Krett N L, Wei L L, Francis M D, Nordeen S K, Gordon D F, Wood W M, Horwitz K B
Department of Medicine, University of Colorado Health Sciences Center, Denver 80262.
Biochem Biophys Res Commun. 1988 Nov 30;157(1):278-85. doi: 10.1016/s0006-291x(88)80044-5.
In order to investigate the origin and functional independence of the human progesterone receptor A binding protein, we have expressed a truncated human progesterone receptor cDNA in both gene transfer and in vitro translation assays. Proteins identical in size and antigenicity to the A-receptors found naturally in human progesterone target cells are synthesized from this cDNA that lacks the putative B receptor initiator methionine codon of the complete cDNA. The functional independence of A-receptors is suggested by their ability to bind hormone and to stimulate transcription from the progestin responsive mouse mammary tumor virus promoter.
为了研究人孕激素受体A结合蛋白的起源和功能独立性，我们在基因转移和体外翻译试验中表达了截短的人孕激素受体cDNA。从该缺少完整cDNA推定的B受体起始甲硫氨酸密码子的cDNA中合成的蛋白质，其大小和抗原性与人孕激素靶细胞中天然存在的A受体相同。A受体能够结合激素并刺激孕激素反应性小鼠乳腺肿瘤病毒启动子的转录，这表明了其功能独立性。
