Activation of the NADPH oxidase in a cell-free system from human neutrophils stimulated by phorbol myristate acetate
- Kawasaki Medical School, Okayama (Japan)
Kinetics of activation of the NADPH oxidase in a fully soluble cell-free system from phorbol myristate acetate (PMA)-stimulated human neutrophils were investigated. In a cell-free system in which Mg{sup 2+} and sodium dodecyl sulfate, an anionic detergent required for the activation of NADPH oxidase are contained, cytosol prepared from PMA-stimulated neutrophils failed to activate PMA-stimulated neutrophil oxidase. However, cytosol prepared from resting (control) neutrophils was capable of activating PMA-stimulated neutrophil oxidase in a cell-free system in which its Km for NADPH was almost similar to that of control neutrophil oxidase. Cytosol from PMA-stimulated neutrophils could not activate control neutrophil oxidase, although it did not contain any inhibitors of NADPH oxidase activation. These results suggest that, in PMA-stimulated neutrophils, cytosolic activation factors may be consumed or exhausted, and that the affinity for NADPH of PMA-stimulated neutrophil oxidase may be the same as that of control neutrophil oxidase.
- OSTI ID:
- 6967648
- Journal Information:
- Life Sciences; (USA), Journal Name: Life Sciences; (USA) Vol. 46:16; ISSN 0024-3205; ISSN LIFSA
- Country of Publication:
- United States
- Language:
- English
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63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMALS
BIOLOGICAL EFFECTS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARCINOGENS
COENZYMES
ENZYME ACTIVITY
ENZYMES
ESTERS
LEUKOCYTES
MAMMALS
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NADP
NEUTROPHILS
NUCLEOTIDES
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PHORBOL ESTERS
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