Fibronectin matrix polymerization increases tensile strength of model tissue.
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.
Department of Biomedical, University of Rochester Medical Center, 601 Elmwood Ave., PO Box 711, Rochester, NY 14642, USA.
Candace D
CD
Gildner
Amy L
AL
Lerner
Denise C
DC
Hocking
D000199:Actins / Q000502:physiology; D000818:Animals; D002478:Cells, Cultured; D003094:Collagen / Q000737:chemistry*; D003599:Cytoskeleton / Q000502:physiology; D005109:Extracellular Matrix / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism* / Q000494:pharmacology; D005782:Gels; D051379:Mice; D009130:Muscle, Smooth / Q000166:cytology / Q000378:metabolism*; D010446:Peptide Fragments / Q000494:pharmacology; D011108:Polymers / Q000378:metabolism*; D013718:Tensile Strength
D000199:Actins; D005353:Fibronectins; D005782:Gels; D010446:Peptide Fragments; D011108:Polymers; C487893:glutathione-S-transferase-III-1H,8-10; D003094:Collagen