which was saturable (Bmax = 29.0 +/- 0.95 pmol/g wet wt.) and of high affinity (pKd) = 9.92 +/- 0.16) was also detected in sections of monkey spinal cord and had a similar localization to that of specific 125I-CCK binding. These data indicate that in striking contrast to CCK receptors in rat spinal cord, those in the primate cord are of the CCK-A receptor subclass.

摘要

采用放射自显影技术测定了人、猴和大鼠脊髓切片中胆囊收缩素(CCK)受体的结合情况。在每个物种中,均在背角浅层(即胶状质)检测到高水平的特异性125I-博尔顿-亨特CCK结合。在猴和人的脊髓中,但在大鼠脊髓中未发现,低浓度的选择性CCK-A拮抗剂L-364,718可剂量依赖性地抑制125I-CCK结合。在猴脊髓切片中还检测到[3H]L-364,718的结合,其具有饱和性(Bmax = 29.0 +/- 0.95 pmol/g湿重)和高亲和力(pKd = 9.92 +/- 0.16),且其定位与特异性125I-CCK结合的定位相似。这些数据表明,与大鼠脊髓中的CCK受体形成鲜明对比的是,灵长类动物脊髓中的CCK受体属于CCK-A受体亚类。

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