Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin inhibits protein kinase C-mediated …
JA WATSON, MG RUMSBY… - Biochemical …, 1999 - portlandpress.com
JA WATSON, MG RUMSBY, RG WOLOWACZ
Biochemical Journal, 1999•portlandpress.comUsing phage display we identify the redox proteins thioredoxin and superoxide dismutase
(SOD) as novel protein kinase C (PKC)-interacting proteins. Overlay assays demonstrated
that PKC bound to immobilized thioredoxin, providing supporting evidence for the phage
display results. Kinase assays demonstrated that SOD and thioredoxin were not direct
substrates for PKC but that both proteins blocked autophosphorylation of PKC. Moreover,
thioredoxin inhibited PKC-mediated phosphorylation of histone (IC50of approx. 20 ng/ml).
(SOD) as novel protein kinase C (PKC)-interacting proteins. Overlay assays demonstrated
that PKC bound to immobilized thioredoxin, providing supporting evidence for the phage
display results. Kinase assays demonstrated that SOD and thioredoxin were not direct
substrates for PKC but that both proteins blocked autophosphorylation of PKC. Moreover,
thioredoxin inhibited PKC-mediated phosphorylation of histone (IC50of approx. 20 ng/ml).
Using phage display we identify the redox proteins thioredoxin and superoxide dismutase (SOD) as novel protein kinase C (PKC)-interacting proteins. Overlay assays demonstrated that PKC bound to immobilized thioredoxin, providing supporting evidence for the phage display results. Kinase assays demonstrated that SOD and thioredoxin were not direct substrates for PKC but that both proteins blocked autophosphorylation of PKC. Moreover, thioredoxin inhibited PKC-mediated phosphorylation of histone (IC50of approx. 20 ng/ml).
portlandpress.com
