Journal of Thrombosis and Haemostasis最新文献

{"title":"Choosing the optimal oral anticoagulant for stroke prevention in atrial fibrillation: direct oral anticoagulants vs vitamin K antagonists","authors":"Stephanie Carlin ,&nbsp;Noel Chan ,&nbsp;Alejandro Godoy ,&nbsp;Vinai Bhagirath ,&nbsp;Jack Hirsh ,&nbsp;John Eikelboom","doi":"10.1016/j.jtha.2024.11.005","DOIUrl":"10.1016/j.jtha.2024.11.005","url":null,"abstract":"<div><div>Direct oral anticoagulants (DOACs) have replaced vitamin K antagonists (VKAs) for stroke prevention in many patients with atrial fibrillation, but VKAs may still be preferred in some situations. We use a case-based approach to present the evidence for the possible use of a VKA in preference to a DOAC in patients with atrial fibrillation and rheumatic mitral stenosis, high body mass index, frailty, and breakthrough stroke despite being prescribed a DOAC.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1207-1214"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142710571","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mice with reduced protease-activated receptor 4 reactivity show decreased venous thrombosis and platelet procoagulant activity","authors":"Elizabeth A. Knauss ,&nbsp;Johana Guci ,&nbsp;Norman Luc ,&nbsp;Dante Disharoon ,&nbsp;Grace H. Huang ,&nbsp;Anirban Sen Gupta ,&nbsp;Marvin T. Nieman","doi":"10.1016/j.jtha.2024.12.031","DOIUrl":"10.1016/j.jtha.2024.12.031","url":null,"abstract":"<div><h3>Background</h3><div>Hypercoagulation and thrombin generation are major risk factors for venous thrombosis. Sustained thrombin signaling through protease-activated receptor (PAR) 4 promotes platelet activation, phosphatidylserine exposure, and subsequent thrombin generation. A single nucleotide polymorphism in PAR4 (rs2227376) changes proline to leucine extracellular loop 3, which decreases PAR4 reactivity and is associated with a lower risk for venous thromboembolism (VTE) in a genome wide association studies meta-analysis.</div></div><div><h3>Objectives</h3><div>The goal of this study was to determine the mechanism for the association of rs2227376 with a reduced risk of VTE using mice with a homologous mutation (PAR4-P322L).</div></div><div><h3>Methods</h3><div>Venous thrombosis was examined using our recently generated PAR4-P322L mice in the inferior vena cava stasis and stenosis models. Coagulation and clot stability were measured using rotational thromboelastometry. Thrombin-generating potential was measured in platelet-rich plasma. Phosphatidylserine surface expression and platelet-neutrophil aggregates were analyzed using flow cytometry.</div></div><div><h3>Results</h3><div>Mice heterozygous (PAR4^P/L) or homozygous (PAR4^L/L) at position 310 had reduced sizes of venous clots at 48 hours. PAR4^P/L and PAR4^L/L platelets had progressively decreased phosphatidylserine in response to thrombin and convulxin, in addition to decreased thrombin generation and decreased PAR4-mediated platelet-neutrophil aggregation.</div></div><div><h3>Conclusion</h3><div>The leucine allele in extracellular loop 3, PAR4-322L, leads to fewer procoagulant platelets, decreased endogenous thrombin potential, and reduced platelet-neutrophil aggregation. This decreased ability to generate thrombin and bind to neutrophils offers a mechanism for PAR4’s role in VTE, highlighting a key role for PAR4 signaling.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1278-1288"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142971363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peak and trough concentrations of apixaban and rivaroxaban in adult patients: a systematic review and meta-analysis","authors":"Christian Andrew Almalbis ,&nbsp;Adyani Md Redzuan ,&nbsp;Chester Paul Andrada ,&nbsp;Nicole Ann Gonzaga ,&nbsp;Shamin Mohd Saffian","doi":"10.1016/j.jtha.2024.12.032","DOIUrl":"10.1016/j.jtha.2024.12.032","url":null,"abstract":"<div><h3>Background</h3><div>Apixaban and rivaroxaban are activated factor X (FXa) inhibitors commonly used for treatment of venous thromboembolism and stroke prevention in patients with atrial fibrillation. While routine monitoring of their concentrations is not recommended, but it may be beneficial in certain situations. Expected peak and trough concentrations remain poorly understood, with most data derived from small studies.