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J. Biol. Chem., Vol. 265, Issue 17, 9904-9908, Jun, 1990
V Ellis, TC Wun, N Behrendt, E Ronne and K Dano
Urokinase-type plasminogen activator (uPA) binds to a specific receptor on
various cell types, the bound molecule retaining its enzymatic activity
against plasminogen. We have now investigated whether receptor- bound uPA
also retains the ability to react with and be inhibited by plasminogen
activator inhibitors (PAI-1 and PAI-2). uPA bound to its receptor on human
U937 monocyte-like cells was inhibited by PAI-1 (in its active form in the
presence of vitronectin fragments) with an association rate constant of 4.5
x 10(6) M-1 s-1, which was 40% lower than that obtained for uPA in solution
(7.9 x 10(6) M-1 s-1). The inhibition of uPA by PAI-2 was decreased to a
similar extent by receptor binding, falling from 5.3 x 10(5) to 3.3 x 10(5)
M-1 s-1. Stimulation of U937 cells with phorbol 12-myristate 13-acetate was
accompanied by a further reduction in receptor-bound uPA inhibition by
PAI-1 and PAI-2 to 1.7 x 10(6) and 1.1 x 10(5) M-1 s-1, respectively. These
constants although lower than those for uPA in solution still represent
rather rapid inhibition of the enzyme, and demonstrate that uPA bound to
its specific cellular receptor remains available for efficient inhibition
by PAI's, which may therefore play a major role in controlling cell-surface
plasminogen activation and extracellular proteolytic activity.
Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors
Finsen Laboratory, Rigshospitalet, Copenhagen, Denmark.
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