NADPH AND NADH OXIDATION BY GUINEA PIG POLYMORPHONUCLEAR LEUCOCYTES

1963 ◽  
Vol 41 (1) ◽  
pp. 427-434 ◽  
Author(s):  
G. Y. N. Iyer ◽  
J. H. Quastel
Keyword(s):  
Hydrogen Peroxide ◽  
Guinea Pig ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Enzyme System ◽  
Polymorphonuclear Leucocytes ◽  
Hexose Monophosphate ◽  
Manganese Ions ◽  
Hexose Monophosphate Pathway ◽  
Stimulation Of

A homogenate of guinea pig polymorphonuclear leucocytes contains an enzyme system capable of oxidizing, in presence of oxygen, NADPH and NADH with the formation of hydrogen peroxide. The enzyme is much more active towards NADPH than to NADH. The presence of manganese ions strongly enhances the oxidase activity. It is suggested that the release of the NADPH oxidase in the leucocytes, during phagocytosis, accounts for the stimulation of the hexose monophosphate pathway that occurs in phagocytosis.

NADPH AND NADH OXIDATION BY GUINEA PIG POLYMORPHONUCLEAR LEUCOCYTES

1963 ◽  
Vol 41 (2) ◽  
pp. 427-434 ◽  
Author(s):  
G. Y. N. Iyer ◽  
J. H. Quastel
Keyword(s):  
Hydrogen Peroxide ◽  
Guinea Pig ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Enzyme System ◽  
Polymorphonuclear Leucocytes ◽  
Hexose Monophosphate ◽  
Manganese Ions ◽  
Hexose Monophosphate Pathway ◽  
Stimulation Of

A homogenate of guinea pig polymorphonuclear leucocytes contains an enzyme system capable of oxidizing, in presence of oxygen, NADPH and NADH with the formation of hydrogen peroxide. The enzyme is much more active towards NADPH than to NADH. The presence of manganese ions strongly enhances the oxidase activity. It is suggested that the release of the NADPH oxidase in the leucocytes, during phagocytosis, accounts for the stimulation of the hexose monophosphate pathway that occurs in phagocytosis.

scholarly journals NADPH Oxidase-dependent Oxidation and Externalization of Phosphatidylserine during Apoptosis in Me2SO-differentiated HL-60 Cells

2002 ◽  
Vol 277 (51) ◽  
pp. 49965-49975 ◽  
Author(s):  
Antonio Arroyo ◽  
Martin Modrianský ◽  
F. Behice Serinkan ◽  
Rosario I. Bello ◽  
Tatsuya Matsura ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Nadph Oxidase ◽  
Phorbol Myristate Acetate ◽  
Oxidase Activity ◽  
Caspase 3 ◽  
Myristate Acetate ◽  
Phosphatidylserine Externalization ◽  
Activated Neutrophils ◽  
Stimulation Of

Resolution of inflammation requires clearance of activated neutrophils by phagocytes in a manner that protects adjacent tissues from injury. Mechanisms governing apoptosis and clearance of activated neutrophils from inflamed areas are still poorly understood. We used dimethylsulfoxide-differentiated HL-60 cells showing inducible oxidase activity to study NADPH oxidase-induced apoptosis pathways typical of neutrophils. Activation of the NADPH oxidase by phorbol myristate acetate caused oxidative stress as shown by production of superoxide and hydrogen peroxide, depletion of intracellular glutathione, and peroxidation of all three major classes of membrane phospholipids, phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine. In addition, phorbol myristate acetate stimulation of the NADPH oxidase caused apoptosis, as evidenced by apoptosis-specific phosphatidylserine externalization, increased caspase-3 activity, chromatin condensation, and nuclear fragmentation. Furthermore, phorbol myristate acetate stimulation of the NADPH oxidase caused recognition and ingestion of dimethylsulfoxide-differentiated HL-60 cells by J774A.1 macrophages. To reveal the apoptosis-related component of oxidative stress in the phorbol myristate acetate-induced response, we pretreated cells with a pancaspase inhibitor, benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (z-VAD-fmk), and found that it caused partial inhibition of hydrogen peroxide formation as well as selective protection of only phosphatidylserine, whereas more abundant phospholipids, phosphatidylcholine and phosphatidylethanolamine, were oxidized to the same extent in the absence or presence of z-VAD-fmk. In contrast, inhibitors of NADPH oxidase activity, diphenylene iodonium and staurosporine, as well as antioxidant enzymes, superoxide dismutase/catalase, completely protected all phospholipids against peroxidation, inhibited expression of apoptotic biomarkers and externalization of phosphatidylserine, and reduced phagocytosis of differentiated HL-60 cells by J774A.1 macrophages. Similarly, zymosan-induced activation of the NADPH oxidase resulted in the production of superoxide and oxidation of different classes of phospholipids of which only phosphatidylserine was protected by z-VAD-fmk. Accordingly, zymosan caused apoptosis in differentiated HL-60 cells, as evidenced by caspase-3 activation and phosphatidylserine externalization. Finally, zymosan triggered caspase-3 activation and extensive SOD/catalase-inhibitable phosphatidylserine exposure in human neutrophils. Overall, our results indicate that NADPH oxidase-induced oxidative stress in neutrophil-like cells triggers apoptosis and subsequent recognition and removal of these cells through pathways dependent on oxidation and externalization of phosphatidylserine.

scholarly journals Subplasmalemmal hydrogen peroxide triggers calcium influx in gonadotropes

