Adrenomedullin-RAMP2 System in Vascular Endothelial Cells
Authors:
Open Access
- 1 January 2015
- journal article
- review article
- Published by Japan Atherosclerosis Society in Journal of Atherosclerosis and Thrombosis
- Vol. 22 (7) , 647-653
Abstract
Vascular endothelial cells play key roles in maintaining vascular and organ homeostasis. Adrenomedullin (AM), originally identified as a vasodilating peptide, is now recognized to be a pleiotropic molecule involved in both circulatory homeostasis and the pathogenesis of cardiovascular diseases. We have reported that knockout mice deficient in AM or receptor activity-modifying protein 2 (RAMP2), an AM-receptor accessory protein, show vascular endothelial cell deformities that are embryonically lethal. To directly clarify the pathophysiological functions of the vascular AM-RAMP2 system, we generated vascular endothelial cell-specific RAMP2 knockout mice. Using these mice, we found that the AM-RAMP2 system is a key determinant of vascular integrity and homeostasis from prenatal stages through adulthood. This review highlights the functions of AM-RAMP2 in vascular endothelial cells.Keywords
This publication has 49 references indexed in Scilit:
- Inflammation 2010: New Adventures of an Old FlameCell, 2010
- Endothelial Function and Oxidative Stress in Cardiovascular DiseasesCirculation Journal, 2009
- Vascular Integrity Mediated by Vascular Endothelial Cadherin and Regulated by Sphingosine 1-Phosphate and Angiopoietin-1Circulation Journal, 2009
- The role of exercise and PGC1α in inflammation and chronic diseaseNature, 2008
- Vascular Cell SenescenceCirculation Research, 2007
- Endothelial cell–cell junctions: happy togetherNature Reviews Molecular Cell Biology, 2004
- Adrenomedullin augments collateral development in response to acute ischemiaBiochemical and Biophysical Research Communications, 2003
- Endothelial signaling during developmentNature Medicine, 2003
- Angiogenesis in health and diseaseNature Medicine, 2003
- Adrenomedullin: A Novel Hypotensive Peptide Isolated from Human PheochromocytomaBiochemical and Biophysical Research Communications, 1993