Reciprocal interactions between protein kinase C and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester

• Published in: The Journal of biological chemistry Vol. 269; no. 14; pp. 10813 - 10819
• Main Authors: CURNUTTE, J. T, ERICKSON, R. W, JIABING DING, BADWEY, J. A
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 08.04.1994
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Biological Transport; Detergents; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Granulomatous Disease, Chronic - immunology; Granulomatous Disease, Chronic - metabolism; Humans; In Vitro Techniques; Molecular Sequence Data; NADH, NADPH Oxidoreductases - metabolism; NADPH Dehydrogenase - metabolism; NADPH Oxidases; Neutrophils - drug effects; Neutrophils - immunology; Neutrophils - metabolism; Octoxynol; Oxidoreductases; Oxygen - metabolism; Phosphoprotein Phosphatases - antagonists & inhibitors; Phosphoproteins - metabolism; Protein Kinase C - metabolism; Protein Kinase Inhibitors; Superoxides - metabolism; Tetradecanoylphorbol Acetate - pharmacology; Human; Phosphorylation; Protein kinase C; Enzymatic activity; Enzyme; Molecular assembly; Oxidase; Neutrophil

The 47-kDa subunit of the NADPH oxidase system (p47-phox) of neutrophils undergoes an association with proteins in the Triton X-100-insoluble fraction upon stimulation of the cells with 4 beta-phorbol 12-myristate 13-acetate. This fraction contains the assembled oxidase that catalyzes the generation...