Document Detail


Fibrin structure and wound healing.
MedLine Citation:
PMID:  16689737     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fibrinogen and fibrin play an important role in blood clotting, fibrinolysis, cellular and matrix interactions, inflammation, wound healing, angiogenesis, and neoplasia. The contribution of fibrin(ogen) to these processes largely depends not only on the characteristics of the fibrin(ogen) itself, but also on interactions between specific-binding sites on fibrin(ogen), pro-enzymes, clotting factors, enzyme inhibitors, and cell receptors. In this review, the molecular and cellular biology of fibrin(ogen) is reviewed in the context of cutaneous wound repair. The outcome of wound healing depends largely on the fibrin structure, such as the thickness of the fibers, the number of branch points, the porosity, and the permeability. The binding of fibrin(ogen) to hemostasis proteins and platelets as well as to several different cells such as endothelial cells, smooth muscle cells, fibroblasts, leukocytes, and keratinocytes is indispensable during the process of wound repair. High-molecular-weight and low-molecular-weight fibrinogen, two naturally occurring variants of fibrin, are important determinants of angiogenesis and differ in their cell growth stimulation, clotting rate, and fibrin polymerization characteristics. Fibrin sealants have been investigated as matrices to promote wound healing. These sealants may also be an ideal delivery vehicle to deliver extra cells for the treatment of chronic wounds.
Authors:
N Laurens; P Koolwijk; M P M de Maat
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Journal of thrombosis and haemostasis : JTH     Volume:  4     ISSN:  1538-7933     ISO Abbreviation:  J. Thromb. Haemost.     Publication Date:  2006 May 
Date Detail:
Created Date:  2006-05-12     Completed Date:  2006-07-31     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101170508     Medline TA:  J Thromb Haemost     Country:  England    
Other Details:
Languages:  eng     Pagination:  932-9     Citation Subset:  IM    
Affiliation:
Department of Biomedical Research, TNO-Quality of Life, Gaubius Laboratory, Leiden, the Netherlands.
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MeSH Terms
Descriptor/Qualifier:
Fibrin / chemistry*,  metabolism,  physiology
Fibrinogen / chemistry,  metabolism
Humans
Neovascularization, Physiologic
Protein Conformation
Proteins / metabolism
Wound Healing / physiology*
Chemical
Reg. No./Substance:
0/Proteins; 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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