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Metalloproteinases of the extracellular matrix and their inhibitors

100%

Kudaka D. M., Lodej P., Baier A., Szyszka R.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

2016

tom 97

nr 2

Mechanism of inhibition of the protein kinase C by nonstructure protein 3 of hepatitis C virus

100%

Hartjen P., Reinholz M., Baier A., Borowski P.

Cellular and Molecular Biology Letters

2005

tom 10

nr Suppl.2

The NTPase/helicase domain of hepatitis C virusnonstructural protein 3 inhibits protein kinase C inependently of its NTPase activity

51%

Hartjen P., Hochst B., Heim D., Von Der Kammer H., Lucke J., Reinholz M., Baier A., Smeets R., Wege H., Borowski P., Schulze zur Wiesch J.

Cellular and Molecular Biology Letters

2013

tom 18

nr 3

Helicase motif VI is a short arginine-rich motif within the NTPase/helicase domain of the non-structural protein 3 (NS3) of the hepatitis C virus (HCV). We previously demonstrated that it reduces the catalytic activity and intracellular shuttling of protein kinase C (PKC). Thus, NS3-mediated PKC inhibition may be involved in HCV-associated hepatocellular carcinoma (HCC). In this study, we expand on our earlier results, which were obtained in experiments with short fragments of NS3, to show for the first time that the catalytically active, longer C-terminal NTPase/helicase of NS3 acts as a potent PKC inhibitor in vitro. PKC inhibition assays with the NTPase-inactive mutant NS3h-D1316A revealed a mixed type kinetic inhibition pattern. A broad range of 11 PKC isotypes was tested and all of the PKC isotypes were inhibited with IC50-values in the low micromolar range. These findings were confirmed for the wild-type NTPase/helicase domain in a non-radiometric PKC inhibition assay with ATP regeneration to rule out any effect of ATP hydrolysis caused by its NTPase activity. PKCα was inhibited with a micromolar IC50 in this assay, which compares well with our result for NS3h-D1316A (IC50 = 0.7 μM). In summary, these results confirm that catalytically active NS3 NTPase/helicase can act in an analogous manner to shorter NS3 fragments as a pseudosubstrate inhibitor of PKC.

Ograniczanie wyników

2 Cellular and Molecular Biology Letters

1 BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

3 Baier A.

2 Borowski P.

2 Hartjen P.

2 Reinholz M.

1 Heim D.

1 Hochst B.

1 Kudaka D. M.

1 Lodej P.

1 Lucke J.

1 Schulze zur Wiesch J.

1 Smeets R.

1 Szyszka R.

1 Von Der Kammer H.

1 Wege H.

1 2016

1 2013

1 2005

Wyniki wyszukiwania

Metalloproteinases of the extracellular matrix and their inhibitors

Mechanism of inhibition of the protein kinase C by nonstructure protein 3 of hepatitis C virus

The NTPase/helicase domain of hepatitis C virusnonstructural protein 3 inhibits protein kinase C inependently of its NTPase activity