Collagen-fibronectin interactions in normal and Rous sarcoma virus-transformed avian tendon cells: possible mechanisms for increased extracellular matrix turnover after transformation.
Using gelatin, casein, and fibronectin as substrates and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have identified protein-degrading enzymes in both normal and Rous sarcoma virus-transformed primary avian tendon cells. Although there are some consistent differences in the profile of the gelatinolytic activities (mainly metalloproteinases) between normal and transformed cells, the amounts of fibronectin-degrading activities seem to be comparable. In vitro studies reported here demonstrate that the degradation of fibronectin is partially and specifically inhibited by gelatin and collagen. We therefore propose that the abundant collagen present in normal tendon cells protects fibronectin against degradation. Conversely, in transformed cells, where collagen levels are drastically reduced, fibronectin may be more accessible to degradation. Thus differences in the steady-state levels of fibronectin on normal and transformed cells may be, at least in part, a consequence of changes in collagen levels.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000502:physiology; D001717:Birds; D002472:Cell Transformation, Viral; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism*; D003470:Culture Media; D005109:Extracellular Matrix / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D013710:Tendons / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*
D003470:Culture Media; D005353:Fibronectins; D003094:Collagen; D010447:Peptide Hydrolases