| The molecular origins of the mechanical properties of fibrin. | |
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MedLine Citation:
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PMID: 20888119 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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When normal blood circulation is compromised by damage to vessel walls, clots are formed at the site of injury. These clots prevent bleeding and support wound healing. To sustain such physiological functions, clots are remarkably extensible and elastic. Fibrin fibers provide the supporting framework of blood clots, and the properties of these fibers underlie the mechanical properties of clots. Recent studies, which examined individual fibrin fibers or cylindrical fibrin clots, have shown that the mechanical properties of fibrin depend on the mechanical properties of the individual fibrin monomers. Within the fibrin monomer, three structures could contribute to these properties: the coiled-coil connectors the folded globular nodules and the relatively unstructured αC regions. Experimental data suggest that each of these structures contributes. Here we review the recent work with a focus on the molecular origins of the remarkable biomechanical properties of fibrin clots. |
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Authors:
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Michael R Falvo; Oleg V Gorkun; Susan T Lord |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review |
Journal Detail:
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Title: Biophysical chemistry Volume: 152 ISSN: 1873-4200 ISO Abbreviation: Biophys. Chem. Publication Date: 2010 Nov |
Date Detail:
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Created Date: 2010-11-08 Completed Date: 2011-02-22 Revised Date: 2011-11-01 |
Medline Journal Info:
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Nlm Unique ID: 0403171 Medline TA: Biophys Chem Country: Netherlands |
Other Details:
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Languages: eng Pagination: 15-20 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Physics and Astronomy, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Fibrin
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chemistry*,
physiology Fibrinogen / chemistry Humans Protein Structure, Tertiary Stress, Mechanical |
| Grant Support | |
ID/Acronym/Agency:
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HL031508/HL/NHLBI NIH HHS; P41-EB002025/EB/NIBIB NIH HHS |
| Chemical | |
Reg. No./Substance:
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9001-31-4/Fibrin; 9001-32-5/Fibrinogen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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