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(D)-Leu-(L)-Ser-(L)-Thr-(L)-Arg p-nitroanilide + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GYPGQV + H2O
7-methoxycoumarin-4-acetate + GYPGQV
-
-
-
-
?
7-methoxycoumarin-4-acetyl-IVGGQE + H2O
7-methoxycoumarin-4-acetate + IVGGQE
-
-
-
-
?
7-methoxycoumarin-4-acetyl-SFLLRN + H2O
7-methoxycoumarin-4-acetate + SFLLRN
-
-
-
-
?
7-methoxycoumarin-4-acetyl-VSQKSP + H2O
7-methoxycoumarin-4-acetate + VSQKSP
-
-
-
-
?
7-methoxycoumarin-4-acetyl-VYQPQP + H2O
7-methoxycoumarin-4-acetate + VYQPQP
-
-
-
-
?
AVSQSKP-7-amido-4-methylcoumarin + H2O
AVSQSKP + 7-amino-4-methylcoumarin
-
low activity
-
-
?
AVYQPQP-7-amido-4-methylcoumarin + H2O
AVYQPQP + 7-amino-4-methylcoumarin
-
low activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Leu-Pro-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Leu-Pro-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Val-Pro-Arg + 4-nitroaniline
-
-
-
?
Bz-Ile-Glu-Arg-4-nitroanilide + H2O
Bz-Ile-Glu-Arg + 4-nitroaniline
-
chromogenic commercial substrate
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
D-Ala-Pro-Arg-4-nitroanilide + H2O
D-Ala-Pro-Arg + 4-nitroaniline
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
-
-
?
Factor X + H2O
Factor Xa + ?
Fibrinogen + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
enzyme CP cleaves fibronectin between Ala and Val residues, in regions rich in Pro and Gln residues. The 45 and 60 kDa fragments have the same N-terminal sequence, generated by cleavage of the bond between Ala292 and Val293
-
-
?
GDR-7-amido-4-methylcoumarin + H2O
GDR + 7-amino-4-methylcoumarin
-
low activity
-
-
?
Glu-Glu-Phe-Lys-4-nitroanilide + H2O
Glu-Glu-Phe-Lys + 4-nitroaniline
-
-
-
?
Glu-Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Glu-Pro-Arg + 4-nitroaniline
inactive factor X + H2O
active factor Xa + ?
Laminin + H2O
?
-
-
-
-
?
Leu-Pro-Arg-4-nitroanilide + H2O
Leu-Pro-Arg + 4-nitroaniline
-
-
-
?
LPAPR-7-amido-4-methylcoumarin + H2O
LPAPR + 7-amino-4-methylcoumarin
-
-
-
-
?
methylsulfonyl-D-cyclohexylalanyl-butyl-Arg-4-nitroanilide + H2O
methylsulfonyl-D-cyclohexylalanyl-butyl-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
PKSQSVA-7-amido-4-methylcoumarin + H2O
PKSQSVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
PQPQYVA-7-amido-4-methylcoumarin + H2O
PQPQYVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
PQVR-7-amido-4-methylcoumarin + H2O
PQVR + 7-amino-4-methylcoumarin
QSPVR-7-amido-4-methylcoumarin + H2O
QSPVR + 7-amino-4-methylcoumarin
-
-
-
-
?
QVR-7-amido-4-methylcoumarin + H2O
QVR + 7-amino-4-methylcoumarin
-
-
-
-
?
RGD-7-amido-4-methylcoumarin + H2O
RGD + 7-amino-4-methylcoumarin
-
low activity
-
-
?
Sar-Pro-Arg-p-nitroanilide + H2O
Sar-Pro-Arg + p-nitroaniline
-
-
-
-
?
sarcosyl-Pro-Arg-4-nitroanilide + H2O
sarcosyl-Pro-Arg + 4-nitroaniline
-
-
-
?
tert-butoxycarbonyl-AVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-AVR + 7-amino-4-methylcoumarin
-
high activity
-
-
?
tert-butoxycarbonyl-AVYQPQP-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-AVYQPQP + 7-amino-4-methylcoumarin
-
high activity
-
-
?
tert-butoxycarbonyl-GDR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-GDR + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-PKSQSVA-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PKSQSVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
tert-butoxycarbonyl-PQPQYVA-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PQPQYVA + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-PQVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PQVR + 7-amino-4-methylcoumarin
-
best substrate, this substrate is also cleaved by collagenase
-
-
?
tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
tert-butoxycarbonyl-RGD-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-RGD + 7-amino-4-methylcoumarin
-
-
-
-
?
thrombin TH + H2O
?