</div></div><div><h3>Objectives</h3><div>To establish the average peak and trough concentrations of apixaban and rivaroxaban from real-world studies.</div></div><div><h3>Methods</h3><div>PubMed, Scopus, and Web of Science were searched until October 2023 for observational studies reporting apixaban and rivaroxaban concentrations. Meta-regression was used to examine factors influencing these concentrations.</div></div><div><h3>Results</h3><div>Sixteen studies involving 1054 apixaban and 1321 rivaroxaban patients were pooled using random-effects model. Mean apixaban peak concentrations were 157 ng/mL (95% CI, 127-187) for 2.5 mg and 228 ng/mL (95% CI, 204-252) for 5 mg, with trough concentrations of 77 ng/mL (95% CI, 56-98) and 113 ng/mL (95% CI, 101-124), respectively. Mean rivaroxaban peak concentrations were 168 ng/mL (95% CI, 104-232) for 10 mg, 225 ng/mL (95% CI, 192-257) for 15 mg, and 229 ng/mL (95% CI, 193-264) for 20 mg, with trough concentrations of 23 ng/mL (95% CI, 13-32), 31 ng/mL (95% CI, 26-36), and 36 ng/mL (95% CI, 25-47), respectively. Meta-regression revealed age and creatinine clearance correlated with apixaban peak concentrations. Creatinine clearance correlated with apixaban and rivaroxaban trough concentrations.</div></div><div><h3>Conclusion</h3><div>The pooled mean concentrations align with expected concentration ranges reported in different pharmacokinetic studies.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1289-1314"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142971441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A mutant complement factor H (W1183R) enhances proteolytic cleavage of von Willebrand factor by ADAMTS-13 under shear","authors":"Wenjing Cao ,&nbsp;Yi Liu ,&nbsp;X. Frank Zhang ,&nbsp;X. Long Zheng","doi":"10.1016/j.jtha.2024.11.031","DOIUrl":"10.1016/j.jtha.2024.11.031","url":null,"abstract":"<div><h3>Background</h3><div>A loss-of-functional mutation (W1183R) in human complement factor H (CFH) is associated with complement-associated hemolytic uremic syndrome; mice carrying a similar mutation (W1206R) in CFH also develop thrombotic microangiopathy but its plasma von Willebrand factor (VWF) multimer sizes were dramatically reduced. The mechanism underlying such a dramatic change in plasma VWF multimer distribution in these mice is not fully understood.</div></div><div><h3>Objectives</h3><div>To determine the VWF and CFH interaction and how CFH proteins affect VWF multimer distribution.</div></div><div><h3>Methods</h3><div>We employed recombinant protein expression, purification, and various biochemical and biophysical tools.</div></div><div><h3>Results</h3><div>Purified recombinant W1183R-CFH but not wild-type (WT) CFH protein enhanced the proteolytic cleavage of both peptidyl and multimeric VWF substrates by recombinant ADAMTS-13 in a concentration-dependent manner. Microscale thermophoresis assay demonstrated that both W1183R-CFH and WT-CFH proteins bound various VWF fragments (eg, AIM-A1, A1-A2-A3, D’D3, D’D3-A1, and D’D3-A1-A2) with high affinities. Optical tweezer experiments further showed a concentration-dependent alteration in the contour length (L_c) and the persistent length (L_p) following pulling VWF-A2 domain in the presence of W1183R-CFH or WT-CFH protein. AlphaFold experiments revealed conformational changes in the VWF-A2, particularly the central region where the cleavage bond resides following addition of W1183R-CFH or WT-CFH protein.