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Activation of protein kinase C by tyrosine phosphorylation in response to H 2 O 2
Open accessAbstract
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 H 2 O 2 . These isoforms isolated from the H 2 O 2 -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 H 2 O 2 . These results suggest that PKC isoforms can be activated through tyrosine phosphorylation in a manner unrelated to receptor-coupled hydrolysis of inositol phospholipids.
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Cites
Protein kinase C and lipid signaling for sustained cellular responses
Nishizuka, Y. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.7.7737456 · Cited by 2,499
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Metadata
- Authors
- Konishi, H., Tanaka, M., Takemura, Y., Matsuzaki, H., Ono, Y., Kikkawa, U., & Nishizuka, Y.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-10-14
- Volume
- 94
- Issue
- 21
- Pages
- 11233-11237
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2000586934
- Cited by
- 605
- References
- 1
- FWCI
- 10.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Konishi, H., Tanaka, M., Takemura, Y., Matsuzaki, H., Ono, Y., Kikkawa, U., & Nishizuka, Y. (1997). Activation of protein kinase C by tyrosine phosphorylation in response to H 2 O 2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.21.11233
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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