ArticleCirculation research2010
Plasminogen activator inhibitor-1 regulates myoendothelial junction formation.
Article in Circulation research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
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- Unbiased proteomics identifies plasminogen activator inhibitor-1 as a negative regulator of endothelial nitric oxide synthase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Myoendothelial Junctions of Mature Coronary Vessels Express Notch Signaling Proteins.Frontiers in physiology · 2020Article
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- No Sweetie Pie: Newly Uncovered Role for PAI (Plasminogen Activator Inhibitor)-1 in Inflammatory Responses to Ischemia/Reperfusion.Arteriosclerosis, thrombosis, and vascular biology · 2018Article
- Targeting Pulmonary Endothelial Hemoglobin α Improves Nitric Oxide Signaling and Reverses Pulmonary Artery Endothelial Dysfunction.American journal of respiratory cell and molecular biology · 2017Article
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- A Cell Culture Model of Resistance Arteries.Journal of visualized experiments : JoVE · 2017Article
- Two functionally distinct pools of eNOS in endothelium are facilitated by myoendothelial junction lipid composition.Biochimica et biophysica acta · 2016Article
- Endothelium-Derived Hyperpolarization and Coronary Vasodilation: Diverse and Integrated Roles of Epoxyeicosatrienoic Acids, Hydrogen Peroxide, and Gap Junctions.Microcirculation (New York, N.Y. : 1994) · 2016Review
- Recombinant PAI-1 therapy restores myoendothelial junctions and erectile function in PAI-1-deficient mice.Andrologia · 2015Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
rationalePlasminogen activator inhibitor-1 (PAI-1) is a biomarker for several vascular disease states; however, its target of action within the vessel wall is undefined.
objectiveDetermine the ability of PAI-1 to regulate myoendothelial junction (MEJ) formation. METHODS AND
resultsMEJs are found throughout the vasculature linking endothelial cells (ECs) and vascular smooth muscle cells. Using a vascular cell coculture we isolated MEJ fractions and performed two-dimensional differential gel electrophoresis. Mass spectrometry identified PAI-1 as being enriched within MEJ fractions, which we confirmed in vivo. In the vascular cell coculture, recombinant PAI-1 added to the EC monolayer significantly increased MEJs. Conversely, addition of a PAI-1 monoclonal antibody to the EC monolayer reduced the number of MEJs. This was also observed in vivo where mice fed a high fat diet had increased PAI-1 and MEJs and the number of MEJs in coronary arterioles of PAI-1(-/-) mice was significantly reduced when compared to C57Bl/6 mice. The presence of MEJs in PAI-1(-/-) coronary arterioles was restored when their hearts were transplanted into and exposed to the circulation of C57Bl/6 mice. Application of biotin-conjugated PAI-1 to the EC monolayer in vitro confirmed the ability of luminal PAI-1 to translocate to the MEJ. Functionally, phenylephrine-induced heterocellular calcium communication in the vascular cell coculture was temporally enhanced when recombinant PAI-1 was present, and prolonged when PAI-1 was absent.
conclusionOur data implicate circulating PAI-1 as a key regulator of MEJ formation and a potential target for pharmacological intervention in diseases with vascular abnormalities (eg, diabetes mellitus).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.