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Article: The NADPH oxidase of endothelial cells.

Babior, B M

2000 Volume 50, Issue 4-5, Page(s) 267–269

Abstract: The best known NADPH oxidase is that of phagocytes-neutrophils and monocytes. In these cells, the enzyme manufactures large quantities of O2- and other reactive oxidants that are used for the purpose of killing invading microorganisms. Recent studies, ... ...

Abstract	The best known NADPH oxidase is that of phagocytes-neutrophils and monocytes. In these cells, the enzyme manufactures large quantities of O2- and other reactive oxidants that are used for the purpose of killing invading microorganisms. Recent studies, however, have suggested that a number of other tissues contain NADPH oxidases. In contrast to the very vigorous production of oxidants by phagocytes, rates of oxidant production by these other cell types are quite low. Oxidant production by these cells is generally thought to serve a signaling function.
MeSH term(s)	Animals ; Anticholesteremic Agents/pharmacology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/enzymology ; Endothelium, Vascular/metabolism ; Humans ; NADPH Oxidases/metabolism ; Phagocytes/enzymology ; Reactive Oxygen Species/metabolism ; Superoxides/metabolism
Chemical Substances	Anticholesteremic Agents ; Reactive Oxygen Species ; Superoxides (11062-77-4) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2000-10
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1080/713803730
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Article: Phagocytes and oxidative stress.

Babior, B M

The American journal of medicine

2000 Volume 109, Issue 1, Page(s) 33–44

Abstract: Neutrophils and other phagocytes manufacture O(2)(-) (superoxide) by the one-electron reduction of oxygen at the expense of NADPH. Most of the O(2)(-) reacts with itself to form H(2)O(2) (hydrogen peroxide). From these agents a large number of highly ... ...

Abstract	Neutrophils and other phagocytes manufacture O(2)(-) (superoxide) by the one-electron reduction of oxygen at the expense of NADPH. Most of the O(2)(-) reacts with itself to form H(2)O(2) (hydrogen peroxide). From these agents a large number of highly reactive microbicidal oxidants are formed, including HOCl (hypochlorous acid), which is produced by the myeloperoxidase-catalyzed oxidation of Cl(-) by H(2)O(2); OH() (hydroxyl radical), produced by the reduction of H(2)O(2) by Fe(++) or Cu(+); ONOO(-) (peroxynitrite), formed by the reaction between O(2)(-) and NO(); and many others. These reactive oxidants are manufactured for the purpose of killing invading microorganisms, but they also inflict damage on nearby tissues, and are thought to be of pathogenic significance in a large number of diseases. Included among these are emphysema, acute respiratory distress syndrome, atherosclerosis, reperfusion injury, malignancy and rheumatoid arthritis.
MeSH term(s)	Humans ; Nitric Oxide/metabolism ; Oxidants/metabolism ; Oxidative Stress/physiology ; Phagocytes/physiology ; Phagocytosis/physiology ; Superoxides/metabolism
Chemical Substances	Oxidants ; Superoxides (11062-77-4) ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2000-07
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	80015-6
ISSN	1555-7162 ; 1873-2178 ; 0002-9343 ; 1548-2766
ISSN (online)	1555-7162 ; 1873-2178
ISSN	0002-9343 ; 1548-2766
DOI	10.1016/s0002-9343(00)00481-2
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Article: Confidentiality.

Babior, B M

Current opinion in hematology

1999 Volume 6, Issue 1, Page(s) 1–2

MeSH term(s)	Biology ; Confidentiality ; Peer Review, Research
Language	English
Publishing date	1999-01
Publishing country	United States
Document type	Editorial
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/00062752-199901000-00001
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Article: NADPH oxidase: an update.

Babior, B M

Blood

1999 Volume 93, Issue 5, Page(s) 1464–1476

MeSH term(s)	Animals ; Enzyme Activation ; Humans ; Leukocytes/enzymology ; NADPH Oxidases/physiology ; Substrate Specificity
Chemical Substances	NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	1999-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
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Article: Familial Mediterranean fever and the control of inflammation.

