Fibronectin matrix polymerization increases tensile strength of model tissue

1 Department of Biomedical Engineering and 2 Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, New York 14642 Submitted 10 September 2003 ; accepted in final form 26 February 2004 The composition and organization of the extracellular matrix (ECM) contribut...

Full description

Saved in:
Bibliographic Details
Published in:American journal of physiology. Heart and circulatory physiology 2004-07, Vol.287 (1), p.H46-H53
Main Authors: Gildner, Candace D, Lerner, Amy L, Hocking, Denise C
Format: Article
Language:English
Subjects:
Actins - physiology
Animals
Cells, Cultured
Collagen - chemistry
Cytoskeleton - physiology
Extracellular Matrix - metabolism
Fibroblasts - metabolism
Fibronectins - metabolism
Fibronectins - pharmacology
Gels
Mice
Muscle, Smooth - cytology
Muscle, Smooth - metabolism
Peptide Fragments - pharmacology
Polymers - metabolism
Tensile Strength
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:1 Department of Biomedical Engineering and 2 Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, New York 14642 Submitted 10 September 2003 ; accepted in final form 26 February 2004 The composition and organization of the extracellular matrix (ECM) contribute to the mechanical properties of tissues. The polymerization of fibronectin into the ECM increases actin organization and regulates the composition of the ECM. In this study, we examined the ability of cell-dependent fibronectin matrix polymerization to affect the tensile properties of an established tissue model. Our data indicate that fibronectin polymerization increases the ultimate strength and toughness, but not the stiffness, of collagen biogels. A fragment of fibronectin that stimulates mechanical tension generation by cells, but is not incorporated into ECM fibrils, did not increase the tensile properties, suggesting that changes in actin organization in the absence of fibronectin fibril formation are not sufficient to increase tensile strength. The actin cytoskeleton was needed to initiate the fibronectin-induced increases in the mechanical properties. However, once fibronectin-treated collagen biogels were fully contracted, the actin cytoskeleton no longer contributed to the tensile strength. These data indicate that fibronectin polymerization plays a significant role in determining the mechanical strength of collagen biogels and suggest a novel mechanism by which fibronectin can be used to enhance the mechanical performance of artificial tissue constructs. tissue engineering; extracellular matrix; mechanical properties Address for reprint requests and other correspondence: D. C. Hocking, Dept. of Biomedical Engineering and Dept. of Pharmacology and Physiology, Univ. of Rochester Medical Center, 601 Elmwood Ave., PO Box 711, Rochester, NY 14642 (E-mail: denise_hocking{at}urmc.rochester.edu ).
ISSN:0363-6135
1522-1539
DOI:10.1152/ajpheart.00859.2003