Mayeux P, Pallu S, Gobert S, Lacombe C, Gisselbrecht S
INSERM U363, ICGM, Hopital Cochin, Paris, France.
Proc Soc Exp Biol Med. 1994 Jul;206(3):200-4. doi: 10.3181/00379727-206-43742.
Despite extensive studies, the structure of the erythropoietin receptor remains little understood. cDNAs encoding the human and murine erythropoietin receptors have been cloned and the structure of these proteins is discussed. Although the proteins encoded by these cDNAs play key roles in erythropoietin binding and in erythropoietin signal transduction, increasing evidence strongly suggests that the erythropoietin receptor is a multimeric complex. The murine erythropoietin receptor has been solubilized under mild conditions and the molecular mass of the native receptor has been shown to be significantly higher than the molecular mass of the cloned chain. Cross-linking experiments have revealed the presence of three proteins covalently bound to erythropoietin by the cross-linking reagents; however, only one of them seems to derive from the cloned chain. Moreover, functional evidence also suggests the presence of other erythropoietin receptor subunits.
尽管进行了广泛的研究，但促红细胞生成素受体的结构仍知之甚少。编码人和鼠促红细胞生成素受体的cDNA已被克隆，并对这些蛋白质的结构进行了讨论。虽然这些cDNA编码的蛋白质在促红细胞生成素结合和促红细胞生成素信号转导中起关键作用，但越来越多的证据强烈表明促红细胞生成素受体是一种多聚体复合物。鼠促红细胞生成素受体已在温和条件下溶解，天然受体的分子量已显示明显高于克隆链的分子量。交联实验揭示了三种蛋白质通过交联试剂与促红细胞生成素共价结合；然而，其中只有一种似乎来自克隆链。此外，功能证据也表明存在其他促红细胞生成素受体亚基。
