{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:36:04Z","timestamp":1760060164106,"version":"build-2065373602"},"reference-count":38,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2025,8,5]],"date-time":"2025-08-05T00:00:00Z","timestamp":1754352000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Research, Development and Innovation Office (NKFIH)","award":["K120633","K139293","DETKA","LP2024-1\/2024"],"award-info":[{"award-number":["K120633","K139293","DETKA","LP2024-1\/2024"]}]},{"name":"University of Debrecen Scientific Research Bridging Fund","award":["K120633","K139293","DETKA","LP2024-1\/2024"],"award-info":[{"award-number":["K120633","K139293","DETKA","LP2024-1\/2024"]}]},{"name":"Hungarian Academy of Sciences","award":["K120633","K139293","DETKA","LP2024-1\/2024"],"award-info":[{"award-number":["K120633","K139293","DETKA","LP2024-1\/2024"]}]},{"name":"University of Debrecen","award":["K120633","K139293","DETKA","LP2024-1\/2024"],"award-info":[{"award-number":["K120633","K139293","DETKA","LP2024-1\/2024"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Alpha2-plasmin inhibitor (\u03b12PI) has a heterogeneous structure due to proteolytic cleavages in the circulation. The C-terminally cleaved form loses the plasminogen binding site and is, therefore, a slow plasmin inhibitor (NPB-\u03b12PI). As FXIII primarily crosslinks the plasminogen-binding intact form (PB-\u03b12PI) to fibrin, the effect of NPB-\u03b12PI on fibrinolysis has been less studied. Herein, we investigated the effect of C-terminal truncation. Total-, PB-, and NPB-\u03b12PI antigen levels and \u03b12PI incorporation were measured by ELISAs from samples of 80 healthy individuals. Clot lysis parameters of the same subjects were investigated using an in vitro clot lysis assay. \u03b12PI incorporation into the clot was demonstrated by Western blotting. Clot lysis and clot structure were also analyzed using an \u03b12PI-deficient plasma substituted with recombinant PB- and NPB-\u03b12PI. Both plasma and clot-bound levels of total- and NPB-\u03b12PI showed a significant positive correlation with clot lysis parameters. NPB-\u03b12PI was detected in the clot due to non-covalent binding. Regardless of the type of binding, both forms affected the clot structure by increasing the thickness of the fibrin fibers and reducing the pore size. In conclusion, we found that NPB-\u03b12PI can bind non-covalently to fibrin, and this binding contributes to changes in clot structure and inhibition of fibrinolysis.<\/jats:p>","DOI":"10.3390\/biom15081127","type":"journal-article","created":{"date-parts":[[2025,8,5]],"date-time":"2025-08-05T08:46:55Z","timestamp":1754383615000},"page":"1127","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Effect of Alpha2-Plasmin Inhibitor C-Terminal Heterogeneity on Clot Lysis and Clot Structure"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-7628-9426","authenticated-orcid":false,"given":"R\u00e9ka","family":"Bog\u00e1ti","sequence":"first","affiliation":[{"name":"Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"},{"name":"K\u00e1lm\u00e1n Laki Doctoral School, University of Debrecen, 4032 Debrecen, Hungary"}]},{"given":"Barbara","family":"Bar\u00e1th","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Semmelweis University, 1094 Budapest, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7481-6921","authenticated-orcid":false,"given":"D\u00f3ra","family":"Pituk","sequence":"additional","affiliation":[{"name":"Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"},{"name":"K\u00e1lm\u00e1n Laki Doctoral School, University of Debrecen, 4032 Debrecen, Hungary"}]},{"given":"Rita","family":"Orb\u00e1n-K\u00e1lm\u00e1ndi","sequence":"additional","affiliation":[{"name":"Healthcare Industry Institute, Faculty of Pharmacy, University of Debrecen, 4032 Debrecen, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4635-6427","authenticated-orcid":false,"given":"P\u00e9ter","family":"Sz\u0171cs","sequence":"additional","affiliation":[{"name":"Department of Anatomy, Histology and Embryology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5005-3333","authenticated-orcid":false,"given":"Zolt\u00e1n","family":"Hegyi","sequence":"additional","affiliation":[{"name":"Department of Anatomy, Histology and Embryology, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1483-3703","authenticated-orcid":false,"given":"Zsuzsanna","family":"Bereczky","sequence":"additional","affiliation":[{"name":"Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5314-5607","authenticated-orcid":false,"given":"Zsuzsa","family":"Bagoly","sequence":"additional","affiliation":[{"name":"Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"},{"name":"MTA-DE Lend\u00fclet \u201cMomentum\u201d Hemostasis and Stroke Research Group, 4032 Debrecen, Hungary"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3476-794X","authenticated-orcid":false,"given":"\u00c9va","family":"Katona","sequence":"additional","affiliation":[{"name":"Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary"}]}],"member":"1968","published-online":{"date-parts":[[2025,8,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1055\/s-2007-1002671","article-title":"The fibrinolytic enzyme system and its role in the etiology of thromboembolic disease","volume":"16","author":"Wiman","year":"1990","journal-title":"Semin. 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