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J Biol Chem, Vol. 273, Issue 13, 7457-7461, March 27, 1998

Autoactivation of Avian Urokinase-type Plasminogen Activator (uPA)
A NOVEL MODE OF INITIATION OF THE uPA/PLASMIN CASCADE

From the Department of Pathology, State University of New York, Stony Brook, New York 11794-8651

In contrast to mammalian urokinase-type plasminogen activator (uPA), which is produced and maintained in zymogen form, avian uPA is found in the active two-chain form in cultures of normal and transformed chicken cells in the absence of plasmin, the putative natural activator of pro-uPA. Recombinant chicken uPA (ch-uPA_wt) synthesized in two distinct expression systems also presents in the active two-chain form. In addition, conversion to the active uPA in both natural and recombinant expression systems could be prevented by uPA-specific inhibitors including a monoclonal antibody that uniquely inhibits the catalytic activity of ch-uPA. Most significantly, an active site mutant of avian uPA (ch-uPA_S353A) that lacks catalytic activity is produced and maintained in single-chain form. Furthermore, the single-chain ch-uPA_S353A mutant can be converted to the two-chain form by purified active ch-uPA_wt. These results strongly indicate an autocatalytic mechanism of activation of ch-uPA. Autoactivation appears to be an intrinsic property of ch-uPA and may be the initiating molecular event in uPA-mediated proteolytic cascades.

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