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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ragno P,Montuori N,Vassalli JD,Rossi G

doi

10.1016/0014-5793(93)81357-6

subject

Has Abstract

pub_date

1993-06-01 00:00:00

pages

279-84

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81357-6

journal_volume

323

pub_type

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