Respiratory burst in adherent human neutrophils: triggering by colony- stimulating factors CSF-GM and CSF-G

Nathan, C F

doi:10.1182/blood.v73.1.301.301

Cited by 193 publications

(35 citation statements)

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“…This series of micrographs was collected at 10 min intervals of time. The time scale of these observations match the 15-90 min required to trigger the oxidase of adherent neutrophils (Nathan, 1987(Nathan, , 1989. As these micrographs show, the level of NAD(P)H-associated autofluorescence varies greatly in the vicinity of phagosornes.…”

Section: Antibody-dependent Phagocytosis Triggers Largesupporting

confidence: 58%

Imaging neutrophil activation: Analysis of the translocation and utilization of NAD(P)H‐associated autofluorescence during antibody‐dependent target oxidation

Bing

Petty

1992

Journal Cellular Physiology

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Fluorescence intensified/enhanced microscopy has been used to study the metabolic activation of living human neutrophils in time-lapse sequences. The autofluorescence associated with NAD(P)H's emission band was studied within individual quiescent and stimulated cells. Excitation of NAD(P)H-associated autofluorescence was provided by a high-intensity Hg-vapor lamp. The background-subtracted autofluorescence signals were computer enhanced. In some cases the ratio image of NAD(P)H-associated autofluorescence to tetramethyl-rhodamine methyl ester (TRME) fluorescence, which was found to be uniformly distributed within neutrophils, was calculated to normalize autofluorescence intensities for cell thickness. Activation of the NADPH oxidase by phorbol myristate acetate, F-, N-formyl-methionyl-leucyl-phenylalanine (FMLP), or tumor necrosis factor (TNF) dramatically reduced autofluorescence levels. Membrane solubilization with sodium dodecyl sulfate eliminated autofluorescence. Thus, control experiments indicated that most or all of the detectable NAD(P)H-associated autofluorescence was due to NAD(P)H, consistent with previous non-microscopic studies. To understand the metabolic events surrounding the internalization and oxidative destruction of targets, we have imaged the NAD(P)H-associated autofluorescence of neutrophils and the Soret band of antibody coated target erythrocytes during cell-mediated cytotoxicity. Absorption contrast microscopy of the erythrocyte's Soret band is an especially sensitive indicator of the entry of reactive oxygen metabolites into this target's cytosol. Thus, it is possible to spectroscopically dissect and image the substrate (NADPH) and product (O2-) reactions of the NADPH oxidase in living unlabeled neutrophils. During real-time experiments at 37 degrees C, the level of NAD(P)H-associated autofluorescence surrounding phagosomes greatly increases before the disappearance of the target's Soret band. NAD(P)H-associated autofluorescence in the vicinity of phagocytosed erythrocytes is greatly diminished after target oxidation. This suggests that NAD(P)H is translocated to the vicinity of phagosomes prior to the oxidation of targets. The apparent cytosolic redistribution of NAD(P)H was confirmed by ratio imaging microscopy to control for cell thickness. We suggest that NADPH including its sources and/or carriers accumulate near phagosomes prior to target oxidation and that local NADPH molecules are consumed during target oxidation.

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Section: Antibody-dependent Phagocytosis Triggers Largesupporting

confidence: 58%

Imaging neutrophil activation: Analysis of the translocation and utilization of NAD(P)H‐associated autofluorescence during antibody‐dependent target oxidation

Bing

Petty

1992

Journal Cellular Physiology

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“…rhG-CSF is known to influence neutrophil function at several stages of development; it shortens bone marrow transit time, primes neutrophil respiratory burst, enhances superoxide production, up-regulates surface expression of CD11b/CD18 and induces shedding of CD62L (13)(14)(15). The animals in our study developed a neutrophilia proportional to the dosage of rhG-CSF given.…”

Section: Discussionmentioning

confidence: 60%

Efficacy of recombinant granulocyte colony-stimulating factor (rhG-CSF) in experimental colitis

