Decorin Effect on Hemostasis: What Is New? | ||||
| The Egyptian Journal of Hospital Medicine | ||||
| Article 147, Volume 90, Issue 2, January 2023, Page 2967-2969 PDF (324.26 K) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/ejhm.2023.287852 | ||||
 View on SCiNiTO | ||||
| Authors | ||||
Abeer Albiomy Khalifa; Reham Hassan ELazony; Malak Musa AL-Klbash  ; Shaimaa El-Ssayed Hadhoud
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| Abstract | ||||
| There is growing evidence that many environmental factors control how fibrin clots. Fibrinogen's D regions are bound by decorin and regulates the action of transforming growth factor and collagen fibrillogenesis. The construction, structure, and clearance of fibrin fibres are modified by the interaction between decorin and fibrinogen. Compared to fibrinogen, decorin core protein-controlled clotting in substoichiometric levels, however, for a comparable impact, the active decorin peptide needed to be in excess. These concentration-dependent outcomes suggest that decorin binds to the D regions to sterically influence fibrin synthesis. Images of fibrin that has clot in the presence of increasing amounts of the decorin core protein taken using scanning electron microscopy indicated successively decreased fibre diameter. The budget cuts of Zn2+ ions from the fibrinogen-binding domain at the N-terminus prevented decorin from integrating into the fibrin network. The decorin-formed curving thin fibres underwent quicker plasminogen activator-dependent fibrinolysis of the tissue-type as opposed to the linear bulkier fibrin fibres. Together, our findings show that decorin can control fibrin organisation and provide new insight into how extracellular matrix elements might affect hemostasis, thrombosis, and wound healing. | ||||
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