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  • Title: The mitogenic activity of a heparin-binding fibronectin fragment (Mr 35,000) produced by cathepsin D digestion.
    Author: Savill CM, Ayad SR.
    Journal: Anticancer Res; 1986; 6(2):321-6. PubMed ID: 3707069.
    Abstract:
    Fibronectin was partially digested using the lysosomal proteinase cathepsin D and the fragments produced tested for their effect on the rate of DNA synthesis in quiescent Chinese Hamster Fibroblasts (CH23). A mitogenically active digest was produced after digestion of fibronectin with cathepsin D for 2 to 3h at a 1:200 (w/w) ratio of enzyme to substrate at 37 degrees C. Affinity chromatography of the active digest on both gelatin and heparin 4BCl columns demonstrated that the active fragment was gelatin-nonbinding but heparin-binding, and therefore derived from one of the two or three heparin binding domains of intact fibronectin. The active fragment was found to have a Mr35,000 by gel filtration on sephacryl S200. A dose-response curve of the mitogenic fragment purified by gel filtration against DNA synthesis showed it to be maximally active at a concentration of approximately 10 micrograms/ml.
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