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CC BY 4.0 · TH Open 2026; 10: a27777484
DOI: 10.1055/a-2777-7484
Original Article

Differences and Compatibility between Human and Porcine Fibrinolytic Components toward Plasmin Generation and Fibrin Degradation

Authors

  • Paul Y. Kim 

    1   Thrombosis and Atherosclerosis Research Institute, Hamilton, Canada
    2   Department of Medicine, McMaster University, Hamilton, Canada

  • Chengliang Wu

    1   Thrombosis and Atherosclerosis Research Institute, Hamilton, Canada
    2   Department of Medicine, McMaster University, Hamilton, Canada

  • Hena Noorzada

    1   Thrombosis and Atherosclerosis Research Institute, Hamilton, Canada
    3   Department of Medical Sciences, McMaster University, Hamilton, Canada

  • Ali Aftabjahani

    1   Thrombosis and Atherosclerosis Research Institute, Hamilton, Canada
    3   Department of Medical Sciences, McMaster University, Hamilton, Canada

Funding Information P.Y.K. is supported by the Department of Medicine Career Award (McMaster University). A.A. is supported by the CanVECTOR Studentship Award.
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Graphical Abstract

Abstract

Background

Fibrinolysis is the process of blood clot breakdown by the enzyme plasmin. Despite increased usage of large animals such as pigs to study fibrinolysis in human disease models, a comprehensive study comparing the human and porcine fibrinolytic factors has not been reported.

Objective

To directly compare and characterize structural and functional differences between human and porcine fibrinolytic factors.

Methods

Using human or porcine source of plasminogen, tissue-type plasminogen activator (tPA), and fibrinogen, we investigated how various permutations of the three fibrinolytic factors affect overall plasmin generation. Human or porcine plasmin breakdown of fibrin generated from human or porcine fibrinogen was also investigated using turbidity-based lysis assay and visualized using SDS-PAGE. Primary structures of the various proteins were also compared.

Results

All-human components had a 24-fold higher plasmin generation than all-porcine components. Species dependence on plasmin generation was the most dependent on fibrin source, where human fibrin presence led to a 2- to 34-fold higher plasmin generation than porcine fibrin. Porcine plasmin was the better enzyme for human or porcine fibrin breakdown due to a 2.7-fold and 6.7-fold higher kcat, respectively. Peptide sequence analyses show the greatest differences lie in Kringle domain 1 for plasminogen and Kringle domain 2 for tPA, both of which bind fibrin. Fibrinogen chains also show the greatest difference within the αC domain, which has known plasminogen and tPA binding sites.

Conclusion

Although similar, there are notable and specific differences between the human and porcine fibrinolytic systems, particularly toward plasmin generation and fibrin breakdown.

Keywords

swine - fibrinolysis - plasminogen - plasminogen activators - proteolysis

Contributors' Statement

P.Y.K.: conceptualization, funding acquisition, investigation, project administration, supervision, writing—original draft, writing—review and editing; C.W.: data curation, formal analysis, investigation, writing—review and editing; H.N.: data curation, formal analysis, writing—review and editing; A.A.: data curation, formal analysis, investigation, writing—review and editing.


Supplementary Material



Publication History

Received: 12 September 2025

Accepted: 22 December 2025

Accepted Manuscript online:
23 December 2025

Article published online:
09 January 2026

© 2026. The Author(s). This is an open access article published by Thieme under the terms of the Creative Commons Attribution License, permitting unrestricted use, distribution, and reproduction so long as the original work is properly cited. (https://creativecommons.org/licenses/by/4.0/)

Georg Thieme Verlag KG
Oswald-Hesse-Straße 50, 70469 Stuttgart, Germany

Bibliographical Record
Paul Y. Kim, Chengliang Wu, Hena Noorzada, Ali Aftabjahani. Differences and Compatibility between Human and Porcine Fibrinolytic Components toward Plasmin Generation and Fibrin Degradation. TH Open 2026; 10: a27777484.
DOI: 10.1055/a-2777-7484
 

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