Surface-bound FXIII enhances deposition and straightness of fibrin fibers
Cross-linked fibrous networks are central to maintaining the structural integrity and functional relevance of many biological and engineered materials. Fibrin networks are the building blocks of blood clots, mediators of tissue injury and repair, and synthetic wound sealants. Cross-linking of fibrin...
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-06-01
|
| Series: | Biophysical Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667074725000126 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849733750778232832 |
|---|---|
| author | Myra Awan Maya Papez Ankita P. Walvekar Sang-Joon J. Lee Kinjal Dasbiswas Anand K. Ramasubramanian |
| author_facet | Myra Awan Maya Papez Ankita P. Walvekar Sang-Joon J. Lee Kinjal Dasbiswas Anand K. Ramasubramanian |
| author_sort | Myra Awan |
| collection | DOAJ |
| description | Cross-linked fibrous networks are central to maintaining the structural integrity and functional relevance of many biological and engineered materials. Fibrin networks are the building blocks of blood clots, mediators of tissue injury and repair, and synthetic wound sealants. Cross-linking of fibrin fibers is catalyzed by the activated form of transglutaminase enzyme FXIIIa, which becomes available in plasma but is also readily presented on the surface of activated platelets and macrophages. The contribution of surface-bound FXIIIa to fibrin structure has not been well understood. In this work, we investigated the role of surface-bound FXIIIa on the formation and structure of fibrin fibers from FXIII-deficient plasma by confining the cross-linking reactions to the surface of microspheres. Quantitative microscopy revealed that cross-linking on FXIIIa-coated surfaces facilitates fibrin deposition following a sigmoidal kinetics, and that these fibers were straighter, longer, and more numerous compared with uncross-linked fibers bound to surfaces coated with anti-fibrin antibody. Our results suggest that, by modifying local fibrin density and structure, surface-bound FXIIIa may play a significant role in the mechanobiology of hemostasis and inflammation. |
| format | Article |
| id | doaj-art-2c92fef4f7c8469693a8958fd7f530a8 |
| institution | DOAJ |
| issn | 2667-0747 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biophysical Reports |
| spelling | doaj-art-2c92fef4f7c8469693a8958fd7f530a82025-08-20T03:07:58ZengElsevierBiophysical Reports2667-07472025-06-015210020710.1016/j.bpr.2025.100207Surface-bound FXIII enhances deposition and straightness of fibrin fibersMyra Awan0Maya Papez1Ankita P. Walvekar2Sang-Joon J. Lee3Kinjal Dasbiswas4Anand K. Ramasubramanian5Department of Chemical and Materials Engineering, San José State University, San José, CaliforniaDepartment of Chemical and Materials Engineering, San José State University, San José, CaliforniaDepartment of Chemical and Materials Engineering, San José State University, San José, CaliforniaDepartment of Mechanical Engineering, San José State University, San José, CaliforniaDepartment of Physics, University of California, Merced, Merced, CaliforniaDepartment of Chemical and Materials Engineering, San José State University, San José, California; Corresponding authorCross-linked fibrous networks are central to maintaining the structural integrity and functional relevance of many biological and engineered materials. Fibrin networks are the building blocks of blood clots, mediators of tissue injury and repair, and synthetic wound sealants. Cross-linking of fibrin fibers is catalyzed by the activated form of transglutaminase enzyme FXIIIa, which becomes available in plasma but is also readily presented on the surface of activated platelets and macrophages. The contribution of surface-bound FXIIIa to fibrin structure has not been well understood. In this work, we investigated the role of surface-bound FXIIIa on the formation and structure of fibrin fibers from FXIII-deficient plasma by confining the cross-linking reactions to the surface of microspheres. Quantitative microscopy revealed that cross-linking on FXIIIa-coated surfaces facilitates fibrin deposition following a sigmoidal kinetics, and that these fibers were straighter, longer, and more numerous compared with uncross-linked fibers bound to surfaces coated with anti-fibrin antibody. Our results suggest that, by modifying local fibrin density and structure, surface-bound FXIIIa may play a significant role in the mechanobiology of hemostasis and inflammation.http://www.sciencedirect.com/science/article/pii/S2667074725000126 |
| spellingShingle | Myra Awan Maya Papez Ankita P. Walvekar Sang-Joon J. Lee Kinjal Dasbiswas Anand K. Ramasubramanian Surface-bound FXIII enhances deposition and straightness of fibrin fibers Biophysical Reports |
| title | Surface-bound FXIII enhances deposition and straightness of fibrin fibers |
| title_full | Surface-bound FXIII enhances deposition and straightness of fibrin fibers |
| title_fullStr | Surface-bound FXIII enhances deposition and straightness of fibrin fibers |
| title_full_unstemmed | Surface-bound FXIII enhances deposition and straightness of fibrin fibers |
| title_short | Surface-bound FXIII enhances deposition and straightness of fibrin fibers |
| title_sort | surface bound fxiii enhances deposition and straightness of fibrin fibers |
| url | http://www.sciencedirect.com/science/article/pii/S2667074725000126 |
| work_keys_str_mv | AT myraawan surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers AT mayapapez surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers AT ankitapwalvekar surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers AT sangjoonjlee surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers AT kinjaldasbiswas surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers AT anandkramasubramanian surfaceboundfxiiienhancesdepositionandstraightnessoffibrinfibers |