Babior, B M

Current opinion in hematology

1998 Volume 5, Issue 1, Page(s) 1–2

MeSH term(s)	Cytoskeletal Proteins ; Familial Mediterranean Fever/enzymology ; Familial Mediterranean Fever/genetics ; Familial Mediterranean Fever/physiopathology ; Humans ; Inflammation/prevention & control ; Proteins/genetics ; Pyrin ; Serine Endopeptidases/genetics
Chemical Substances	Cytoskeletal Proteins ; MEFV protein, human ; Proteins ; Pyrin ; Serine Endopeptidases (EC 3.4.21.-)
Language	English
Publishing date	1998-01
Publishing country	United States
Document type	Editorial
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/00062752-199801000-00001
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Article: Superoxide: a two-edged sword.

Babior, B M

Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas

1997 Volume 30, Issue 2, Page(s) 141–155

Abstract: Superoxide (O2-) is the compound obtained when oxygen is reduced by one electron. For a molecule with an unpaired electron, O2- is surprisingly inert, its chief reaction being a dismutation in which it reacts with itself to form H2O2 and oxygen. The ... ...

Abstract	Superoxide (O2-) is the compound obtained when oxygen is reduced by one electron. For a molecule with an unpaired electron, O2- is surprisingly inert, its chief reaction being a dismutation in which it reacts with itself to form H2O2 and oxygen. The involvement of O2- in biological systems was first revealed by the discovery in 1969 of superoxide dismutase, an enzyme that catalyzes the dismutation of O2-. Since then it has been found that biological systems produce a bewildering variety of reactive oxidants, all but a few arising ultimately from O2-. These oxidants include O2- itself, H2O2 and alkyl peroxides, hydroxyl radical and other reactive oxidizing radicals, oxidized halogens and halamines, singlet oxygen, and peroxynitrite. These various oxidants are able to damage molecules in their environment, and are therefore very dangerous. They are thought to participate in the pathogenesis of a number of common diseases, including among others malignancy, by their ability to mutate the genome, and atherosclerosis, by their capacity for oxidizing lipoproteins. Their properties are put to good use, however, in host defense, where they serve as microbicidal and parasiticidal agents, and in biological signalling, where their liberation in small quantities results in redox-mediated changes in the functions of enzymes and other proteins.
MeSH term(s)	Animals ; Antioxidants/chemistry ; Antioxidants/metabolism ; Catalase/chemistry ; Male ; Oxidative Stress ; Superoxide Dismutase/chemistry ; Superoxides/chemistry
Chemical Substances	Antioxidants ; Superoxides (11062-77-4) ; Catalase (EC 1.11.1.6) ; Superoxide Dismutase (EC 1.15.1.1)
Language	English
Publishing date	1997-02
Publishing country	Brazil
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	786234-9
ISSN	0100-879X
ISSN	0100-879X
DOI	10.1590/s0100-879x1997000200001
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Article: The respiratory burst oxidase.

Babior, B M

Current opinion in hematology

1995 Volume 2, Issue 1, Page(s) 55–60

Abstract: ... B lymphocytes. Activation is accomplished by any number of signal transduction pathways, and involves ...

Abstract	The respiratory burst oxidase catalyzes the production of O2- by activated phagocytes and B lymphocytes. Activation is accomplished by any number of signal transduction pathways, and involves protein kinase C, MAP kinase, or both, and perhaps lipid-mediated pathways. Failure of O2- production is characteristic of chronic granulomatous disease, an inherited disorder of phagocyte function. A number of new mutations responsible for chronic granulomatous disease have been reported. O2- production is also altered in other diseases, most notably certain hematologic malignancies.
MeSH term(s)	Enzyme Activation ; Granulomatous Disease, Chronic/enzymology ; Humans ; NADH, NADPH Oxidoreductases/metabolism ; NADPH Oxidases ; Oxygen/blood
Chemical Substances	NADH, NADPH Oxidoreductases (EC 1.6.-) ; NADPH Oxidases (EC 1.6.3.-) ; superoxide-forming enzyme (EC 1.6.99.-) ; Oxygen (S88TT14065)
Language	English
Publishing date	1995-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/00062752-199502010-00008
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Article: Activation of the respiratory burst oxidase.

