The myofibroblast in wound healing and fibrocontractive diseases
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- 1 July 2003
- journal article
- review article
- Published by Wiley in The Journal of Pathology
- Vol. 200 (4) , 500-503
- https://doi.org/10.1002/path.1427
Abstract
The demonstration that fibroblastic cells acquire contractile features during the healing of an open wound, thus modulating into myofibroblasts, has open a new perspective in the understanding of mechanisms leading to wound closure and fibrocontractive diseases. Myofibroblasts synthesize extracellular matrix components such as collagen types I and III and during normal wound healing disappear by apoptosis when epithelialization occurs. The transition from fibroblasts to myofibroblasts is influenced by mechanical stress, TGF‐β and cellular fibronectin (ED‐A splice variant). These factors also play important roles in the development of fibrocontractive changes, such as those observed in liver cirrhosis, renal fibrosis, and stroma reaction to epithelial tumours. Copyright © 2003 John Wiley & Sons, Ltd.Keywords
This publication has 17 references indexed in Scilit:
- The NH2-terminal peptide of α–smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivoThe Journal of cell biology, 2002
- Myofibroblasts and mechano-regulation of connective tissue remodellingNature Reviews Molecular Cell Biology, 2002
- Cooperative Role for Activated α4β1 Integrin and Chondroitin Sulfate Proteoglycans in Cell Adhesion to the Heparin III Domain of FibronectinPublished by Elsevier ,1999
- Activation of Distinct α5β1-mediated Signaling Pathways by Fibronectin's Cell Adhesion and Matrix Assembly DomainsThe Journal of cell biology, 1998
- Fibronectin Type III Repeats Mediate RGD-independent Adhesion and Signaling through Activated β1 IntegrinsJournal of Biological Chemistry, 1997
- Fibronectin Type III5 Repeat Contains a Novel Cell Adhesion Sequence, KLDAPT, Which Binds Activated α4β1 and α4β7 IntegrinsJournal of Biological Chemistry, 1997
- The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo.The Journal of cell biology, 1995
- Transforming growth factor-beta 1 induces alpha-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblastsThe Journal of cell biology, 1993
- Transforming growth factor‐β regulates the splicing pattern of fibronectin messenger RNA precursorFEBS Letters, 1990
- A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation.The Journal of cell biology, 1986