Abstract:
:Enzymatic properties of phosphorylated urokinase plasminogen activator (P-uPA) (1) extracted from human carcinomatous cell line Detroit 562 cells were compared with those of non-phosphorylated uPA of urinary origin (nP-uPA). Using plasminogen as a substrate, the Km and Kcat of P-uPA were higher than that of nP-uPA while the Kcat/Km was lower. By zymography, a greater degree of plasminogen activation was observed. Concanavalin A reacted to both the enzymes. P-uPA had a low affinity for the inhibitors of plasminogen activator PAI-1 and PAI-2, and was inhibited only by the excess amounts of inhibitors. For PAI-1, and the KIs of P-uPA was greater and for PAI-2, KI was higher for P-uPA. These alterations by phosphorylation enable uPA to be more efficient in a focal proteolysis through plasminogen activation.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Takahashi K,Kwaan HC,Koh E,Tanabe Mdoi
10.1016/0006-291x(92)91900-bsubject
Has Abstractpub_date
1992-02-14 00:00:00pages
1473-81issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(92)91900-Bjournal_volume
182pub_type
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