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Scientific article
English

Processing of complex between urokinase and its type-2 inhibitor on the cell surface. A possible regulatory mechanism of urokinase activity

Published inFEBS letters, vol. 323, no. 3, p. 279-284
Publication date1993
Abstract

Complexes between the urokinase-type plasminogen activator (uPA) and its type-2 inhibitor (PAI-2) are bound by a cell-surface receptor for uPA and rapidly cleaved into two fragments of 70 and 22 kDa. The 70-kDa fragment contains the active site of uPA and PAI-2, while the 22-kDa species was identified as the amino terminal fragment of uPA, that binds specifically to the receptor. When the experiment is performed at 4 degrees C, both fragments remain bound to the cell surface and can be eluted by acid treatment. We therefore postulate that after the binding of the uPA-PAI-2 complex, a new binding site for the 70-kDa species becomes available. This additional binding favours the cleavage of the complex into the 70-and 22-kDa fragments; the 70-kDa species is endocytosed or released, while the 22-kDa fragment remains on the cell surface to prevent the binding of intact uPA.

Keywords
  • Cell Line
  • Cell Membrane/metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Homeostasis
  • Humans
  • Molecular Weight
  • Plasminogen Activator Inhibitor 2/isolation & purification/ metabolism
  • Protein Binding
  • Receptors, Cell Surface/metabolism
  • Receptors, Urokinase Plasminogen Activator
  • Urokinase-Type Plasminogen Activator/isolation & purification/ metabolism
Citation (ISO format)
RAGNO, P. et al. Processing of complex between urokinase and its type-2 inhibitor on the cell surface. A possible regulatory mechanism of urokinase activity. In: FEBS letters, 1993, vol. 323, n° 3, p. 279–284. doi: 10.1016/0014-5793(93)81357-6
Identifiers
ISSN of the journal0014-5793
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