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J. Biol. Chem., Vol. 266, Issue 33, 22307-22312, 11, 1991
DL Evans, M McGrogan, RW Scott and RW Carrell
Structural and functional properties of alpha-protease nexin I (alpha- PNI)
expressed in Chinese hamster ovary cells were studied. All three cysteines
were in the reduced form, showing that the potential disulfide bridge
between residues Cys117 and Cys131 was not formed. Heparin association rate
enhancements were from ka = 8.3 x 10(5) to 0.7- 1.6 x 10(9) M-1 s-1 for the
interaction of PNI with thrombin, from ka = 5.1 x 10(3) to 3.5 x 10(5) M-1
s-1 for interaction with Factor Xa, and from ka = 2.2 x 10(6) to 1.0 x
10(7) M-1 s-1 for interaction with trypsin; there was no rate enhancement
of the plasmin interaction (ka = 1.0 x 10(5) M-1 s-1). The minimal heparin
pentasaccharide had no effect on these interactions. Cleavage of the
reactive center loop of PNI by three different proteases gave the typical
stressed to relaxed change in thermal stability, but unlike with
antithrombin III, there was no loss of heparin affinity. A similar
difference from antithrombin was that PNI-thrombin complexes retained
normal heparin affinity. These results are compatible with a role for
protease nexin I as a cell- associated thrombin inhibitor that remains
bound to the cell surface even after complexing with the protease, as
compared with the role of antithrombin III as a circulating inhibitor of
thrombin that becomes activated on binding to the microvasculature and is
released on complex formation.
Protease specificity and heparin binding and activation of recombinant protease nexin I
Department of Haematology, University of Cambridge, United Kingdom.
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