Compounds > vitamin-k-semiquinone-radical

vitamin-k-semiquinone-radical and 1-2-naphthoquinone

vitamin-k-semiquinone-radical has been researched along with 1-2-naphthoquinone* in 2 studies

Other Studies

2 other study(ies) available for vitamin-k-semiquinone-radical and 1-2-naphthoquinone

Article	Year
Scanning electrochemical microscopy of living cells: different redox activities of nonmetastatic and metastatic human breast cells. Proceedings of the National Academy of Sciences of the United States of America, 2000, Aug-29, Volume: 97, Issue:18 Electrochemical methods have been widely used to monitor physiologically important molecules in biological systems. This report describes the first application of the scanning electrochemical microscope (SECM) to probe the redox activity of individual living cells. The possibilities of measuring the rate and investigating the pathway of transmembrane charge transfer are demonstrated. By this approach, significant differences are detected in the redox responses given by nonmotile, nontransformed human breast epithelial cells, breast cells with a high level of motility (engendered by overexpression of protein kinase Calpha), and highly metastatic breast cancer cells. SECM analysis of the three cell lines reveals reproducible differences with respect to the kinetics of charge transfer by several redox mediators. Topics: Animals; Breast; Breast Neoplasms; Cattle; Cell Line; Cell Membrane; Cell Movement; Cells, Immobilized; Electrochemistry; Epithelial Cells; Female; Humans; Isoenzymes; Microscopy, Electron, Scanning; Naphthoquinones; Neoplasm Metastasis; Oxidation-Reduction; Protein Kinase C; Protein Kinase C-alpha; Transfection; Tumor Cells, Cultured; Vitamin K	2000
Stimulation of tyrosine-specific protein phosphorylation in the rat liver plasma membrane by oxygen radicals. Biochemical and biophysical research communications, 1986, Sep-14, Volume: 139, Issue:2 Incorporation of 32P from [gamma-32P]ATP into endogenous proteins, added histone and the copolymers Glu 80 Tyr 20 by rat liver plasma membranes was markedly increased by several naphthoquinones, including menadione. This stimulation was most marked with Glu 80 Tyr 20, has an absolute requirement for either dithiothreitol or reduced glutathione, and was inhibited by superoxide dismutase, catalase, and desferrioxamine to varying degrees depending on the quinones used. Their effectiveness in stimulating the apparent tyrosine-specific protein phosphorylation correlated with the rates of DTT-dependent redox cycling measured by oxygen consumption. Increased protein phosphorylation was also seen with particulate fractions isolated from hepatocytes incubated with quinones. A free radical-mediated mechanism is suggested for the quinone stimulation of protein phosphorylation. Topics: Adenosine Triphosphate; Animals; Benzoquinones; Cell Membrane; Deferoxamine; Free Radicals; Hydroquinones; Liver; Naphthoquinones; Oxidation-Reduction; Oxygen; Oxygen Consumption; Protein-Tyrosine Kinases; Quinones; Rats; Structure-Activity Relationship; Superoxide Dismutase; Vitamin K	1986

Article

Year

Scanning electrochemical microscopy of living cells: different redox activities of nonmetastatic and metastatic human breast cells.

Proceedings of the National Academy of Sciences of the United States of America, 2000, Aug-29, Volume: 97, Issue:18

Electrochemical methods have been widely used to monitor physiologically important molecules in biological systems. This report describes the first application of the scanning electrochemical microscope (SECM) to probe the redox activity of individual living cells. The possibilities of measuring the rate and investigating the pathway of transmembrane charge transfer are demonstrated. By this approach, significant differences are detected in the redox responses given by nonmotile, nontransformed human breast epithelial cells, breast cells with a high level of motility (engendered by overexpression of protein kinase Calpha), and highly metastatic breast cancer cells. SECM analysis of the three cell lines reveals reproducible differences with respect to the kinetics of charge transfer by several redox mediators.

Topics: Animals; Breast; Breast Neoplasms; Cattle; Cell Line; Cell Membrane; Cell Movement; Cells, Immobilized; Electrochemistry; Epithelial Cells; Female; Humans; Isoenzymes; Microscopy, Electron, Scanning; Naphthoquinones; Neoplasm Metastasis; Oxidation-Reduction; Protein Kinase C; Protein Kinase C-alpha; Transfection; Tumor Cells, Cultured; Vitamin K

2000

Stimulation of tyrosine-specific protein phosphorylation in the rat liver plasma membrane by oxygen radicals.

Biochemical and biophysical research communications, 1986, Sep-14, Volume: 139, Issue:2

Incorporation of 32P from [gamma-32P]ATP into endogenous proteins, added histone and the copolymers Glu 80 Tyr 20 by rat liver plasma membranes was markedly increased by several naphthoquinones, including menadione. This stimulation was most marked with Glu 80 Tyr 20, has an absolute requirement for either dithiothreitol or reduced glutathione, and was inhibited by superoxide dismutase, catalase, and desferrioxamine to varying degrees depending on the quinones used. Their effectiveness in stimulating the apparent tyrosine-specific protein phosphorylation correlated with the rates of DTT-dependent redox cycling measured by oxygen consumption. Increased protein phosphorylation was also seen with particulate fractions isolated from hepatocytes incubated with quinones. A free radical-mediated mechanism is suggested for the quinone stimulation of protein phosphorylation.

Topics: Adenosine Triphosphate; Animals; Benzoquinones; Cell Membrane; Deferoxamine; Free Radicals; Hydroquinones; Liver; Naphthoquinones; Oxidation-Reduction; Oxygen; Oxygen Consumption; Protein-Tyrosine Kinases; Quinones; Rats; Structure-Activity Relationship; Superoxide Dismutase; Vitamin K

1986