ArticleShock (Augusta, Ga.)2015
α-Enolase Causes Proinflammatory Activation of Pulmonary Microvascular Endothelial Cells and Primes Neutrophils Through Plasmin Activation of Protease-Activated Receptor 2.
Article in Shock (Augusta, Ga.), 2015. 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, 21 citations in OpenAlex.
- Enolase-1 and Inflammation.Biomolecules · 2026Review
- Critical role of keratinocytes and protease-activated receptor 2 in secondary lymphedema development.Clinical and translational medicine · 2026Article
- Protease-activated receptor-2: Role in asthma pathogenesis and utility as a biomarker of disease severity.Frontiers in medicine · 2022Review
- Plasminogen activator receptor assemblies in cell signaling, innate immunity, and inflammation.American journal of physiology. Cell physiology · 2021Review
- Plasmin improves blood-gas barrier function in oedematous lungs by cleaving epithelial sodium channels.British journal of pharmacology · 2020Article
- Proteomic profiling of proteins in the dorsal horn of the spinal cord in dairy cows with chronic lameness.PloS one · 2020Article
- Fibrinolysis protease receptors promote activation of astrocytes to express pro-inflammatory cytokines.Journal of neuroinflammation · 2019Article
- Plasmin-mediated fibrinolysis enables macrophage migration in a murine model of inflammation.Blood · 2019Article
- Tissue-type plasminogen activator neutralizes LPS but not protease-activated receptor-mediated inflammatory responses to plasmin.Journal of leukocyte biology · 2019Article
- Schistosoma "Eggs-Iting" the Host: Granuloma Formation and Egg Excretion.Frontiers in immunology · 2018Review
- Supernatants and lipids from stored red blood cells activate pulmonary microvascular endothelium through the BLT2 receptor and protein kinase C activation.Transfusion · 2017Article
- Targeting Enolase in Reducing Secondary Damage in Acute Spinal Cord Injury in Rats.Neurochemical research · 2017Article
- Hemorrhagic shock and tissue injury drive distinct plasma metabolome derangements in swine.The journal of trauma and acute care surgery · 2017Article
- The accumulation of lipids and proteins during red blood cell storage: the roles of leucoreduction and experimental filtration.Blood transfusion = Trasfusione del sangue · 2017Review
- Neuron specific enolase: a promising therapeutic target in acute spinal cord injury.Metabolic brain disease · 2016Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
unlabelledProinflammatory activation of vascular endothelium leading to increased surface expression of adhesion molecules and neutrophil (PMN) sequestration and subsequent activation is paramount in the development of acute lung injury and organ injury in injured patients. We hypothesize that α-enolase, which accumulates in injured patients, primes PMNs and causes proinflammatory activation of endothelial cells leading to PMN-mediated cytotoxicity.
methodsProteomic analyses of field plasma samples from injured versus healthy patients were used for protein identification. Human pulmonary microvascular endothelial cells (HMVECs) were incubated with α-enolase or thrombin, and intercellular adhesion molecule-1 surface expression was measured by flow cytometry. A two-event in vitro model of PMN cytotoxicity HMVECs activated with α-enolase, thrombin, or buffer was used as targets for lysophosphatidylcholine-primed or buffer-treated PMNs. The PMN priming activity of α-enolase was completed, and lysates from both PMNs and HMVECs were immunoblotted for protease-activated receptor 1 (PAR-1) and PAR-2 and coprecipitation of α-enolase with PAR-2 and plasminogen/plasmin.
resultsα-Enolase increased 10.8-fold in injured patients (P < 0.05). Thrombin and α-enolase significantly increased intercellular adhesion molecule-1 surface expression on HMVECs, which was inhibited by antiproteases, induced PMN adherence, and served as the first event in the two-event model of PMN cytotoxicity. α-Enolase coprecipitated with PAR-2 and plasminogen/plasmin on HMVECs and PMNs and induced PMN priming, which was inhibited by tranexamic acid, and enzymatic activity was not required.
conclusionsα-Enolase increases after injury and may activate pulmonary endothelial cells and prime PMNs through plasmin activity and PAR-2 activation. Such proinflammatory endothelial activation may predispose to PMN-mediated organ injury.
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