The respiratory burst oxidase

&NA; 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.

[1]  A. Monaco,et al.  Cloning the gene for an inherited human disorder—chronic granulomatous disease—on the basis of its chromosomal location , 1986, Nature.

[2]  J. Curnutte,et al.  Activation of neutrophil NADPH oxidase in a cell-free system. Partial purification of components and characterization of the activation process. , 1987, The Journal of biological chemistry.

[3]  P. Andrews,et al.  A possible role for protein phosphorylation in the activation of the respiratory burst in human neutrophils. Evidence from studies with cells from patients with chronic granulomatous disease. , 1986, The Journal of biological chemistry.

[4]  A. Segal,et al.  Stimulated neutrophils from patients with autosomal recessive chronic granulomatous disease fail to phosphorylate a Mr-44,000 protein , 1985, Nature.

[5]  P. Bellavite,et al.  The cytochrome b and flavin content and properties of the O2- -forming NADPH oxidase solubilized from activated neutrophils. , 1983, Biochimica et biophysica acta.

[6]  B. Babior,et al.  Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. , 1973, The Journal of clinical investigation.

[7]  A. Segal,et al.  Cytochrome b-245 from human neutrophils is a glycoprotein. , 1985, The Biochemical journal.

[8]  K. Kakinuma,et al.  Electron spin resonance studies on a flavoprotein in neutrophil plasma membranes. Redox potentials of the flavin and its participation in NADPH oxidase. , 1986, The Journal of biological chemistry.

[9]  H. Hattori.  Studies on the labile, stable Nadi oxidase and peroxidase staining reactions in the isolated particles of horse granulocyte. , 1961, Nagoya journal of medical science.

[10]  E. Goetzl,et al.  Structural and catalytic properties of the solubilized superoxide-generating activity of human polymorphonuclear leukocytes. Solubilization, stabilization in solution, and partial characterization. , 1979, Biochemistry.

[11]  J. Cox,et al.  Activation of the human neutrophil nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase by protein kinase C. , 1985, The Journal of clinical investigation.

[12]  W. Nauseef,et al.  NADPH oxidase of human neutrophils. Subcellular localization and characterization of an arachidonate-activatable superoxide-generating system. , 1987, The Journal of biological chemistry.

[13]  A. Fauci,et al.  B cell lines as models for inherited phagocytic diseases: abnormal superoxide generation in chronic granulomatous disease and giant granules in Chediak-Higashi syndrome. , 1984, Journal of immunology.

[14]  J. Parkinson,et al.  Mechanism of the superoxide-producing oxidase of neutrophils. O2 is necessary for the fast reduction of cytochrome b-245 by NADPH. , 1985, The Biochemical journal.

[15]  R. Lutter,et al.  Purification and partial characterization of the b-type cytochrome from human polymorphonuclear leukocytes. , 1985, The Journal of biological chemistry.

[16]  K. Takeshige,et al.  NADPH binding component of neutrophil superoxide-generating oxidase. , 1986, The Journal of biological chemistry.

[17]  J. A. Badwey,et al.  Active oxygen species and the functions of phagocytic leukocytes. , 1980, Annual review of biochemistry.

[18]  A. Segal,et al.  ABSENCE OF A NEWLY DESCRIBED CYTOCHROME b FROM NEUTROPHILS OF PATIENTS WITH CHRONIC GRANULOMATOUS DISEASE , 1978, The Lancet.

[19]  B. Babior,et al.  Superoxide-forming enzyme from human neutrophils: evidence for a flavin requirement. , 1977, Blood.

[20]  A. Segal.  Absence of both cytochrome b−245 subunits from neutrophils in X-linked chronic granulomatous disease , 1987, Nature.

[21]  R. S. Kipnes,et al.  Solubilization of the O2(-)-forming activity responsible for the respiratory burst in human neutrophils. , 1978, The Journal of biological chemistry.

[22]  J. T. Santinga,et al.  Functional relationship of the cytochrome b to the superoxide-generating oxidase of human neutrophils. , 1982, The Journal of biological chemistry.

[23]  C. Walsh,et al.  Characteristics of the cofactor requirements for the superoxide-generating NADPH oxidase of human polymorphonuclear leukocytes. , 1981, Biochemistry.

[24]  J. Parkinson,et al.  The superoxide-generating oxidase of leucocytes. NADPH-dependent reduction of flavin and cytochrome b in solubilized preparations. , 1984, The Biochemical journal.

[25]  A. Segal,et al.  Oxidation-reduction properties of the cytochrome b found in the plasma-membrane fraction of human neutrophils. A possible oxidase in the respiratory burst. , 1981, The Biochemical journal.