Enzymatic properties of the phosphorylated urokinase-type plasminogen activator isolated from a human carcinomatous cell line

Kei Takahashi*, Hau C. Kwaan, Enki Koh, Masataka Tanabe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

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 subsrate, 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, 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.

Original languageEnglish (US)
Pages (from-to)1473-1481
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume182
Issue number3
DOIs
StatePublished - Feb 14 1992

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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