</div></div><div><h3>Conclusion</h3><div>These results demonstrate for the first time that W1183R-CFH but not WT-CFH protein enhances the proteolytic cleavage of VWF by ADAMTS-13 under shear. This may be achieved by mechanic-induced conformational changes of the central A2 domain, leading to an enhanced cleavage of Tyr¹⁶⁰⁵-Met¹⁶⁰⁶ bond by ADAMTS-13 under pathophysiological conditions.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1229-1240"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142971360","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to ‘FRONTIER1: a partially randomized phase 2 study assessing the safety, pharmacokinetics, and pharmacodynamics of Mim8, a factor VIIIa mimetic’","authors":"Steven R. Lentz ,&nbsp;Pratima Chowdary ,&nbsp;Lidia Gil ,&nbsp;Francisco J. Lopez-Jaime ,&nbsp;Johnny Mahlangu ,&nbsp;Irina Matytsina ,&nbsp;Anne Louise Nielsen ,&nbsp;Jerzy Windyga","doi":"10.1016/j.jtha.2025.02.008","DOIUrl":"10.1016/j.jtha.2025.02.008","url":null,"abstract":"","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1456-1457"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143472661","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Therapeutic potential of roxadustat in immune thrombocytopenia: a Mendelian randomization analysis","authors":"Jingyao Ma ,&nbsp;Yu Hu ,&nbsp;Shuyue Dong ,&nbsp;Jinxi Meng ,&nbsp;Zhifa Wang ,&nbsp;Juntao Ouyang ,&nbsp;Zheyan Lin ,&nbsp;Xiaoling Cheng ,&nbsp;Zhenping Chen ,&nbsp;Runhui Wu","doi":"10.1016/j.jtha.2024.12.028","DOIUrl":"10.1016/j.jtha.2024.12.028","url":null,"abstract":"<div><h3>Background</h3><div>Immune thrombocytopenia (ITP) is characterized by immune-mediated platelet destruction and impaired megakaryocyte maturation. Hypoxia-inducible factor-1α (HIF-1α), pivotal in the development of megakaryocytes and immune regulation, is downregulated in ITP. Roxadustat, which stabilizes HIF-1α, has emerged as a potential therapeutic drug for ITP that acts by enhancing HIF-1α–mediated megakaryocyte development and modulating immune responses.</div></div><div><h3>Objectives</h3><div>This study evaluates the safety profile of roxadustat and its therapeutic efficacy for ITP treatment using Mendelian randomization (MR) analysis.</div></div><div><h3>Methods</h3><div>We used expression quantitative trait loci data for roxadustat’s target genes (<em>EGLN1</em>, <em>EGLN2</em>, and <em>EGLN3</em>) and genetic associations with ITP and adverse outcomes from the Open Genome-Wide Association Study project. MR analysis included inverse-variance weighted, MR-Egger regression, weighted median, and MR pleiotropy residual sum and outlier methods to evaluate pleiotropy. Heterogeneity was assessed using Cochran’s Q statistic and I² measure with sensitivity analyses. A meta-analysis was performed to integrate effect sizes from multiple literature sources.</div></div><div><h3>Results</h3><div>MR analysis revealed a significant association between roxadustat and reduced ITP risk (odds ratio, 0.79; 95% CI, 0.66-0.95; <em>P =</em> .01) with no evidence of horizontal pleiotropy. Meta-analysis confirmed the protective effect of roxadustat on ITP. Utilizing the expression quantitative trait loci of roxadustat’s target gene <em>EGLN1</em> as instrumental variables, an MR analysis of 39 potential adverse reactions revealed no significant increase, suggesting a favorable safety profile for roxadustat.</div></div><div><h3>Conclusion</h3><div>Roxadustat demonstrates a potential protective effect against ITP without increasing the risk of adverse outcomes, suggesting its promise as a therapeutic option for ITP and warranting further investigation.