Plasma membrane and phagosome localisation of the activated NADPH oxidase in elicited peritoneal macrophages of the guinea-pig

1982 ◽  
Vol 136 (3) ◽  
pp. 241-252 ◽  
Author(s):  
Giorgio Berton ◽  
Paolo Bellavite ◽  
Guiseppina de Nicola ◽  
Pietro Dri ◽  
Filippo Rossi
1973 ◽  
Vol 21 (5) ◽  
pp. 488-498 ◽  
Author(s):  
R. E. POELMANN ◽  
W. T. DAEMS ◽  
E. J. VAN LOHUIZEN

This cytochemical and electron microscopic study on peritoneal macrophages of the guinea pig has raised doubts concerning the validity of lead methods for the demonstration of plasma membrane-bound adenosine triphosphatase activity. The problems encountered are inherent in the use of lead ions as a capture reagent. The nonenzymatically formed precipitates reflect sites of heterogeneous nucleation specific for certain kinds of cells, e.g., resident peritoneal macrophages, eosinophilic granulocytes and, to a lesser degree, exudate monocytes. This type of precipitation is also catalyzed on the surface of nonbiologic matrices such as latex particles. Enzymatic processes may well occur, but they cannot be distinguished from nonenzymatic processes.


1981 ◽  
Vol 91 (1) ◽  
pp. 221-226 ◽  
Author(s):  
M C Pike ◽  
R Snyderman

Chemotactic factors have been shown to inhibit the methylation of phosphatidylethanolamine in macrophages without affecting total phospholipid synthesis. It would thus be anticipated that newly synthesized membranes of macrophages exposed to chemoattractants would have an increased ratio of phosphatidylethanolamine to its methylated derivatives. These ratios were measured directly in newly synthesized phospholipids of plasma membranes isolated from guinea pig peritoneal macrophages. The phosphatidylethanolamine: methylated phospholipid ratio in such plasma membranes was increased by 53 to 111% upon exposure of the cells to chemotactic factors. This increase was due to decreased synthesis of methylated phospholipids and not to altered formation of phosphatidylethanolamine or activation of phospholipases. Methylated phospholipid ratios were also studied in the leading front lamellipodia isolated from macrophages migrating under chemotactic and nonchemotactic conditions. The phosphatidylethanolamine:methylated phospholipid ratios were increased up to fourfold in lamellipodia of macrophages migrating towards chemotactic agents when compared to those from cells migrating randomly. Biophysical changes in the plasma membrane produced by an increase in the ratio of phosphatidylethanolamine:methylated phospholipids as a result of exposure of cells to chemoattractants may be required for sustained directed migration.


Blood ◽  
1980 ◽  
Vol 56 (1) ◽  
pp. 23-29 ◽  
Author(s):  
HJ Cohen ◽  
ME Chovaniec ◽  
SE Ellis

Superoxide production by granulocytes is a result of the activation of an NAD(P)H-dependent oxidase present in the plasma membrane. Chlorpromazine (5–50 muM) prolongs the time necessary to activation of the superoxide generating system and inhibits the extent of activation. When chlorpromazine is added after activation, there is an inhibition of further superoxide production. These effects are seen with digitonin, phorbol myristate acetate, and opsonized zymosan stimulated guinea pig and human granulocytes. Other phenothiazines (1–20 muM) and tetracaine (0.1–1.0 muM) produce similar effects. Lidocaine (1–10 mM) inhibits superoxide production but has no effect on the rate of activation. The effect of chlorpromazine on the rate of activation is reversible, but its effect on extent of activation is unaffected by extensive washing. Incubation of granulocytes with chlorpromazine results in decreased activation of the plasma membrane superoxide generating NADPH oxidase. Chlorpromazine also competes with NADPH for the membrane oxidase. These data and previously published results provide the basis of a model for the activation of the superoxide generating system.


Blood ◽  
1980 ◽  
Vol 56 (1) ◽  
pp. 23-29 ◽  
Author(s):  
HJ Cohen ◽  
ME Chovaniec ◽  
SE Ellis

Abstract Superoxide production by granulocytes is a result of the activation of an NAD(P)H-dependent oxidase present in the plasma membrane. Chlorpromazine (5–50 muM) prolongs the time necessary to activation of the superoxide generating system and inhibits the extent of activation. When chlorpromazine is added after activation, there is an inhibition of further superoxide production. These effects are seen with digitonin, phorbol myristate acetate, and opsonized zymosan stimulated guinea pig and human granulocytes. Other phenothiazines (1–20 muM) and tetracaine (0.1–1.0 muM) produce similar effects. Lidocaine (1–10 mM) inhibits superoxide production but has no effect on the rate of activation. The effect of chlorpromazine on the rate of activation is reversible, but its effect on extent of activation is unaffected by extensive washing. Incubation of granulocytes with chlorpromazine results in decreased activation of the plasma membrane superoxide generating NADPH oxidase. Chlorpromazine also competes with NADPH for the membrane oxidase. These data and previously published results provide the basis of a model for the activation of the superoxide generating system.


1977 ◽  
Vol 7 (6) ◽  
pp. 441-455 ◽  
Author(s):  
Eileen Remold-o'donnell

1981 ◽  
Vol 18 (11) ◽  
pp. 999-1005 ◽  
Author(s):  
Sugiyama Nobutoshi ◽  
Tamoto Koichi ◽  
Koyama Jiro

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