Human growth hormone deletion mutant (hGH44-191) binds with high affinity to lactogenic receptors but not to somatogenic receptors.
Human growth hormone deletion mutant (hGH44-191) binds with high affinity to lactogenic receptors but not to somatogenic receptors.
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DOI：
10.1006/bbrc.1996.0760
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发表时间：
1996-05
影响因子：
3.1
通讯作者：
L. Haro;R. Singh;U. Lewis;A. Martinez;S. Galosy;N. Staten;G. Krivi
中科院分区：
文献类型：
--
作者：
L. Haro;R. Singh;U. Lewis;A. Martinez;S. Galosy;N. Staten;G. Krivi
羧基末端hGH片段hGH 44 -191显示出致糖尿病活性。为了了解这种生物活性是否是通过促体细胞生长或催乳受体介导的，我们研究了hGH 44 -191结合两种受体类别的能力。我们发现，hGH 44 -191不能与[125 I]hGH或[125 I]bGH竞争牛肝体原性结合位点。此外，当使用人肝微粒体作为受体来源时，hGH 44 -191不能从体源性受体位点置换[125 I]hGH。相比之下，hGH 44 -191有效地与[125 I]hGH竞争泌乳乳腺微粒体和牛肝微粒体的催乳受体位点。总之，hGH 44 -191不与体细胞受体结合，但也不与催乳受体结合。这些数据表明，hGH 44 -191的生物学作用可以通过催乳素受体介导。
The carboxyl-terminal hGH fragment, hGH44-191, displays diabetogenic activity. To understand whether this biological activity is mediated through somatogenic or lactogenic receptors, we investigated the ability of hGH44-191 to bind both receptor classes. We found that hGH44-191 could not compete with [125I]hGH or [125I]bGH for bovine liver somatogenic binding sites. Additionally, hGH44-191 could not displace [125I]hGH from the somatogenic receptor sites when human liver microsomes were used as the receptor source. In contrast, hGH44-191 effectively competed with [125I]hGH for lactogenic receptor sites of lactating mammary gland microsomes and of bovine liver microsomes. In summary, hGH44-191 does not bind to somatogenic receptors but does not bind to lactogenic receptors. These data suggest that the biological actions of hGH44-191 could be mediated through lactogenic receptors.