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1442-1451"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142932195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"New targets for antithrombotic medications: seeking to decouple thrombosis from hemostasis","authors":"Geoffrey D. Barnes","doi":"10.1016/j.jtha.2024.12.003","DOIUrl":"10.1016/j.jtha.2024.12.003","url":null,"abstract":"<div><div>Arterial and venous thromboses are the leading causes of morbidity and mortality worldwide. Numerous antithrombotic agents are currently available with antiplatelet, thrombolytic/fibrinolytic, and anticoagulant activity. However, all the currently available antithrombotic agents carry a risk of bleeding that often prevents their use. This unfavorable risk-benefit profile is particularly challenging for patients with cancer-associated venous thromboembolism, patients with atrial fibrillation at a high risk of bleeding, and patients with end-stage renal disease. Patients with ischemic stroke and acute coronary syndromes have not yet found a favorable risk-benefit profile with anticoagulant therapy to help reduce the residual thromboembolic risk that remains after antiplatelet and lipid therapy. Two emerging classes of antithrombotic agents, factor (F)XI or activated factor Ⅺ (FⅪa) inhibitors and glycoprotein VI inhibitors, have shown promise in their ability to prevent pathologic thrombosis without increasing the risk of hemostatic-related bleeding in phase 2 studies. Among the FⅪ/FXIa inhibitors of coagulation, a parenterally administered monoclonal antibody (abelacimab) and 2 orally administered small molecule inhibitors (asundexian, milvexian) are collectively being studied in patients with atrial fibrillation, cancer-associated venous thromboembolism, acute coronary syndrome, and ischemic stroke. One parenterally administered glycoprotein VI antiplatelet agent (glenzocimab) is currently being studied in patients with ischemic stroke. If shown to be efficacious and safe in ongoing phase 3 studies, both classes of emerging antithrombotic agents have the potential to greatly improve outcomes for patients with challenging thrombotic conditions.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1146-1159"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142829154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Thrombin reveals new faces with a tiny trick","authors":"Raimondo De Cristofaro","doi":"10.1016/j.jtha.2025.01.001","DOIUrl":"10.1016/j.jtha.2025.01.001","url":null,"abstract":"","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1203-1204"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143767905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure-resolved dynamics of type 2M von Willebrand disease","authors":"Alexander Tischer,&nbsp;Laurie Moon-Tasson,&nbsp;Matthew Auton","doi":"10.1016/j.jtha.2024.12.026","DOIUrl":"10.1016/j.jtha.2024.12.026","url":null,"abstract":"<div><h3>Background</h3><div>Genetically determined amino acid substitutions in the platelet adhesive A1 domain alter von Willebrand factor’s (VWF) platelet agglutination competence, resulting in both gain- (type 2B) and loss-of-function (type 2M) phenotypes of von Willebrand disease. Prior studies of variants in both phenotypes revealed defects in secondary structure that altered stability and folding of the domain. An intriguing observation was that loss of function arose from both misfolding of A1 and, in a few cases, hyperstabilization of the native structure.</div></div><div><h3>Objectives</h3><div>To fully understand the 2M phenotype, we thoroughly investigated the structure/function relationships of 15 additional type 2M variants and 2 polymorphisms in the A1 domain.</div></div><div><h3>Methods</h3><div>These variants were characterized using circular dichroism, fluorescence, calorimetry, hydrogen-deuterium exchange mass spectrometry, surface plasmon resonance, and platelet adhesion under shear flow.