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Mol. Hum. Reprod. Advance Access originally published online on July 28, 2005
Molecular Human Reproduction 2005 11(8):591-600; doi:10.1093/molehr/gah205
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© The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oupjournals.org

Splice variants of the relaxin and INSL3 receptors reveal unanticipated molecular complexity

Marco Muda1,4, Chaomei He1, Paolo G.V. Martini1, Tania Ferraro2, Sharon Layfield2, Deanne Taylor1, Colette Chevrier1, Rene Schweickhardt1, Christie Kelton1, Peter L. Ryan3 and Ross A.D. Bathgate2

1Serono Research Institute, One Technology Place, Rockland, MA, USA, 2Howard Florey Institute, University of Melbourne, Victoria, Australia and 3Department of Animal and Dairy Sciences, Mississippi State University, MS, USA

4 To whom correspondence should be addressed at: Serono Research Institute, One Technology Place, Rockland, MA 02370, USA. E-mail: marco.muda{at}serono.com

LGR7 and LGR8 are G protein-coupled receptors that belong to the leucine-rich repeat-containing G-protein coupled receptor (LGR) family, including the thyroid-stimulating hormone (TSH), LH and FSH receptors. LGR7 and LGR8 stimulate cAMP production upon binding of the cognate ligands, relaxin and insulin-like peptide 3 (INSL3), respectively. We cloned several novel splice variants of both LGR7 and LGR8 and analysed the function of four variants. LGR7.1 is a truncated receptor, including only the N-terminal region of the receptor and two leucine rich repeats. In contrast, LGR7.2, LGR7.10 and LGR 8.1 all contain an intact seven transmembrane domain and most of the extracellular region, lacking only one or two exons in the ectodomain. Our analysis demonstrates that although LGR7.10 and LGR8.1 are expressed at the cell surface, LGR7.2 is predominantly retained within cells and LGR7.1 is partially secreted. mRNA expression analysis revealed that several variants are co-expressed in various tissues. None of these variants were able to stimulate cAMP production following relaxin or INSL3 treatment. Unexpectedly, we did not detect any direct specific relaxin or INSL3 binding on any of the splice variants. The large number of receptor splice variants identified suggests an unforeseen complexity in the physiology of this novel hormone-receptor system.

Key words: GPCR/INSL3/LGR7/LGR8/relaxin/splice variants


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