Abstract
The peptide hormone relaxin mediates many biological actions including anti-fibrotic, vasodilatory, angiogenic, anti-inflammatory, anti-apoptotic, and organ protective effects across a range of tissues. At the cellular level, relaxin binds to the G protein-coupled receptor relaxin family peptide receptor 1 (RXFP1) to activate a variety of downstream signal transduction pathways. This signalling cascade is complex and also varies in diverse cellular backgrounds. Moreover, RXFP1 signalling shows crosstalk with other receptors to mediate some of its physiological functions. This review summarises known signalling pathways induced by acute versus chronic treatment with relaxin across a range of cell types, it describes RXFP1 crosstalk with other receptors, signalling pathways activated by other ligands targeting RXFP1, and it also outlines physiological relevance of RXFP1 signalling outputs. Comprehensive understanding of the mechanism of relaxin actions in fibrosis, vasodilation, as well as organ protection, will further support relaxin's clinical potential.
| Original language | English |
|---|---|
| Pages (from-to) | 24-33 |
| Number of pages | 10 |
| Journal | Molecular and Cellular Endocrinology |
| Volume | 487 |
| DOIs | |
| Publication status | Published - 1 May 2019 |
Keywords
- GPCR
- Insulin-like peptides
- Relaxin
- RXFP1
Cite this
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Understanding relaxin signalling at the cellular level. / Valkovic, Adam L.; Bathgate, Ross AD; Samuel, Chrishan S.; Kocan, Martina.
In: Molecular and Cellular Endocrinology, Vol. 487, 01.05.2019, p. 24-33.Research output: Contribution to journal › Review Article › Research › peer-review
TY - JOUR
T1 - Understanding relaxin signalling at the cellular level
AU - Valkovic, Adam L.
AU - Bathgate, Ross AD
AU - Samuel, Chrishan S.
AU - Kocan, Martina
PY - 2019/5/1
Y1 - 2019/5/1
N2 - The peptide hormone relaxin mediates many biological actions including anti-fibrotic, vasodilatory, angiogenic, anti-inflammatory, anti-apoptotic, and organ protective effects across a range of tissues. At the cellular level, relaxin binds to the G protein-coupled receptor relaxin family peptide receptor 1 (RXFP1) to activate a variety of downstream signal transduction pathways. This signalling cascade is complex and also varies in diverse cellular backgrounds. Moreover, RXFP1 signalling shows crosstalk with other receptors to mediate some of its physiological functions. This review summarises known signalling pathways induced by acute versus chronic treatment with relaxin across a range of cell types, it describes RXFP1 crosstalk with other receptors, signalling pathways activated by other ligands targeting RXFP1, and it also outlines physiological relevance of RXFP1 signalling outputs. Comprehensive understanding of the mechanism of relaxin actions in fibrosis, vasodilation, as well as organ protection, will further support relaxin's clinical potential.
AB - The peptide hormone relaxin mediates many biological actions including anti-fibrotic, vasodilatory, angiogenic, anti-inflammatory, anti-apoptotic, and organ protective effects across a range of tissues. At the cellular level, relaxin binds to the G protein-coupled receptor relaxin family peptide receptor 1 (RXFP1) to activate a variety of downstream signal transduction pathways. This signalling cascade is complex and also varies in diverse cellular backgrounds. Moreover, RXFP1 signalling shows crosstalk with other receptors to mediate some of its physiological functions. This review summarises known signalling pathways induced by acute versus chronic treatment with relaxin across a range of cell types, it describes RXFP1 crosstalk with other receptors, signalling pathways activated by other ligands targeting RXFP1, and it also outlines physiological relevance of RXFP1 signalling outputs. Comprehensive understanding of the mechanism of relaxin actions in fibrosis, vasodilation, as well as organ protection, will further support relaxin's clinical potential.
KW - GPCR
KW - Insulin-like peptides
KW - Relaxin
KW - RXFP1
UR - http://www.scopus.com/inward/record.url?scp=85060718648&partnerID=8YFLogxK
U2 - 10.1016/j.mce.2018.12.017
DO - 10.1016/j.mce.2018.12.017
M3 - Review Article
VL - 487
SP - 24
EP - 33
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
SN - 0303-7207
ER -