Babior, B M

Environmental health perspectives

1994 Volume 102 Suppl 10, Page(s) 53–56

Abstract: The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of oxygen ...

Abstract	The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of oxygen by NADPH to form O2-, the precursor of a group of reactive oxidants that are employed by phagocytes as microbicidal agents. The enzyme is active in stimulated cells but dominant in resting cells. It molecular weight guanine nucleotide-binding protein. The components p22phox and gp91phox from cytochrome b558, a flavohemoprotein that resides in the cortical cytoskeleton and in the membranes of the specific granules. The other components are found in the cytosol of resting cells, but migrate to the cortical cytoskeleton when the neutrophils are activated, where they assemble the active oxidase. Migration to the cortical cytoskeleton is caused in part by the appearance of a membrane binding site on one or more of the cytosolic subunits, possibly due to the phosphorylation of p47phox that takes place during cell activation.
MeSH term(s)	B-Lymphocytes/metabolism ; Cell Membrane/metabolism ; Cytosol/metabolism ; NADH, NADPH Oxidoreductases/physiology ; NADPH Oxidases ; Phagocytes/metabolism
Chemical Substances	NADH, NADPH Oxidoreductases (EC 1.6.-) ; NADPH Oxidases (EC 1.6.3.-) ; superoxide-forming enzyme (EC 1.6.99.-)
Language	English
Publishing date	1994-12
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	195189-0
ISSN	1552-9924 ; 0091-6765 ; 1078-0475
ISSN (online)	1552-9924
ISSN	0091-6765 ; 1078-0475
DOI	10.1289/ehp.94102s1053
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Article: Neutrophil function as related to neutrophil-endothelial cell interactions.

Babior, B M

Nouvelle revue francaise d'hematologie

1992 Volume 34 Suppl, Page(s) S29–35

Abstract: Advances have recently been made in several areas related to neutrophil-mediated tissue damage. Certain chemotactic receptors have been cloned, their relationship to G proteins examined, and their mechanisms of downregulation partly elucidated. ... ...

Abstract	Advances have recently been made in several areas related to neutrophil-mediated tissue damage. Certain chemotactic receptors have been cloned, their relationship to G proteins examined, and their mechanisms of downregulation partly elucidated. Downregulation of chemotactic receptors could be useful in controlling the damage inflicted by neutrophils on nearby tissues. Studies of neutrophil adhesion to endothelium have revealed two classes of adhesion proteins: selectins, and the integrin/integrin receptor system. Selectins are involved in neutrophil margination, while the integrin system participates in the egress of neutrophils into regions of inflammation. The microfilaments are strands of polymerized actin which form a network that pervades the neutrophil cytoplasm. On activation of the neutrophil, changes occur in the state of the microfilament network that appear to act in combination with the integrin/integrin receptor system to cause neutrophils to be retained in capillaries of tissues reperfused after hypoxia. To the extent that reperfusion injury is caused by these retained neutrophils, prevention of their effect may require measures directed at the microfilament network as well as the integrin/integrin receptor system. With regard to mechanisms of neutrophil-mediated tissue damage, recent studies have emphasized the extent to which oxidative systems interact with proteases to augment the damage inflicted by activated neutrophils. The unique efficacy of secretory leukoprotease in preventing neutrophil-mediated proteolysis is discussed.
MeSH term(s)	Actin Cytoskeleton/physiology ; Carbohydrate Sequence ; Cell Adhesion ; Cell Adhesion Molecules/physiology ; Chemotaxis, Leukocyte ; Endopeptidases/metabolism ; Endopeptidases/secretion ; Endothelium, Vascular/pathology ; Humans ; Integrins/physiology ; Molecular Sequence Data ; Neutrophils/enzymology ; Neutrophils/physiology ; Oxidation-Reduction ; Reactive Oxygen Species ; Receptors, Cell Surface/metabolism ; Reperfusion Injury/pathology ; Respiratory Burst
Chemical Substances	Cell Adhesion Molecules ; Integrins ; Reactive Oxygen Species ; Receptors, Cell Surface ; Endopeptidases (EC 3.4.-)
Language	English
Publishing date	1992
Publishing country	Germany
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	205332-9
ISSN	0029-4810
ISSN	0029-4810
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Article: The respiratory burst oxidase.

