Scatter factor is a glycoprotein but glycosylation is not required for its activity

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Scatter factor (SF) is a protein produced by fibroblasts, smooth muscle cells, and human placenta which scatter cohesive epithelial cell colonies and increases cellular motility. SF bound to concanavalin A and other lectins with high affinity. SF could also be stained with a glycoprotein specific stain. Incubation of producer cells (N-ras-transformed 3T3), with tunicamycin homolog A1 did not have any significant effect on the secretory activity of SF. The treatment of SF with N-and O-glycanases as well as endoglycosidase H had no effect on its activity. However, treatment of target (Madin Darby canine kidney) cells with tunicamycin A1, abolished the scattering response. These studies suggest that scatter factor is a glycoprotein, but glycosylation is not required for its secretion or activity by the producer cells; however, glycosylation of proteins in the target cells is required for SF action. © 1992.




Hofmann, R., Joseph, A., Bhargava, M. M., Rosen, E. M., & Goldberg, I. (1992). Scatter factor is a glycoprotein but glycosylation is not required for its activity. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1120(3), 343–350.

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