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Access through your institution Buy or subscribe Although relaxin is structurally related to insulin, some data indicated that it might bind to a G-protein-coupled receptor (GPCR) instead of
a tyrosine-kinase receptor. So, the authors tested whether any of the orphan leucine-rich GPCRs (LGRs) might be the missing relaxin receptor. They expressed LGR7 or its relative LGR8 (which
was discovered based on GenBank searches for genes with similar structure to glycoprotein hormone receptors) in cells and found that relaxin could indeed increase cyclic AMP levels in these
cells in a dose-dependent manner, whereas it had no effect on cells that did not express these receptors. Crosslinking analysis showed that relaxin can bind to the extracellular domain of
LGR7. Moreover, the soluble extracellular domain of LGR7 inhibited the effect of relaxin on cells. This inhibition was also observed _in vivo_, as pregnant mice treated with the
extracellular domain of LGR7 had a delayed birth and reduced nipple size. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your
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our FAQs * Contact customer support REFERENCES ORIGINAL RESEARCH PAPER * Hsu, S. Y. et al. Activation of orphan receptors by the hormone relaxin. _Science_ 295, 671–674 (2002) Article CAS
Google Scholar FURTHER READING * Ivell, R. This hormone has been relaxin' too long. _Science_ 295, 637–638 (2002) Article CAS Google Scholar Download references Authors * Raluca
Gagescu View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Gagescu, R.
Time to relax. _Nat Rev Mol Cell Biol_ 3, 147 (2002). https://doi.org/10.1038/nrm748 Download citation * Issue Date: 01 March 2002 * DOI: https://doi.org/10.1038/nrm748 SHARE THIS ARTICLE
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