-
-
-
-
?
Val-Pro-Arg-4-nitroanilide + H2O
Val-Pro-Arg + 4-nitroaniline
-
-
-
?
additional information
?
-
D-Ala-Pro-Arg-4-nitroanilide + H2O
D-Ala-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ala-Pro-Arg-4-nitroanilide + H2O
D-Ala-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
factor X + H2O
?
-
-
-
-
?
factor X + H2O
?
-
that triggers blood coagulation by directly activating factor X in the absence of factor VII
-
-
?
factor X + H2O
?
-
thiol protease with thrombin-like specificity
-
-
?
factor X + H2O
?
-
factor X-activating cysteine proteinase
-
-
?
factor X + H2O
?
-
that triggers blood coagulation by directly activating factor X in the absence of factor VII
-
-
?
factor X + H2O
?
-
factor X-activating cysteine proteinase
-
-
?
factor X + H2O
factor Xa
-
-
-
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond, activation of the coaglutation factor X
-
?
factor X + H2O
factor Xa
-
activation
-
-
?
factor X + H2O
factor Xa
-
activation, commercial substrate
-
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19
-
?
Glu-Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
Glu-Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X, degradation of factor X during 24 h
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X (57.3 kDa), cleavage of factor X at the conventional activation site, i.e. between Arg52 and Ile53, in the heavy chain
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
PAR-1 receptor + H2O
?
-
-
-
?
PAR-1 receptor + H2O
?
-
enzyme competes with thrombin for the same protease-activated receptor, i.e. PAR-1, on the blood platelet surface
-
?
PQVR-7-amido-4-methylcoumarin + H2O
PQVR + 7-amino-4-methylcoumarin
-
-
-
-
?
PQVR-7-amido-4-methylcoumarin + H2O
PQVR + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
-
best synthetic substrate
-
-
?
tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
-
high activity
-
-
?
additional information
?
-
-
substrate specificity, overview
-
?
additional information
?
-
-
substrate recognition depends on the secondary and tertiary configuration of the protein substrate rather than on the primary sequence alone, no activity with substrates containing the sequence Xaa-Lys-ProP2-TyrP1-
-
?
additional information
?
-
-
enzyme seems to be regulated allosterically
-
?
additional information
?
-
-
the activity of cancer procoagulant in cases of uterine leiomyomas, overview
-
-
?
additional information
?
-
-
the enzyme is able to stimulate blood platelet adhesion to fibrinogen and collagen, which can also play a role in metastatic spread of cancer as well as primary tumor growth
-
-
?
additional information
?
-
-
the enzyme plays a role in pathogenesis of cancer-related thrombosis, the enzyme concentration in serum is positively correlated to fibrinogen concentration, but negatively correlated to free protein S plasma content, determination of prothrobotic parameters and correlation to enzyme activity, overview
-
-
?
additional information
?
-
-
the enzyme is a cysteine protease, the enzyme mediates growth and adhesion of MCF-7 cancer cells to vitronectin in vitro
-
-
?
additional information
?
-
-
high level of cancer procoagulant is a risk factor for multiple myeloma
-
-
?
additional information
?
-
-
substrate specificity analysis, mass spectrometric detection of cleavage products. No activity with tert-benzyloxycarbonyl-QSPVR-7-amido-4-methylcoumarin and TLDPR-7-amido-4-methylcoumarin. Enzyme CP shows very little cysteine protease activity, it appears to exhibit mixed protease activity, but acts predominantly as a serine protease
-
-
?
additional information
?
-
-
cancer procoagulant is a cysteine protease acting as an activator of coagulation factor X, the protein activates factor X in the absence of tissue factor and factor VII
-
-
?
additional information
?
-
-
rat and human cancer procoagulant activity bind similarly to antiCP antibodies
-
-
?
additional information
?
