A new reconstituted connective tissue matrix: preparation, biochemical, structural and mechanical studies.
A fibrinogen derivative generated by thrombin was reacted with elastin to yield a new addition product or adduct between the two proteins. Addition of fibronectin, and then of collagen, did not interfere with the basic elastin-fibrinogen reaction and conferred the qualities of an artificial connective tissue to the product. Biochemical, structural and biomechanical aspects of the new matrix were studied. Aprotinin, heparin, thiomersal, and thiourea did not inhibit the main reaction; indeed, some of these ingredients improved the matrix cohesion. Scanning electron microscopy showed the genesis of a true network whose meshes were more reticulated by the addition of thiourea. Biomechanical studies, i.e., strength and elasticity showed the thiourea matrix to be the strongest. These intrinsic properties suggest the product could have biological and clinical applications.
Aprahamian
M
M
Unité 61 INSERM, Strasbourg, France.
Lambert
A
A
Balboni
G
G
Lefebvre
F
F
Schmitthaeusler
R
R
Damge
C
C
Rabaud
M
M
D001672:Biocompatible Materials; D003094:Collagen; D003238:Connective Tissue; D003450:Cryoglobulins; D004548:Elasticity; D004549:Elastin; D005109:Extracellular Matrix; D005340:Fibrinogen; D005353:Fibronectins; D008855:Microscopy, Electron, Scanning; D011480:Protease Inhibitors; D013718:Tensile Strength; D013917:Thrombin
D001672:Biocompatible Materials; D003450:Cryoglobulins; D005353:Fibronectins; D011480:Protease Inhibitors; D005340:Fibrinogen; D003094:Collagen; D004549:Elastin; D013917:Thrombin