Babior, B M

Advances in enzymology and related areas of molecular biology

1992 Volume 65, Page(s) 49–95

Abstract: Sbarra and Karnovsky were the first to present evidence suggesting the presence in phagocytes of a special enzyme designed to generate reactive oxidants for purposes of host defense. In the years since their report appeared, a great deal has been learned ...

Abstract	Sbarra and Karnovsky were the first to present evidence suggesting the presence in phagocytes of a special enzyme designed to generate reactive oxidants for purposes of host defense. In the years since their report appeared, a great deal has been learned about this enzyme, now known as the respiratory burst oxidase. It has been found to be a plasma membrane-bound heme- and flavin-containing enzyme, dormant in resting cells, that catalyzes the one-electron reduction of oxygen to O2- at the expense of NADPH: O2 + NADPH----O2- + NADP+ + H+ Its behavior in whole cells and its response to various activating stimuli have been described in detail, although important insights continue to emerge, as for example a very interesting new series of observations on differences in oxidase activation patterns between suspended and adherent cells. The enzyme has been shown by biochemical and genetic studies to consist of at least six components. In the resting cell, three of these components are in the cytosol and three in the plasma membrane, but when the cell passes from its resting to its activated state the cytosolic components are all transferred to the plasma membrane, presumably assembling the oxidase. Of the components initially bound to the membrane, two constitute cytochrome b558, a heme protein characteristic of the respiratory burst oxidase, and the third may represent an oxidase flavoprotein. With regard to the cytosolic components, one is a phosphoprotein and another is the NADPH-binding component, possibly a second oxidase flavoprotein. The nature of the third (p67phox) is a puzzle. Four of the six oxidase components have now been cloned and sequenced. These findings only scratch the surface, however, and many questions remain. How many oxidase components, for example, remain to be discovered, and how do they fit together to form the active enzyme? How is the route of activation of the oxidase integrated into the general signal transduction systems of the cell? How did the oxidase come to be? Could there be a widespread system that generates small amounts of O2- as an intercellular signaling molecule, as recent work is beginning to suggest, and did the ever-destructive respiratory burst oxidase arise from that innocuous system as the creation of some evolutionary Frankenstein--an oxidase from hell? Finally, will it be possible to develop drugs that specifically block the respiratory burst oxidase, and will such drugs prove to be clinically useful as anti-inflammatory agents?(ABSTRACT TRUNCATED AT 400 WORDS)
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Membrane/enzymology ; Enzyme Activation ; Granulomatous Disease, Chronic/enzymology ; Humans ; Molecular Sequence Data ; Oxidoreductases/chemistry ; Oxidoreductases/isolation & purification ; Oxidoreductases/physiology ; Phagocytes/enzymology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Conformation ; Respiratory Burst/physiology
Chemical Substances	Phosphoproteins ; Oxidoreductases (EC 1.-)
Language	English
Publishing date	1992
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	27-9
ISSN	0065-258X
ISSN	0065-258X
DOI	10.1002/9780470123119.ch2
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