Zukin R S, Eghbali M, Olive D, Unterwald E M, Tempel A
Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461.
Proc Natl Acad Sci U S A. 1988 Jun;85(11):4061-5. doi: 10.1073/pnas.85.11.4061.
kappa opioid receptors (kappa receptors) have been characterized in homogenates of guinea pig and rat brain under in vitro binding conditions. kappa receptors were labeled by using the tritiated prototypic kappa opioid ethylketocyclazocine under conditions in which mu and delta opioid binding was suppressed. In the case of guinea pig brain membranes, a single population of high-affinity kappa opioid receptor sites (kappa sites; Kd = 0.66 nM, Bmax = 80 fmol/mg of protein) was observed. In contrast, in the case of rat brain, two populations of kappa sites were observed--high-affinity sites at low density (Kd = 1.0 nM, Bmax = 16 fmol/mg of protein) and low-affinity sites at high density (Kd = 13 nM, Bmax = 111 fmol/mg of protein). To test the hypothesis that the high- and low-affinity kappa sites represent two distinct kappa receptor subtypes, a series of opioids were tested for their abilities to compete for binding to the two sites. U-69,593 and Cambridge 20 selectively displaced the high-affinity kappa site in both guinea pig and rat tissue, but were inactive at the rat-brain low-affinity site. Other kappa opioid drugs, including U-50,488, ethylketocyclazocine, bremazocine, cyclazocine, and dynormphin (1-17), competed for binding to both sites, but with different rank orders of potency. Quantitative light microscopy in vitro autoradiography was used to visualize the neuroanatomical pattern of kappa receptors in rat and guinea pig brain. The distribution patterns of the two kappa receptor subtypes of rat brain were clearly different. The pattern of rat high-affinity kappa sites paralleled that of guinea pig in the caudate-putamen, mid-brain, central gray substance of cerebrum, and substantia nigra; interspecies differences were apparent throughout most of the rest of the brain. Collectively, these data provide direct evidence for the presence of two kappa receptor subtypes; the U-69,593-sensitive, high-affinity kappa 1 site predominates in guinea pig brain, and the U-69,593-insensitive, low-affinity kappa 2 site predominates in rat brain.
κ阿片受体(κ受体)已在豚鼠和大鼠脑匀浆的体外结合条件下得到表征。在抑制μ和δ阿片结合的条件下,使用氚标记的原型κ阿片乙基酮环唑辛对κ受体进行标记。对于豚鼠脑膜,观察到单一群体的高亲和力κ阿片受体位点(κ位点;Kd = 0.66 nM,Bmax = 80 fmol/mg蛋白质)。相比之下,在大鼠脑中,观察到两个κ位点群体——低密度的高亲和力位点(Kd = 1.0 nM,Bmax = 16 fmol/mg蛋白质)和高密度的低亲和力位点(Kd = 13 nM,Bmax = 111 fmol/mg蛋白质)。为了检验高亲和力和低亲和力κ位点代表两种不同κ受体亚型的假设,测试了一系列阿片类药物竞争结合这两个位点的能力。U - 69,593和剑桥20在豚鼠和大鼠组织中均选择性地取代了高亲和力κ位点,但对大鼠脑低亲和力位点无活性。其他κ阿片药物,包括U - 50,488、乙基酮环唑辛、布马佐辛、环唑辛和强啡肽(1 - 17),竞争结合这两个位点,但效价顺序不同。体外放射自显影定量光学显微镜用于可视化大鼠和豚鼠脑中κ受体的神经解剖学模式。大鼠脑的两种κ受体亚型的分布模式明显不同。大鼠高亲和力κ位点的模式在尾状核 - 壳核、中脑、大脑中央灰质和黑质中与豚鼠相似;在大脑其余大部分区域,种间差异明显。总体而言,这些数据为存在两种κ受体亚型提供了直接证据;U - 69,593敏感的高亲和力κ1位点在豚鼠脑中占主导,而U - 69,593不敏感的低亲和力κ2位点在大鼠脑中占主导。