Activation of cellular protein kinase C and mode of inhibitory action of phospholipid-interacting compounds
| Autor: | Hiroyuki Nakanishi, Yasutomi Nishizuka, Yuko Uratsuji, Y Takeyama, Akira Kishimoto |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Blood Platelets
PRKCQ Chlorpromazine Octoxynol Biophysics Phospholipid Phosphatidylserines Biochemistry Polyethylene Glycols Cell membrane chemistry.chemical_compound medicine Animals Anesthetics Local Lipid bilayer Molecular Biology Protein kinase C Phospholipids Protein Kinase C integumentary system Kinase Cell Biology Chromatography Ion Exchange Enzyme Activation Membrane medicine.anatomical_structure chemistry Cyclin-dependent kinase complex Tetradecanoylphorbol Acetate lipids (amino acids peptides and proteins) Calcium Rabbits Protein Kinases |
| Zdroj: | Biochemical and biophysical research communications. 130(2) |
| ISSN: | 0006-291X |
| Popis: | 12-O-Tetradecanoylphorbol-13-acetate (TPA), that is intercalated into the cell membrane, binds a roughly stoichiometric amount of protein kinase C to produce a catalytically active complex with phospholipid. Local anesthetics and other phospholipid-interacting compounds such as chlorpromazine inhibit profoundly this complex formation in a manner competitive with phospholipid but not with TPA. A tiny change of the membrane phospholipid bilayer structure that is caused by TPA appears to facilitate this unique phospholipid-protein kinase C interaction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|