Aldosterone Potentiates Angiotensin II–Induced Signaling in Vascular Smooth Muscle Cells
Open accessAbstract
Background— In a double-transgenic human renin and human angiotensinogen rat model, we found that mineralocorticoid receptor (MR) blockade ameliorated angiotensin II (Ang II)–induced renal and cardiac damage. How Ang II and aldosterone (Ald) might interact is ill defined. Methods and Results— We investigated the effects of Ang II (10 −7 mol/L) and Ald (10 −7 mol/L) on extracellular signal–regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) signaling in vascular smooth muscle cells (VSMCs) with Western blotting and confocal microscopy. Ang II induced ERK 1/2 and JNK phosphorylation by 2 minutes. Ald achieved the same at 10 minutes. Ang II+Ald had a potentiating effect by 2 minutes. Two oxygen radical scavengers and the epidermal growth factor receptor (EGFR) antagonist AG1478 reduced Ang II–, Ald-, and combination-induced ERK1/2 phosphorylation. Preincubating the cells with the MR blocker spironolactone (10 −6 mol/L) abolished Ang II–induced ROS generation, EGFR transactivation, and ERK1/2 phosphorylation. Conclusions— Ald potentiates Ang II–induced ERK-1/2 and JNK phosphorylation. Oxygen radicals, the MR, and the EGFR play a role in early signaling induced by Ang II and Ald in VSMCs. These in vitro data may help explain the effects of MR blockade on Ang II–induced end-organ damage in vivo.
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Aldosterone enhances Ang II-stimulated ERK1/2 phosphorylation in vascular smooth muscle cells.
“Aldosterone enhances Ang II-stimulated ERK1/2 phosphorylation in vascular smooth muscle cells.”
From The Vasculature in Prediabetes (2018) · cites this paper as [104]
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References 39 · Cited by 218
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- Carpenter G. The EGF receptor: a nexus for trafficking and signaling. Bioessays. 2000;22:697-707.
- Authors
- Mazak, I., Fiebeler, A., Muller, D. N., Park, J.-K., Shagdarsuren, E., Lindschau, C., Dechend, R., Viedt, C., Pilz, B., Haller, H., & Luft, F. C.
- Affiliations
- From Medical Faculty of the Charité, Franz Volhard Clinic, HELIOS Klinikum-Berlin and Max Delbrück Center for Molecular Medicine, Berlin, Germany (I.M., A.F., D.N.M., E.S., R.D., B.P., F.C.L.); the Department of Internal Medicine and Nephrology, Hannover University Medical School, Hannover, Germany (J.-K.P., C.L., H.H.); and the Department of Internal Medicine III, University of Heidelberg, Heidelberg, Germany (C.V.).
- Max Delbrück Center (DE)
- Venue
- Circulation
- Published
- 2004-06-08
- Volume
- 109
- Issue
- 22
- Pages
- 2792-2800
- ISSN
- 0009-7322 (ISSN-L)
- 1524-4539
- OpenAlex
- W2126174661
- Cited by
- 218
- References
- 39
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 2 · 2022: 6 · 2021: 5 · 2020: 4 · 2019: 2 · 2018: 8 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 11 · 2013: 9 · 2012: 11
- FWCI
- 17.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation (publishedVersion)
- PubMed (publishedVersion)
- German Medical Science (German Research Foundation) (publishedVersion, cc-by-nc-nd)
- MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
- Keywords
- aldosterone, angiotensin II, vascular smooth muscle cells, mineralocorticoid receptor, ERK1/2 phosphorylation, JNK phosphorylation, reactive oxygen species, epidermal growth factor receptor transactivation, spironolactone, renin-angiotensin system
- MeSH terms
- Aldosterone, Mineralocorticoid Receptor Antagonists, Angiotensin II, Animals, Cells, Cultured, Male, Muscle, Smooth, Vascular, Phosphorylation, Spironolactone, Signal Transduction, Rats, Sprague-Dawley, Reactive Oxygen Species, Animals, Genetically Modified, JNK Mitogen-Activated Protein Kinases, Extracellular Signal-Regulated MAP Kinases, Rats, ErbB Receptors
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