Table 1 Inhibition of proteinases by recombinant mouse fetuin-A and fetuin-B.

From: Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

Proteinase

[enzyme]

[S]

Concentration range [fetuin-A; fetuin-B]

Ki [nM]; IC50 [nM] fetuin-A

Ki [nM]; IC50 [nM] fetuin-B

meprin α

0.25 nM

20 µM

3.50 nM–100 nM

n.i.

Ki 33 ± 2.4

meprin β

0.25 nM

20 µM

0.90 nM–100 nM

n.i.

Ki 7 ± 0.8

astacin

1.00 nM

400 µM

0.20 nM–900 nM

n.i.

Ki 16 ± 1.5

ovastacin

320.00 nM

21 µM

0.40 nM–1200 nM

n.i.

IC50 18 ± 1.2

nephrosin

10.00 nM

12 µM

0.02 nM–1 µM

n.i.

IC50 0.6 ± 0.1

TLL2

180.00 nM

20 µM

0.20 nM–2 µM

n.i.

n.i.

BMP1

10.00 nM

24 µM

0.20 nM–20 µM

n.i.

n.i.

ADAM10

38.00 nM

20 µM

1.0 µM

n.i.

n.i.

MMP-2

20.00 nM

20 µM

0.1 µM–20 µM

n.i.

n.i.

MMP-8

25.00 nM

20 µM

0.20 nM–20 µM

n.i.

n.i.

MMP-9

20.00 nM

20 µM

0.20 nM–20 µM

n.i.

n.i.

MMP-13

3.90 nM

20 µM

0.20 nM–20 µM

n.i.

n.i.

trypsin

5 nM

100 µM

100 nM–1 µM

n.i.

n.i.

chymotrypsin

19 nM

100 µM

100 nM–1 µM

n.i.

n.i.

legumain

10.00 nM

50 µM

100 nM–1 µM

n.i.

n.i.

papain

140.00 nM

50 µM

150 nM–300 nM

n.i.

n.i.

cathepsin B

10.00 nM

20 µM

10 nM–1 µM

n.i.

n.i.

cathepsin K

200.00 nM

320 µM

100 nM–1 µM

n.i.

n.i.

cathepsin S

50.00 nM

320 µM

50 nM–1 µM

n.i.

n.i.

cathepsin D

40.00 nM

30 µM

10.0 nM–1 µM

n.i.

n.i.

  1. Proteinase activity assays were performed with fluorescent substrates as detailed in the Methods section. Generally, we used seven or nine different duplicate concentrations of fetuins A and B in the indicated concentration range. Kinetic parameters were determined by fitting the data to the equation for tight binding inhibitors according to71. The standard errors of the fit are indicated. Due to the detection limits of substrate hydrolysis at low enzyme concentrations, it was not possible to determine a Ki-value for ovastacin and nephrosin. n.i.: no inhibition.