Hexose-Monophosphate Shunt

2011 ◽  
Keyword(s):  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt

Cytoplasmic pH regulation in phorbol ester-activated human neutrophils

1986 ◽  
Vol 251 (1) ◽  
pp. C55-C65 ◽  
Author(s):  
S. Grinstein ◽  
W. Furuya
Keyword(s):  
Metabolic Pathways ◽  
Phorbol Esters ◽  
Ph Regulation ◽  
Human Neutrophils ◽  
Hexose Monophosphate ◽  
Cytoplasmic Ph ◽  
Extracellular Acidification ◽  
Hexose Monophosphate Shunt ◽  
Activated Neutrophils ◽  
Cytoplasmic Acidification

Activation of neutrophils by 12-O-tetradecanoylphorbol-13-acetate (TPA) is accompanied by an initial cytoplasmic acidification, followed by an alkalinizing phase due to Na+-H+ countertransport. The source of the acidification, which is fully expressed by activation with TPA in Na+-free or amiloride-containing media, was investigated. The acidification phase was detected also in degranulated and enucleated cytoplasts, ruling out a major contribution by the nucleus or secretory vesicles. Cytoplasmic acidification was found to be associated with an extracellular acidification, suggesting metabolic generation of H+. Two principal metabolic pathways are stimulated in activated neutrophils: the reduction of O2 by NADPH-oxidase and the hexose monophosphate shunt. A good correlation was found between the activity of these pathways and the changes in cytoplasmic pH. Inhibition of superoxide synthesis prevented the TPA-induced cytoplasmic acidification. Moreover, activation of the hexose monophosphate shunt with permeable NADPH-oxidizing agents (in the absence of TPA) also produced a cytoplasmic acidification. Cytoplasmic acidification was also elicited by exogenous diacylglycerol and by other beta-phorbol diesters, which are activators of the kinase, but not by unesterified phorbol or by alpha-phorbol diesters, which are biologically inactive. The results suggest that the cytoplasmic acidification induced by phorbol esters in neutrophils reflects accumulation of H+ liberated during the metabolic burst that follows activation.

Oxidized polyamine-induced inhibition of hexose-monophosphate shunt activity of phagocytosing human polymorphonuclear leucocytes

1982 ◽  
Vol 4 (4) ◽  
pp. 322
Author(s):  
A. Ferrante ◽  
V.O. Rencis ◽  
G.M. Maxwell ◽  
A.C. Allison
Keyword(s):  
Polymorphonuclear Leucocytes ◽  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt

Evidence for an apical membrane effect in the regulation of the hexose monophosphate shunt pathway in toad bladder studies with amiloride

1974 ◽  
Vol 332 (3) ◽  
pp. 350-357 ◽  
Author(s):  
Barbara Beckman ◽  
Beat Guertler ◽  
Rebecca Leaf ◽  
Patricia Witkum ◽  
Geoffrey W.G. Sharp
Keyword(s):  
Apical Membrane ◽  
Toad Bladder ◽  
Hexose Monophosphate ◽  
Shunt Pathway ◽  
Hexose Monophosphate Shunt ◽  
Membrane Effect

31P-Nuclear Magnetic Resonance Evidence of an Activated Hexose-Monophosphate Shunt in Hyperglycemic Rat Lenses In Vivo

Diabetes ◽  
1995 ◽  
Vol 44 (7) ◽  
pp. 810-815 ◽  
Author(s):  
B. S. Szwergold ◽  
S. Lal ◽  
A. H. Taylor ◽  
F. Kappler ◽  
B. Su ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt ◽  
31P Nuclear Magnetic Resonance ◽  
Nuclear Magnetic

Evaluation of hexose monophosphate shunt activity and NBT dye test in both healthy and infected neonates

1974 ◽  
Vol 84 (6) ◽  
pp. 908 ◽  
Author(s):  
D.C. Anderson ◽  
L.K. Pickering ◽  
R.D. Feigin
Keyword(s):  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt

scholarly journals Macrophage variants in oxygen metabolism.

1980 ◽  
Vol 152 (4) ◽  
pp. 808-822 ◽  
Author(s):  
G Damiani ◽  
C Kiyotaki ◽  
W Soeller ◽  
M Sasada ◽  
J Peisach ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cytochrome C ◽  
Superoxide Anion ◽  
Oxygen Metabolism ◽  
Hexose Monophosphate ◽  
Phagocytic Cells ◽  
Form Complex ◽  
Hexose Monophosphate Shunt ◽  
Cytochrome C Reduction ◽  
Generate Superoxide Anion

Whereas phagocytic cells from normal individuals have the capacity to kill ingested bacteria and parasites, those from patients with several uncommon genetic deficiency diseases are known to be defective in bactericidal activity. Studies on neutrophils of these patients have revealed fundamental defects in their ability to reduce molecular oxygen and metabolize it to superoxide anion, hydrogen peroxide, and oxygen radicals. In the present experiments, we describe a clone of a continuous murine macrophage-like cell line, J774.16, that, upon appropriate stimulation, activates the hexose monophosphate shunt, and produces superoxide anion and hydrogen peroxide. With nitroblue tetrazolium to select against cells capable of being stimulated by phorbol myristate acetate to reduce the dye to polymer--formazan--which is toxic fot cells, we have selected for variants that are defective in oxygen metabolism. Four of these subclones have been characterized and found to be lacking in the ability (a) to generate superoxide anion, as measured by cytochrome c reduction; (b) to produce hydrogen peroxide, as measured by the ability to form complex I with cytochrome c peroxidase; and (c) to be stimulated to oxidize glucose via the hexose monophosphate shunt. These variants appear to represent a useful model for studying the molecular basis for macrophage cytocidal activity.

Activities of selected antioxidative, hydrolytic and hexose monophosphate shunt enzymes of skeletal muscle in neuromuscular diseases

2009 ◽  
Vol 69 (S98) ◽  
pp. 176-177
Author(s):  
V. V. Myllylä ◽  
T. E. S. Takala ◽  
U. Tolonen ◽  
A. Salminen ◽  
M. Kihlström ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Neuromuscular Diseases ◽  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt

scholarly journals Function of H2O2, Myeloperoxidase, and Hexose Monophosphate Shunt Enzymes in Phagocytizing Cells from Different Species 1

1970 ◽  
Vol 1 (4) ◽  
pp. 338-344 ◽  
Author(s):  
B. B. Paul ◽  
R. R. Strauss ◽  
A. A. Jacobs ◽  
A. J. Sbarra
Keyword(s):  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt
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