Glycosylation selectively alters the biological activity of prolactin.
Glycosylation selectively alters the biological activity of prolactin.
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DOI：
10.1210/endo-123-3-1303
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发表时间：
1988-09
期刊：
影响因子：
4.8
通讯作者：
E. Markoff;M. B. Sigel;N. Lacour;B. K. Seavey;H. Friesen;U. Lewis
中科院分区：
文献类型：
--
作者：
E. Markoff;M. B. Sigel;N. Lacour;B. K. Seavey;H. Friesen;U. Lewis
我们进行了研究，以确定糖基化对绵羊催乳素（oPRL）催乳活性的影响。在体外小鼠乳腺外植体试验中测定酪蛋白的产生，我们发现糖基化的oPRL具有oPRL活性的80%。在使用泌乳兔乳腺催乳素受体的竞争性结合研究中，糖基化oPRL的效力仅为oPRL的20%。在Nb2试验中，糖基化oPRL在刺激促有丝分裂活性方面的效力也约为oPRL的24%。因此，这些研究表明，PRL的糖基化变体具有比主要PRL形式更低的生物活性，并且通过糖基化改变活性是选择性的。
We have undertaken studies to determine the effect of glycosylation on the lactogenic activity of ovine PRL (oPRL). Measuring casein production in the in vitro mouse mammary gland explant assay, we found that glycosylated oPRL had 80% of the activity of oPRL. In competitive binding studies using lactogen receptors from mammary glands of lactating rabbits, glycosylated oPRL had only 20% the potency of oPRL. In the Nb2 assay also, glycosylated oPRL was approximately 24% as potent as oPRL in stimulating mitogenic activity. Thus, these studies show that the glycosylated variant of PRL has less biological activity than the major PRL form and that the alteration of an activity by glycosylation is selective.