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 Lettjournal_title
FEBS lettersauthors
Ragno P,Montuori N,Vassalli JD,Rossi Gdoi
10.1016/0014-5793(93)81357-6subject
Has Abstractpub_date
1993-06-01 00:00:00pages
279-84issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)81357-6journal_volume
323pub_type
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