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Role of nitric oxide and phosphodiesterase isoenzyme II for reduction of endothelial hyperpermeability
Abstract
Regulation of endothelial permeability is poorly understood. Previous studies have shown that endothelial cells contain phosphodiesterase (PDE) isoenzymes II-IV and that simultaneous adenylate cyclase activation and/or PDE inhibition blocked endothelial hyperpermeability (J.Clin.Invest. 91: 1421-1428, 1993). We now focused on a possible role for guanosine 3',5'-cyclic monophosphate (cGMP)-dependent mechanisms and studied H2O2-exposed porcine pulmonary artery endothelial cell monolayers. Pretreatment of cells with different nitric oxide (NO) donors or atrial natriuretic peptide (ANP) increased endothelial cGMP-content severalfold and blocked H2O2-related effects on permeability; opposite results were obtained with a NO synthase inhibitor. Determination of cGMP degradation in nitroprusside-exposed endothelial cells identified PDE II as the major cGMP metabolizing pathway, whereas PDE III and IV contributed little or nothing. Inhibition of PDE II reduced H2O2-related endothelial hyperpermeability, an effect that could be enhanced synergistically by simultaneous guanylate cyclase activation. In summary, these studies indicate that cGMP-dependent mechanisms (NO donors, ANP, and dibutyryl-cGMP) blocked H2O2-related increases in endothelial permeability. The major cGMP degrading pathway in endothelial cells was PDE II, thereby substituting the missing PDE V in these cells. Simultaneous guanylate cyclase activation and/or PDE II inhibition may be a valuable approach to treat endothelial hyperpermeability.
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“Enterochromaffin cells secrete serotonin and signaling peptides (for example, corticotropin-releasing hormone, cholecystokinin and somatostatin) in response to various physiological and pathological luminal stimuli,53-55 such as microbial factors or bacterial toxins,56-58 as well as central stimuli (see discussion above).31,32”
From Principles and clinical implications of the brain-gut-enteric microbiota axis (2009) · cites this paper as [56]
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Metadata
- Authors
- Suttorp, N., Hippenstiel, S., Fuhrmann, M., Krull, M., & Podzuweit, T.
- Affiliations
- Justus-Liebig-Universität Gießen (DE)
- Department of Internal Medicine, Justus Liebig-University of Giessen,Germany.
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 1996-03-01
- Volume
- 270
- Issue
- 3
- Pages
- C778-C785
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2413676558
- Cited by
- 133
- References
- 20
- Citations by year
- 2025: 1 · 2022: 1 · 2021: 1 · 2017: 2 · 2016: 5 · 2015: 1 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 2.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Phosphodiesterase function and regulation
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
- Keywords
- endothelial hyperpermeability, nitric oxide, cyclic GMP, hydrogen peroxide, atrial natriuretic peptide, guanylate cyclase, endothelial permeability, pulmonary artery endothelial cells, nitric oxide synthase, cGMP degradation
- MeSH terms
- Animals, Arginine, Cell Membrane Permeability, Cells, Cultured, Electric Conductivity, Endothelium, Vascular, Enzyme Inhibitors, Escherichia coli, Nitroglycerin, Hemolysin Proteins, Hydrogen Peroxide, Isoenzymes, Kinetics, Molsidomine, Nitric Oxide, Nitroprusside, Phosphoric Diester Hydrolases, Pulmonary Artery, Swine, Nitric Oxide Synthase, Nitroarginine
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