Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin inhibits protein kinase C-mediated phosphorylation of histone

Autor:	J A, Watson, M G, Rumsby, R G, Wolowacz
Rok vydání:	1999
Předmět:	inorganic chemicals Superoxide Dismutase Reproducibility of Results Substrate Specificity Histones Isoenzymes Inhibitory Concentration 50 Thioredoxins Peptide Library Humans Cloning Molecular Phosphorylation Protein Kinase C Protein Binding Research Article
Zdroj:	The Biochemical journal.
ISSN:	0264-6021
Popis:	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 (IC(50) of approx. 20 ng/ml).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7a0430848ef5f3c63d4041148005fa19 https://pubmed.ncbi.nlm.nih.gov/10510292 Zobrazit plný text záznamu