Hommes¹,

Meenan²,

Dijkhuizen

et al. 1996

Clinical and Experimental Immunology

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SUMMARYInflammatory bowel disease is associated with mucosal neutrophil recruitment and activatation, mediated in part by arachidonic acid metabolites. G-CSF attenuates the immune response to sepsis and ameliorates glycogen storage disease Ib-related colitis. These actions may be effected through the shedding of neutrophil adhesion molecules, or inhibition of proinflammatory mediator synthesis. Immune complex colitis was used to evaluate the effect of rhG-CSF on colonic mucosal inflammation, neutrophil recruitment and the generation of eicosanoids. Immune complex colitis was induced in White New Zealand rabbits. Animals were pretreated with rhG-CSF either 24 h before induction, or at induction, with dosages of 50 and 200 g/kg. rhG-CSF caused a time-and dose-dependent neutrophilia in all animals. Pretreatment with rhG-CSF resulted in increased tissue myeloperoxidase levels, despite a histologically similar mucosal polymorphonuclear cell infiltrate between treated and control colitis groups. Leukotriene B 4 (LTB 4 ) and thromboxane B 2 (TXB 2 ) dialysis fluid levels were lower in treated animals, in particular in the groups receiving two doses (LTB 4 : both P < 0 : 01; TXB 2 : both P < 0 : 01. Prostaglandin E 2 (PGE 2 ) levels in dialysis fluid of the rhG-CSF-treated animals showed no difference from controls. In this model of experimental colitis, high-dose therapy with G-CSF resulted in a marked decrease of proinflammatory mediators, but mucosal generation of the protective PGE 2 was preserved. These results suggest that prolonged high-dose therapy with G-CSF may have anti-inflammatory effects in colitis.

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“…In spite of the large number of studies concerning the transduction pathways involved in phagocytic-cell activation , a possible role of reactive oxyge n intermediates has not been exhaustively examined . Since stimulation of phagocytic cells by different agonists , such as chemotactic peptides [36], colony-stimulating factors [40], tumor necrosis factor [15], and immune complexes [10] are associated with the activation of the NADPH oxidase , it may be speculated that respiratory burstdependent mechanisms could be involved in neutrophil activation induced by these stimuli .…”

Section: Discussionmentioning

confidence: 99%

Neutrophil Erythrotoxicity Induced by Phorbol Myristate Acetate: Mechanisms Involved in Neutrophil Activation

Geffner

Fontán

Sordelli

et al. 1991

Journal of Leukocyte Biology

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The capacity of phorbol myristate acetate (PMA) to prime neutrophil cytotoxic responses induced by a second stimulus was investigated. Treatment of neutrophils with low concentrations of PMA (0.2-0.5 ng/ml) for 18 hr at 37 degrees C markedly enhanced cytotoxicity triggered by Ca2+ ionophore A23187, N-formyl-methionyl-leucyl-phenylalanine (FMLP) and PMA. Pretreatment with PMA also enabled neutrophils to mediate significant cytotoxicity when triggered by platelet-activating factor (PAF), a stimulus unable to induce untreated cells to display cytotoxicity. Conversely, neutrophil cytotoxicity triggered by immune complexes (IC) was not modified by PMA treatment, whereas cytolytic activity of neutrophils against antibody-sensitized target cells was significantly increased. Treatment with PMA concentrations higher than 1 ng/ml directly triggered neutrophil cytotoxicity. Interestingly, we found that PMA-triggered neutrophils were able to sustain maximal levels of cytotoxicity for at least 8 hr after stimulation. With regard to the mechanisms involved in neutrophil activation by PMA, we found that catalase but not superoxide dismutase (SOD) prevented neutrophil activation measured as 1) induction of cytotoxic responses, 2) increase of neutrophil adhesiveness to cell-free surfaces, and 3) inhibition of chemotactic responses to FMLP. These findings suggest that H2O2 may play a major role in neutrophil activation induced by PMA.

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Respiratory burst in adherent human neutrophils: triggering by colony- stimulating factors CSF-GM and CSF-G

Cited by 193 publications

References 0 publications

Imaging neutrophil activation: Analysis of the translocation and utilization of NAD(P)H‐associated autofluorescence during antibody‐dependent target oxidation

Imaging neutrophil activation: Analysis of the translocation and utilization of NAD(P)H‐associated autofluorescence during antibody‐dependent target oxidation

Efficacy of recombinant granulocyte colony-stimulating factor (rhG-CSF) in experimental colitis

Neutrophil Erythrotoxicity Induced by Phorbol Myristate Acetate: Mechanisms Involved in Neutrophil Activation

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