{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T12:38:15Z","timestamp":1785155895397,"version":"3.55.0"},"reference-count":56,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T00:00:00Z","timestamp":1779753600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>Tranexamic acid (TXA) is a synthetic lysine analog that inhibits fibrinolysis by blocking lysine-binding sites on plasminogen and plasmin. Although early therapeutic TXA reduces bleeding mortality in major trials, prophylactic benefit appears context- and timing-dependent. TXA is generally not associated with increased thromboembolism, yet its net effect on thrombus formation remains uncertain. Because plasmin(ogen) also acts on leukocytes, endothelium and platelets via cell-surface receptors, TXA may exert cell-dependent effects beyond antifibrinolysis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objectives<\/jats:title>\n                    <jats:p>To determine how cellular elements modulate TXA\u2019s impact on thrombus formation.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      We studied TXA in an\n                      <jats:italic>in vivo<\/jats:italic>\n                      murine venous thrombosis model without endothelial injury (IVC stenosis). Plasma VWF: Ag and MCP-1 were measured by ELISA. Thrombin generation was assessed in whole blood and plasma-based systems to evaluate cell dependence. Leukocyte-associated plasminogen activation was quantified using plasmin generation assays in fibrin. Primary hemostasis was assessed by tail bleeding.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>TXA reduced the odds of venous thrombus formation by 90% but did not alter thrombus mass once clots formed. VWF: Ag remained unchanged, whereas the stenosis-induced rise in MCP-1 was largely suppressed by TXA. TXA decreased thrombin generation in whole blood but not in platelet-rich plasma, indicating a cellular requirement. Consistently, TXA markedly inhibited leukocyte surface\u2013mediated plasminogen activation within fibrin clots. Tail bleeding was unaffected.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>TXA was not prothrombotic in venous stasis; it reduced thrombus initiation without impairing primary hemostasis. We show for the first time that TXA modulates thrombin generation in a cellular environment, consistent with inhibition of leukocyte-associated plasmin activity.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fimmu.2026.1820813","type":"journal-article","created":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T04:49:55Z","timestamp":1779770995000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":1,"title":["Cell-dependent antithrombotic effect of tranexamic acid"],"prefix":"10.3389","volume":"17","author":[{"given":"Kata","family":"Balog Vir\u00e1g","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University","place":["Budapest, Hungary"]},{"name":"HCEMM-SU Thrombosis and Hemostasis Research Group, Department of Biochemistry, Semmelweis University","place":["Budapest, 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