2018 ◽  
Vol 293 (41) ◽  
pp. 16028-16042 ◽  
Author(s):  
An K. Dang ◽  
Nathan L. Chaplin ◽  
Dilyara A. Murtazina ◽  
Ulrich Boehm ◽  
Colin M. Clay ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Calcium Channels ◽  
Nadph Oxidase ◽  
Calcium Channel ◽  
Anterior Pituitary ◽  
Calcium Influx ◽  
Ros Generation ◽  
Primary Mouse ◽  
The Impact ◽  
Stimulation Of

Gonadotropin-releasing hormone (GnRH) stimulation of its eponymous receptor on the surface of endocrine anterior pituitary gonadotrope cells (gonadotropes) initiates multiple signaling cascades that culminate in the secretion of luteinizing and follicle-stimulating hormones, which have critical roles in fertility and reproduction. Enhanced luteinizing hormone biosynthesis, a necessary event for ovulation, requires a signaling pathway characterized by calcium influx through L-type calcium channels and subsequent activation of the mitogen-activated protein kinase extracellular signal-regulated kinase (ERK). We previously reported that highly localized subplasmalemmal calcium microdomains produced by L-type calcium channels (calcium sparklets) play an essential part in GnRH-dependent ERK activation. Similar to calcium, reactive oxygen species (ROS) are ubiquitous intracellular signaling molecules whose subcellular localization determines their specificity. To investigate the potential influence of oxidant signaling in gonadotropes, here we examined the impact of ROS generation on L-type calcium channel function. Total internal reflection fluorescence (TIRF) microscopy revealed that GnRH induces spatially restricted sites of ROS generation in gonadotrope-derived αT3-1 cells. Furthermore, GnRH-dependent stimulation of L-type calcium channels required intracellular hydrogen peroxide signaling in these cells and in primary mouse gonadotropes. NADPH oxidase and mitochondrial ROS generation were each necessary for GnRH-mediated stimulation of L-type calcium channels. Congruently, GnRH increased oxidation within subplasmalemmal mitochondria, and L-type calcium channel activity correlated strongly with the presence of adjacent mitochondria. Collectively, our results provide compelling evidence that NADPH oxidase activity and mitochondria-derived hydrogen peroxide signaling play a fundamental role in GnRH-dependent stimulation of L-type calcium channels in anterior pituitary gonadotropes.

scholarly journals Hsp90 Regulates NADPH Oxidase Activity and Is Necessary for Superoxide but Not Hydrogen Peroxide Production

2011 ◽  
Vol 14 (11) ◽  
pp. 2107-2119 ◽  
Author(s):  
Feng Chen ◽  
Deepesh Pandey ◽  
Ahmed Chadli ◽  
John D. Catravas ◽  
Teng Chen ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Hydrogen Peroxide Production ◽  
Nadph Oxidase Activity

scholarly journals Reactive Oxygen Intermediate-Dependent NF-κB Activation by Interleukin-1β Requires 5-Lipoxygenase or NADPH Oxidase Activity

1999 ◽  
Vol 19 (3) ◽  
pp. 1950-1960 ◽  
Author(s):  
Giuseppina Bonizzi ◽  
Jacques Piette ◽  
Sonia Schoonbroodt ◽  
Roland Greimers ◽  
Laurence Havard ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Reactive Oxygen ◽  
Lymphoid Cells ◽  
Interleukin 1Β ◽  
Oxygen Intermediates ◽  
Monocytic Cells ◽  
Nadph Oxidase Activity ◽  
Stimulation Of

ABSTRACT We previously reported that the role of reactive oxygen intermediates (ROIs) in NF-κB activation by proinflammatory cytokines was cell specific. However, the sources for ROIs in various cell types are yet to be determined and might include 5-lipoxygenase (5-LOX) and NADPH oxidase. 5-LOX and 5-LOX activating protein (FLAP) are coexpressed in lymphoid cells but not in monocytic or epithelial cells. Stimulation of lymphoid cells with interleukin-1β (IL-1β) led to ROI production and NF-κB activation, which could both be blocked by antioxidants or FLAP inhibitors, confirming that 5-LOX was the source of ROIs and was required for NF-κB activation in these cells. IL-1β stimulation of epithelial cells did not generate any ROIs and NF-κB induction was not influenced by 5-LOX inhibitors. However, reintroduction of a functional 5-LOX system in these cells allowed ROI production and 5-LOX-dependent NF-κB activation. In monocytic cells, IL-1β treatment led to a production of ROIs which is independent of the 5-LOX enzyme but requires the NADPH oxidase activity. This pathway involves the Rac1 and Cdc42 GTPases, two enzymes which are not required for NF-κB activation by IL-1β in epithelial cells. In conclusion, three different cell-specific pathways lead to NF-κB activation by IL-1β: a pathway dependent on ROI production by 5-LOX in lymphoid cells, an ROI- and 5-LOX-independent pathway in epithelial cells, and a pathway requiring ROI production by NADPH oxidase in monocytic cells.

The NADPH oxidase of guinea pig polymorphonuclear leucocytes

1983 ◽  
Vol 52 (1) ◽  
Author(s):  
Paolo Bellavite ◽  
MariaC. Serra ◽  
Anna Davoli ◽  
JoeV. Bannister ◽  
Filippo Rossi
Keyword(s):  
Guinea Pig ◽  
Nadph Oxidase ◽  
Polymorphonuclear Leucocytes
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