Activation of protein kinase C by tyrosine phosphorylation in response to H2O2
H Konishi, M Tanaka, Y Takemura… - Proceedings of the …, 1997 - National Acad Sciences
H Konishi, M Tanaka, Y Takemura, H Matsuzaki, Y Ono, U Kikkawa, Y Nishizuka
Proceedings of the National Academy of Sciences, 1997•National Acad SciencesProtein kinase C (PKC) isoforms, α, βI, and γ of cPKC subgroup, δ and ɛ of nPKC subgroup,
and ζ of aPKC subgroup, were tyrosine phosphorylated in COS-7 cells in response to H2O2.
These isoforms isolated from the H2O2-treated cells showed enhanced enzyme activity to
various extents. The enzymes, PKC α and δ, recovered from the cells were independent of
lipid cofactors for their catalytic activity. Analysis of mutated molecules of PKC δ showed that
tyrosine residues, which are conserved in the catalytic domain of the PKC family, are critical …
and ζ of aPKC subgroup, were tyrosine phosphorylated in COS-7 cells in response to H2O2.
These isoforms isolated from the H2O2-treated cells showed enhanced enzyme activity to
various extents. The enzymes, PKC α and δ, recovered from the cells were independent of
lipid cofactors for their catalytic activity. Analysis of mutated molecules of PKC δ showed that
tyrosine residues, which are conserved in the catalytic domain of the PKC family, are critical …
Protein kinase C (PKC) isoforms, α, βI, and γ of cPKC subgroup, δ and ɛ of nPKC subgroup, and ζ of aPKC subgroup, were tyrosine phosphorylated in COS-7 cells in response to H2O2. These isoforms isolated from the H2O2-treated cells showed enhanced enzyme activity to various extents. The enzymes, PKC α and δ, recovered from the cells were independent of lipid cofactors for their catalytic activity. Analysis of mutated molecules of PKC δ showed that tyrosine residues, which are conserved in the catalytic domain of the PKC family, are critical for PKC activation induced by H2O2. These results suggest that PKC isoforms can be activated through tyrosine phosphorylation in a manner unrelated to receptor-coupled hydrolysis of inositol phospholipids.
National Acad Sciences