Study summary · research use only
Human growth hormone deletion mutant (hGH44-191) binds with high affinity to lactogenic receptors but not to somatogenic receptors
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This in vitro study investigated whether the carboxyl-terminal hGH fragment hGH44-191, which displays diabetogenic activity, binds somatogenic or lactogenic receptors. The abstract reports hGH44-191 could not compete with [125I]hGH or [125I]bGH for bovine liver somatogenic binding sites, nor displace [125I]hGH from somatogenic sites on human liver microsomes. In contrast, hGH44-191 competed with [125I]hGH for lactogenic receptor sites of lactating mammary gland and bovine liver microsomes. The authors conclude the biological actions of hGH44-191 could be mediated through lactogenic receptors.
Abstract
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.
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