Dusanter-Fourt I, Djiane J, Houdebine L M, Kelly P A
Life Sci. 1983 Jan 24;32(4):407-12. doi: 10.1016/0024-3205(83)90087-5.
Antibodies generated against partially purified prolactin receptors from rabbit mammary gland membranes were tested for their effects on prolactin binding to receptors and for their in vivo biological potencies. These antibodies are able to inhibit prolactin binding to crude rabbit mammary gland membranes. When administered intravenously or intramuscularly to pseudopregnant rabbits, they induce respectively an accumulation of beta-casein or an enhancement of beta-casein synthesis and mRNA concentration in the mammary gland. Moreover the stimulatory effect of these anti-prolactin receptor antibodies on casein synthesis is totally abolished by a simultaneous treatment with progesterone, which is a potent in vivo inhibitor of prolactin action. These results better establish the prolactin-like activities of these antibodies previously observed in vitro and give strong support to the hypothesis that prolactin molecule is not required beyond the initial binding to its receptor to induce hormonal effects.
针对从兔乳腺膜中部分纯化的催乳素受体产生的抗体,对其影响催乳素与受体结合的作用及其体内生物学效能进行了测试。这些抗体能够抑制催乳素与兔乳腺粗膜的结合。当对假孕兔静脉内或肌肉内给药时,它们分别诱导β-酪蛋白的积累或乳腺中β-酪蛋白合成及mRNA浓度的增加。此外,通过同时用孕酮处理,这些抗催乳素受体抗体对酪蛋白合成的刺激作用完全消除,孕酮是催乳素作用的一种有效的体内抑制剂。这些结果更好地证实了先前在体外观察到的这些抗体的催乳素样活性,并为以下假设提供了有力支持:催乳素分子在与其受体初始结合后并不需要,即可诱导激素效应。