Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system.

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Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system.

Sonicates from unstimulated human neutrophils produce no measurable superoxide since the superoxide-generating enzyme, NADPH oxidase, is inactive in these preparations. Previous attempts to activate the oxidase in disrupted cells with conventional neutrophil stimuli have been unsuccessful. This report describes a cell-free system in which arachidonic acid (82 microM) was able to activate supero...

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Inhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine dinucleotide phosphate.

Rat liver NAD kinase (ATP : NAD 2’-phosphotransferase, EC 2.7.1.23) was purified about 70-fold. The MichaelisMenten constants (Km) for NAD and ATP were 8 x 10e4 M and 2 x low3 M, respectively. NAD kinase activity was markedly inhibited by NADH and also NADPH. The Ki of NADH was approximately 1 X 10q4 M, and that of NADPH was approximately 5 X 10M5 M. Both inhibitions were competitive with NAD, ...

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Activation of the human neutrophil nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase by protein kinase C.

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Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1.

Galectins are a group of lactose-binding proteins widely distributed in nature. Twelve mammalian galectins have so far been identified, but their functions are to a large extent unknown. In this work we study galectin-1 in its interaction with human neutrophils, with regard to both cell surface binding and activation of the superoxide-producing NADPH-oxidase. We show that galectin-1 is able to ...

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ژورنال

عنوان ژورنال: Journal of Clinical Investigation

سال: 1985

ISSN: 0021-9738

DOI: 10.1172/jci111885