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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Urokinase-type plasminogen-activator and normal thyroid cell adhesion to the extracellular matrix.

The urokinase-type plasminogen activator receptor (uPA-R) focuses the proteolytic activity of its ligand, the urokinase-type plasminogen activator (uPA), on the cell surface, and can also act as an adhesion receptor for vitronectin (VTN). uPA increases uPA-R affinity for VTN and is also able to cleave its receptor. We have previously shown that uPA-R is involved in the adhesion of normal thyroid cells to VTN. In the present report, we have investigated the effect of uPA on normal thyroid cell adhesion to some extracellular matrix ( ECM) components. We show that a short-term treatment with uPA does not change normal thyroid cell adhesion to fibronectin (FNT), collagen ( CGN), laminin ( LMN) and VTN. The prolongation of uPA treatment increases cell adhesion to VTN, and, less efficiently, to other ECM components. Since the short term uPA treatment causes a partial cleavage of uPA-R, that does not increase with time, the observed increase in cell adhesivity cannot be related to the cleavage of uPA-R. We show that the adhesion improvement after the long term uPA treatment is instead due to a strong increase of the cell-surface expression of the integrin beta3 and a moderate increase of the integrin alpha(v). Both alpha(v) beta3 and alpha(v) beta1 are integrinic receptors for VTN.[1]

References

  1. Urokinase-type plasminogen-activator and normal thyroid cell adhesion to the extracellular matrix. Ragno, P., Montuori, N., Salzano, S., Rossi, G. Biochimie (1999) [Pubmed]
 
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