Journal article

Structure and function relationship of murine insulin-like peptide 5 (INSL5): Free C-terminus is essential for RXFP4 receptor binding and activation

A Belgi, MA Hossain, F Shabanpoor, L Chan, S Zhang, RAD Bathgate, GW Tregear, JD Wade

Biochemistry | AMER CHEMICAL SOC | Published : 2011

Abstract

Insulin-like peptide 5 (INSL5) is a member of insulin/relaxin superfamily of peptides. It has recently been identified as the cognate ligand for the G-protein-coupled receptor, RXFP4. Although the complete physiological role of this naturally occurring peptide is still under investigation, there is evidence that it acts to both stimulate appetite and activate colon motility. This suggests that both agonists and antagonists of the peptide may have potential therapeutic applications. To further investigate the physiological role of this peptide and because of the ready availability of the mouse as an experimental animal, the preparation of mouse INSL5 was undertaken. Because of its complex str..

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University of Melbourne Researchers