Inhibition of apelin expression by BMP signaling in endothelial cells
- Resource Type
- Authors
- Florent Soubrier; Kevin Montagne; Mélanie Eyries; Sophie Nadaud; Odette Poirier; Mariana Ciumas
- Source
- American Journal of Physiology-Cell Physiology
American Journal of Physiology-Cell Physiology, 2012, 303 (11), pp.C1139-C1145. ⟨10.1152/ajpcell.00168.2012⟩
- Subject
- medicine.medical_specialty
animal structures
Physiology
Angiogenesis
Bone Morphogenetic Protein 7
[SDV]Life Sciences [q-bio]
Smad Proteins
SMAD
Bone Morphogenetic Protein 4
Bone morphogenetic protein
Cell Line
Internal medicine
medicine
Growth Differentiation Factor 2
Humans
Hypoxia
Lung
Neovascularization, Pathologic
Chemistry
Growth differentiation factor
Endothelial Cells
Cell Biology
BMPR2
Apelin
Cell biology
Endothelial stem cell
Growth Differentiation Factors
Endocrinology
Gene Expression Regulation
embryonic structures
Bone Morphogenetic Proteins
Microvessels
Intercellular Signaling Peptides and Proteins
Signal transduction
Signal Transduction
- Language
- English
- ISSN
- 0363-6143
1522-1563
International audience; The transforming growth factor-β/bone morphogenic protein (BMP) system is a major pathway for angiogenesis and is involved in hereditary vascular diseases. Here we report that the gene encoding the vasoactive and vascular cell growth-regulating peptide apelin is a target of the BMP pathway. We demonstrate that apelin expression is strongly downregulated by BMP in an endothelial cell line as well as in lung endothelial microvascular cells. We show that BMP signals through the BMPR2-SMAD pathway to downregulate apelin expression and that a transcriptional direct and indirect mechanism is required. The BMP-induced downregulation of apelin expression was found to be critical for hypoxia-induced growth of endothelial cells, because the growth inhibitory effect of BMP in this condition is suppressed by enforced expression of apelin. Thus, we describe an important link between a signaling pathway involved in angiogenesis and vascular diseases and a peptide regulating vascular homeostasis.