-
-
in vitro screening of synthetic fluorogenic substrates for detection of cancer procoagulant activity, substrate design, synthesis, and evaluation, e.g. based on the RGD motif of fibronectin, overview. The most reliable assay for the quantification of cancer procoagulant activity is the three-stage chromogenic assay which utilises the ability of cancer procoagulant to activate factor X. In this assay, the activation of factor X leads to the formation of activated thrombin from prothrombin and the eventual hydrolyses of a thrombin chromogenic substrate which contains a p nitroaniline leaving group. No activity with tert-benzyloxycarbonyl-AVSQSKP-7-amido-4-methylcoumarin
-
-
?
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(D)-Phe-Pro-(D,L)-(4'-guanidino)-Phe-trifluoromethyl ketone
-
-
(D)-Phe-Pro-(D,L)-Lys-trifluoromethyl ketone
-
weak
(D)-Phe-Pro-Arg-chloromethyl ketone
-
-
(NH4)2SO4
-
76% inhibition at about 40 mM
alpha1-Aantichymotrypsin
-
antiCP polyclonal antibody
-
-
-
antiFVIIa polyclonal antibody
-
-
-
benzamidine
-
strong inhibition
benzoxycarbonyl-Lys-CHN2
-
-
CaCl2
-
91% inhibition at about 40 mM
diisopropylfluorophosphate
Hg2+
-
0.1 mM: 85.5% decrease of activity
MgCl2
-
81% inhibition at about 40 mM
MgSO4
-
68% inhibition at about 40 mM
Mn2+
-
above 1 mM, activates below 1 mM
N-benzyloxycarbonyl-Phe-Ala-CHN2
-
-
NaCl
-
12-21% inhibition, respectively
p-chloromercuric benzoate
-
-
pepstatin A
-
low inhibition
Peptidyl diazomethyl ketones
Peptidyl dimethylsulfonium salts
-
Peptidyl sulfonium salts
-
-
-
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
-
strong inhibition
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
alpha1-Aantichymotrypsin
-
weak
-
alpha1-Aantichymotrypsin
-
weak
-
alpha2-Macroglobulin
-
weak
-
alpha2-Macroglobulin
-
weak
-
antipain
-
enhanced in reduced environment
antipain
-
enhanced in reduced environment
Cu2+
-
inactivation
Cu2+
-
1 mM: 46% decrease of activity (not statistically significant)
diisopropylfluorophosphate
-
strong
diisopropylfluorophosphate
-
strong
E64
-
-
E64
-
specific inhibition
Fe2+
-
in the presence of Ca2+, complete inactivation at 1 mM Fe2+ and above
HgCl2
-
strong, less effective in reduced environment
HgCl2
-
complete inhibition at about 40 mM
HgCl2
-
strong, less effective in reduced environment
iodoacetamide
-
strong, still enhanced in reduced environment
iodoacetamide
-
strong, still enhanced in reduced environment
leupeptin
-
enhanced in reduced environment
leupeptin
-
enhanced in reduced environment
Mercuric chloride
-
-
Peptidyl chloromethanes
-
-
Peptidyl chloromethanes
-
-
Peptidyl diazomethanes
-
-
Peptidyl diazomethanes
-
-
Peptidyl diazomethyl ketones
-
-
Peptidyl diazomethyl ketones
-
-
Peptidyl dimethylsulfonium salts
-
-
-
Peptidyl dimethylsulfonium salts
-
-
-
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
PMSF
-
-
Sn2+
-
inactivation
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
-
enhanced in reduced environment
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
-
i.e. E-64, thiol protease inhibitor, factor X protects
trans-epoxysuccinyl-L-leucyl-amido(4-guanidino)butane
-
enhanced in reduced environment
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64, reversible, competitive
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
ie.e. E-64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
ie.e. E-64, reversible, competitive
Zn2+
-
in the presence of Ca2+, complete inactivation at 1 mM Zn2+ and above
additional information
-
cystatin, alpha1-antiprotease, antithrombin III
-
additional information
-
no inhibition by alpha2-macroglobulin, alpha1-antiprotease, antithrombin III/heparin, cystatin, cysteamine, alpha1-anichymotrypsin, the effectiveness of most of the inhibitors increase in presence of reducing agents
-
additional information
-
inhibition by specific anti-CP antibodies
-
additional information
-
no or poor inhibition by iodoacetamide and E-64
-
additional information
-
no inhibition by cystamine, benzoxycarbonyl-Val-Phe
-
additional information
-
cystatin, alpha1-antiprotease, antithrombin III
-
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0.059
-
crude extract from independent PA3 tumor, activity of samples is determined by using a 3-stage chromogenic assay
0.068
-
