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PLG — TFPI2
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Rao et al., Biochem Biophys Res Commun 1999
:
Both
plasmin and trypsin activated proMMP-1 by converting the 53-kDa proenzyme to the partially active 43-kDa polypeptide ; this activity was
inhibited by
TFPI-2/MSPI
Neaud et al., J Biol Chem 2000
(Carcinoma, Hepatocellular...) :
Despite the fact that recombinant
TFPI-2 readily
inhibits plasmin , we show that it potentiates HGF induced invasion of HCC cells and is capable of inducing invasion on its own
Rao et al., Biochem Biophys Res Commun 2000
(Fibrosarcoma...) :
The refolded E. coli
TFPI-2 inhibited
plasmin with an inhibition constant ( K ( i ) ) of 5 nM that is similar with the TFPI-2 expressed in a mammalian system
Peerschke et al., Thromb Haemost 2004
(Inflammation) :
Binding of TFPI-2 to gC1qR produced statistically significant but modest reductions in
TFPI-2 inhibition of
plasmin , but had no effect on kallikrein inhibition in fluid phase chromogenic assays
Bajaj et al., J Biol Chem 2011
(Disease Models, Animal...) :
Full-length
TFPI-2 or its isolated first Kunitz domain ( KD1 ) also
inhibits plasmin ; therefore, it has been proposed for use as an antifibrinolytic agent
Petersen et al., Biochemistry 1996
:
In addition to its ability to inhibit the amidolytic and proteolytic activities of the factor VIIa-tissue factor complex,
TFPI-2/PP5 strongly
inhibited the amidolytic activities of human factor XIa, human plasma kallikrein, and human
plasmin with Ki values of 15, 25, and 3 nM, respectively