</div></div><div><h3>Results</h3><div>Six variants were natively folded, with 4 being hyperstabilized. Nine variants disordered A1, causing a loss in α-helical structure and unfolding enthalpy. GPIbα binding affinity and platelet adhesion dynamics were highly correlated to helical structure. Hydrogen-deuterium exchange resolved specific C-terminal secondary structure elements that differentially diminish the GPIbα binding affinity of A1. These localized structural perturbations were highly correlated to GPIbα binding affinity and shear-dependent platelet adhesion.</div></div><div><h3>Conclusion</h3><div>While hyperstabilized dynamics in A1 do impair stable platelet attachment to VWF under flow, variant-induced localized disorder in specific regions of the domain misfolds A1 and abrogates platelet adhesion. These 2 opposing conformational properties represent 2 structural classes of VWF that drive the loss-of-function phenotype that is type 2M von Willebrand disease.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1215-1228"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142932193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Description of the clinical and radiological characteristics of pulmonary embolism in COVID-19 vs non–COVID-19 patients: a multicentric cross-sectional study over a 24-month perspective","authors":"Paola Sterpone ,&nbsp;Marco Paolo Donadini ,&nbsp;Irene Abatangelo ,&nbsp;Laura Tofanelli ,&nbsp;Asim Raza ,&nbsp;Filippo Piacentino ,&nbsp;Francesco Maria Vitale ,&nbsp;Francesco Ricapito ,&nbsp;Massimo Venturini ,&nbsp;Walter Ageno ,&nbsp;Francesco Pavesi ,&nbsp;Emilia Antonucci ,&nbsp;Maurizio Cariati ,&nbsp;Gian Marco Podda ,&nbsp;Simone Birocchi","doi":"10.1016/j.jtha.2024.12.037","DOIUrl":"10.1016/j.jtha.2024.12.037","url":null,"abstract":"<div><h3>Background</h3><div>COVID-19 is associated with intense systemic inflammation and abnormal coagulation profile, leading to an increased incidence of pulmonary embolism (PE).</div></div><div><h3>Objectives</h3><div>This study investigates whether PE in COVID-19 patients has different clinical, laboratory, and radiological characteristics compared with traditional PE in COVID-19–negative patients.</div></div><div><h3>Methods</h3><div>We conducted an observational, multicentric, cross-sectional study on consecutive patients diagnosed with PE at admission or during hospital stay from February 21, 2019, to February 20, 2021. We compared clinical and laboratory data and computed tomography images between COVID-19–positive and COVID-19–negative patients. The extent of PE was evaluated using the Qanadli Index.</div></div><div><h3>Results</h3><div>Among 771 enrolled patients with acute PE, 89 were COVID-19–positive. COVID-19 patients were predominantly male (59.6% vs 41.5%, <em>P</em> = .001) and exhibited fewer classic venous thromboembolism (VTE) risk factors, such as previous VTE (3.5% vs 11.5%, <em>P</em> = .02) and active cancer (4.7% vs 24.2%, <em>P</em> &lt; .0001). Additionally, these patients showed lower median troponin T and pro-B-type-natriuretic-peptide levels (10 vs 32 ng/L, <em>P</em> = .0002; and 383 vs 1448 pg/mL, <em>P</em> = .004, respectively), a lower median Qanadli Index (4 vs 7, <em>P</em> = .0013), more distal PE obstructions (53.5% vs 32.9%, <em>P</em> &lt; .001), and less frequent right ventricular dilatation (4.1% vs 10.9%, <em>P</em> = .09).</div></div><div><h3>Conclusion</h3><div>In COVID-19 patients, traditional VTE risk factors were less frequent, a possible role for <em>in situ</em> thrombo-inflammatory processes. The reduced radiological extent and severity of PE observed in COVID-19 patients may reflect an <em>in situ</em> thrombo-inflammatory process rather than classical embolization; however, this hypothesis needs to be confirmed by other studies.</div></div>","PeriodicalId":17326,"journal":{"name":"Journal of Thrombosis and Haemostasis","volume":"23 4","pages":"Pages 1332-1339"},"PeriodicalIF":5.5,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142971433","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}