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The high molecular weight form of the plasminogen activator urokinase (54 kD) binds to specific receptor sites on the cell membrane of breast carcinomas by its inactive "A" chain. The binding is of high affinity (range of dissociation constants: 5.6 X 10(-11) to 4 X 10(-10) mol l-1 and there were between 20 to 250 fmol of binding sites per milligram of membrane protein) and equilibrium is reached in 60 min. No competition for binding sites was observed with epidermal growth factor, tissue plasminogen activator or the low molecular weight form of urokinase (33 kD). Cross-linking experiments suggest that the receptor is a monomeric unit of molecular weight of 50 kD. This binding site provides a mechanism for the incorporation of urokinase into the cell membrane.

Type

Journal article

Journal

Br J Cancer

Publication Date

01/1987

Volume

55

Pages

13 - 16

Keywords

Binding, Competitive, Breast Neoplasms, Cell Membrane, Epidermal Growth Factor, Female, Humans, Molecular Weight, Receptors, Cell Surface, Urokinase-Type Plasminogen Activator