crude extract from independent PA3 prostate tumor, activity of samples is determined by using a 3-stage chromogenic assay
0.078
-
crude extract from independent PA3 prostate tumor, activity of samples is determined by using a 3-stage chromogenic assay
0.082
-
crude extract from independent PA3 rat prostate tumor, activity of samples is determined by using a 3-stage chromogenic assay
0.098
-
crude extract from independent PA3 prostate tumor, activity of samples is determined by using a 3-stage chromogenic assay
0.16
-
substrate GDR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
0.65
-
substrate PQPQYVA-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
0.98
-
substrate tert-benzyloxycarbonyl-PKSQSVA-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
1.47
-
substrate PKSQSVA-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
1.63
-
substrate tert-benzyloxycarbonyl-PQPQYVA-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
1.95
-
substrate tert-benzyloxycarbonyl-RGD-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
16.6
-
extract from independent PA3 prostate tumor undergoes 1 round of purification on the anion exchanger, 202fold purification, activity of samples is determined by using a 3-stage chromogenic assay
163.28
-
substrate tert-benzyloxycarbonyl-AVR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
17.58
-
substrate RGD-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
2.26
-
extract from independent PA3 prostate tumor undergoes 1 round of purification on the anion exchanger, 33fold purification, activity of samples is determined by using a 3-stage chromogenic assay
2.32
-
extract from independent PA3 prostate tumor undergoes 1 round of purification on the anion exchanger, 30fold purification, activity of samples is determined by using a 3-stage chromogenic assay
2.93
-
substrate AVSQSKP-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
3.09
-
substrate PQVR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
332.25
-
substrate tert-benzyloxycarbonyl-PQVR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
4.91
-
extract from independent PA3 prostate tumor undergoes 1 round of purification on the anion exchanger, 50fold purification, activity of samples is determined by using a 3-stage chromogenic assay
6.67
-
substrate tert-benzyloxycarbonyl-GDR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
66.91
-
substrate tert-benzyloxycarbonyl-AVYQPQP-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
7.7
-
extract from independent PA3 prostate tumor undergoes 1 round of purification on the anion exchanger, 133fold purification, activity of samples is determined by using a 3-stage chromogenic assay
9.44
-
substrate AVYQPQP-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
99.79
-
substrate tert-benzyloxycarbonyl-QVR-7-amido-4-methylcoumarin, pH and temperature not specified in the publication
additional information
-
-
additional information
-
-
additional information
-
specific activity in various rat tissues
additional information
-
three-stage chromatographic assay method
additional information
-
tissue-specific enzyme activity, overview
additional information
-
enzyme has procoagulant activity
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Falanga, A.; Gordon, S.G.
Isolation and characterization of cancer procoagulant: a cysteine proteinase from malignant tissue
Biochemistry
24
5558-5567
1985
Oryctolagus cuniculus
brenda
Falanga, A.; Bolognese Dalessandro, A.P.; Casali, B.; Roncaglioni, M.C.; Donati, M.B.
Several murine metastasizing tumors possess a cysteine proteinase with cancer procoagulant characteristics
Int. J. Cancer
39
774-777
1987
Oryctolagus cuniculus, Mus musculus
brenda
Falanga, A.; Shaw, E.; Donati, M.B.; Consonni, R.; Barbui, T.; Gordon, S.G.
Inhibition of cancer procoagulant by peptidyl diazomethyl ketones and peptidyl sulfonium salts
Thromb. Res.
54
389-398
1989
Oryctolagus cuniculus
brenda
Moore, W.R.
The purification and properties of cancer procoagulant from murine tumors
Biochem. Biophys. Res. Commun.
184
819-824
1992
Mus musculus
brenda
Gordon, S.G.
Cancer procoagulant
Methods Enzymol.
244
568-583
1994
Homo sapiens, Rattus norvegicus
brenda
Mielicki, W.P.; Kozwich, D.L.; Kramer, L.C.; Gordon, S.G.
Effect of divalent ions on the activity of cancer procoagulant
Arch. Biochem. Biophys.
314
165-170
1994
Homo sapiens
brenda
Mielicki, W.P.
