Document Detail


The respiratory burst of phagocytic cells: facts and problems.
MedLine Citation:
PMID:  6283827     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. The so called "soluble" oxidase(s) are not involved in the respiratory burst of guinea pig and human granulocytes and of guinea pig peritoneal resident and elicited macrophages. 2. The activation of the oxidation of NADPH by a membrane bound NAD(P)H oxidase is the main mechanism responsible for the activation of the respiration of phagocytes. 3. The oxidase is inactive in resting cells and the activated form works on the plasma membrane. 4. More than one mechanism is operative in the oxidation of NAD(P)H by cell free particles in vitro. These mechanisms vary in relation to the conditions of assay (pH and concentration of substrate). 5. Under optimal conditions in vitro the enzymatic oxidation of NADPH practically involves the univalent pathway of oxygen reduction with stoichiometry of two nanomoles of O2 formed for one nanomole of NADPH oxidized. 6. Also in intact cells all O2 is first univalently reduced to O2 and then discharged outside the cell or in the phagocytic vacuoles. 7. The main reactions involved in the O2 balance in intact cells are the univalent reduction of O2, the dismutation of O2 to H2O2 and the degradation of the peroxide through catalatic and peroxidatic mechanisms. 8. The total oxygen univalently reduced by the activated oxidase is 2-4 folds the net oxygen consumed by the cells, depending on the mechanism of H2O2 degradation. 9. All the rate of extrarespiration is accounted for by the rate of oxidation of physiological concentration of NADPH by the membrane-bound enzyme. This adequacy can be observed only under appropriate experimental conditions, because the high activity of the oxidase is not a permanent state.
Authors:
F Rossi; P Bellavite; G Berton; P Dri; G Zabucchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Advances in experimental medicine and biology     Volume:  141     ISSN:  0065-2598     ISO Abbreviation:  Adv. Exp. Med. Biol.     Publication Date:  1982  
Date Detail:
Created Date:  1982-08-14     Completed Date:  1982-08-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0121103     Medline TA:  Adv Exp Med Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  283-322     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Compartmentation
Cytochrome c Group / metabolism
Granulocytes / enzymology
Guinea Pigs
Humans
Kinetics
Macrophages / enzymology,  physiology
NADH, NADPH Oxidoreductases / metabolism
Oxygen / metabolism
Oxygen Consumption
Peroxidase / metabolism
Phagocytes / enzymology,  physiology*
Chemical
Reg. No./Substance:
0/Cytochrome c Group; 7782-44-7/Oxygen; EC 1.11.1.7/Peroxidase; EC 1.6.-/NADH, NADPH Oxidoreductases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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