Goidl J A
Biochemistry. 1979 Aug 21;18(17):3674-9. doi: 10.1021/bi00584a006.
Nuclei isolated from the livers of mice are capable of binding [125I]insulin. A class of high-affinity binding sites having a Kd of 1--2 nM and a capacity of approximately 2000 insulin molecules/nucleus are present on these nuclei. Removal of nuclear membranes by Triton X-100 treatment of the nuclei reduces or eliminates the high-affinity binding sites. Nuclei prepared from livers of the genetically obese mouse (ob/ob) lack, or have markedly reduced numbers of, the high-affinity binding sites whether or not the obese nuclei have been exposed to Triton X-100. The reduced insulin-binding capacity of the obese nuclei correlates with the reported decreased binding of insulin to plasma membranes prepared from target tissue of these animals. The possible physiological significance of nuclear insulin binding is discussed.
从小鼠肝脏中分离出的细胞核能够结合[125I]胰岛素。这些细胞核上存在一类高亲和力结合位点,其解离常数(Kd)为1 - 2 nM,结合能力约为每个细胞核2000个胰岛素分子。用Triton X - 100处理细胞核以去除核膜,会减少或消除高亲和力结合位点。无论肥胖小鼠(ob/ob)肝脏制备的细胞核是否经过Triton X - 100处理,这些细胞核都缺乏高亲和力结合位点,或者其数量显著减少。肥胖细胞核胰岛素结合能力的降低与报道的这些动物靶组织制备的质膜上胰岛素结合减少相关。本文讨论了细胞核胰岛素结合可能的生理意义。