Biochemistry of cancer procoagulant
Haemostasis
31 Suppl 1
8-10
2001
Oryctolagus cuniculus, Homo sapiens
brenda
Mielicki, W.P.; Mielicka, E.; Gordon, S.G.
Cancer procoagulant activity studies using synthetic peptidyl substrates
Thromb. Res.
87
251-256
1997
Homo sapiens
brenda
Raasi, S.; Mielicki, W.P.; Gordon, S.G.; Korte, W.
Properties of proteins in cancer procoagulant preparations that are detected by anti-tissue factor antibodies
Arch. Biochem. Biophys.
428
131-135
2004
Homo sapiens
brenda
Kazmierczak, M.; Lewandowski, K.; Wojtukiewicz, M.Z.; Turowiecka, Z.; Kolacz, E.; Lojko, A.; Skrzydlewska, E.; Zawilska, K.; Komarnicki, M.
Cancer procoagulant in patients with adenocarcinomas
Blood Coagul. Fibrinolysis
16
543-547
2005
Homo sapiens
brenda
Kamocka, M.; Rozalski, M.; Krajewska, U.; Wierzbicki, R.; Mielicki, W.P.
Effect of cancer procoagulant (CP) on the growth and adhesion of MCF-7 cells to vitronectin in vitro
Cancer Lett.
222
89-94
2005
Homo sapiens
brenda
Jozwik, M.; Szajda, S.D.; Skrzydlewski, Z.; Jozwik, M.; Sulkowski, S.
The activity of cancer procoagulant in cases of uterine leiomyomas
Eur. J. Gynaecol. Oncol.
26
407-410
2005
Homo sapiens
brenda
Kamocka, M.; Kaplinska, K.; Mielicki, W.P.
Effect of immunisation with cancer procoagulant on the growth of Walker 256 carcinosarcoma cells in rats
Clin. Exp. Med.
6
119-123
2006
Homo sapiens
brenda
Szajda, S.D.; Jozwik, M.; Sulkowska, M.; Chabielska, E.; Sulkowski, S.; Jozwik, M.
Analysis of the relationship between cancer procoagulant activity and PCNA and Ki-67 expression in cases of common and cellular uterine leiomyomas
Eur. J. Gynaecol. Oncol.
27
495-499
2006
Homo sapiens
brenda
Kamocka, M.; Pollard, M.; Suckow, M.; Mielicki, W.P.; Rosen, E.D.
Rat prostate tumors express cancer procoagulant, an activator of coagulation factor X
Comp. Med.
58
282-286
2008
Rattus norvegicus
brenda
Musallam, K.M.; Dahdaleh, F.S.; Shamseddine, A.I.; Taher, A.T.
Incidence and prophylaxis of venous thromboembolic events in multiple myeloma patients receiving immunomodulatory therapy
Thromb. Res.
123
679-686
2009
Homo sapiens
brenda
Kaplinska, K.; Rozalski, M.; Krajewska, U.; Mielicki, W.P.
Cancer procoagulant (CP) analysis in human WM 115 malignant melanoma cells in vitro
Thromb. Res.
124
364-367
2009
Homo sapiens
brenda
Kee, N.L.; Naude, R.J.; Blatch, G.L.; Frost, C.L.
The effect of cancer procoagulant on expression of metastatic and angiogenic markers in breast cancer and embryonic stem cell lines
Biol. Chem.
393
113-121
2012
Homo sapiens
brenda
Hoffman, E.A.; Gizelska, K.; Mirowski, M.; Mielicki, W.
Arsenic trioxide downregulates cancer procoagulant activity in MCF-7 and WM-115 cell lines in vitro
Contemp. Oncol. (Pozn.)
19
108-112
2015
Homo sapiens
brenda
Kee, N.L.; Krause, J.; Blatch, G.L.; Muramoto, K.; Sakka, K.; Sakka, M.; Naude, R.J.; Wagner, L.; Wolf, R.; Rahfeld, J.U.; Demuth, H.U.; Mielicki, W.P.; Frost, C.L.
The proteolytic profile of human cancer procoagulant suggests that it promotes cancer metastasis at the level of activation rather than degradation
Protein J.
34
338-348
2015
Homo sapiens
brenda
Krause, J.; Frost, C.L.
In vitro screening of synthetic fluorogenic substrates for detection of cancer procoagulant activity
Protein J.
37
151-163
2018
Rattus norvegicus
brenda