ArticleProtein science : a publication of the Protein Society2011
Metals affect the structure and activity of human plasminogen activator inhibitor-1. I. Modulation of stability and protease inhibition.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- A Narrative Review on Plasminogen Activator Inhibitor-1 and Its (Patho)Physiological Role: To Target or Not to Target?International journal of molecular sciences · 2021Review
- Dissecting molecular details and functional effects of the high-affinity copper binding site in plasminogen activator Inhibitor-1.Protein science : a publication of the Protein Society · 2021Article
- Identification of a PAI-1-binding site within an intrinsically disordered region of vitronectin.Protein science : a publication of the Protein Society · 2020Article
- High-affinity binding of plasminogen-activator inhibitor 1 complexes to LDL receptor-related protein 1 requires lysines 80, 88, and 207.The Journal of biological chemistry · 2020Article
- Targeting PAI-1 in Cardiovascular Disease: Structural Insights Into PAI-1 Functionality and Inhibition.Frontiers in cardiovascular medicine · 2020Review
- Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region.Biochemistry · 2019Article
- Resolving distinct molecular origins for copper effects on PAI-1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Distinct encounter complexes of PAI-1 with plasminogen activators and vitronectin revealed by changes in the conformation and dynamics of the reactive center loop.Protein science : a publication of the Protein Society · 2016Article
- Single fluorescence probes along the reactive center loop reveal site-specific changes during the latency transition of PAI-1.Protein science : a publication of the Protein Society · 2016Article
- Application of long-acting VLHL PAI-1 during sutureless partial nephrectomy in mice reduces bleeding.BioMed research international · 2015Article
- Vitronectin inhibits efferocytosis through interactions with apoptotic cells as well as with macrophages.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Vitronectin inhibits neutrophil apoptosis through activation of integrin-associated signaling pathways.American journal of respiratory cell and molecular biology · 2012Article
- Crystal structure of plasminogen activator inhibitor-1 in an active conformation with normal thermodynamic stability.The Journal of biological chemistry · 2011Article
- Metals affect the structure and activity of human plasminogen activator inhibitor-1. II. Binding affinity and conformational changes.Protein science : a publication of the Protein Society · 2011Article
- A critical review on serine protease: Key immune manipulator and pathology mediator.Allergologia et immunopathologiaReview
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Human plasminogen activator inhibitor type 1 (PAI-1) is a serine protease inhibitor with a metastable active conformation. Under physiological conditions, half of the inhibitor transitions to a latent state within 1-2 h. The interaction between PAI-1 and the plasma protein vitronectin prolongs this active lifespan by ∼50%. Previously, our group demonstrated that PAI-1 binds to resins using immobilized metal affinity chromatography (Day, U.S. Pat. 7,015,021 B2, March 21, 2006). In this study, the effect of these metals on function and stability was investigated by measuring the rate of the transition from the active to latent conformation. All metals tested showed effects on stability, with the majority falling into one of two types depending on their effects. The first type of metal, which includes magnesium, calcium and manganese, invoked a slight stabilization of the active conformation of PAI-1. A second category of metals, including cobalt, nickel and copper, showed the opposite effects and a unique vitronectin-dependent modulation of PAI-1 stability. This second group of metals significantly destabilized PAI-1, although the addition of vitronectin in conjunction with these metals resulted in a marked stabilization and slower conversion to the latent conformation. In the presence of copper and vitronectin, the half-life of active PAI-1 was extended to 3 h, compared to a half-life of only ∼30 min with copper alone. Nickel had the largest effect, reducing the half-life to ∼5 min. Together, these data demonstrate a heretofore-unknown role for metals in modulating PAI-1 stability.
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Registered trials
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