Role of cytochrome b-559 in arachidonic acid activation of resting human neutrophils.
Whether or not cytochrome b-559 is a necessary component of NADPH oxidase activity in neutrophils is still controversial. In highly purified plasma membranes isolated from resting neutrophils and lacking cytochrome b, addition of arachidonic acid induced an NADPH oxidase activity. This activity was similar to that of plasma membranes isolated from phorbol myristate acetate (PMA)-stimulated cells which possessed cytochrome b. Addition of arachidonic acid to the latter plasma membranes did not alter the oxidase activity. It can be concluded that plasma membranes isolated from resting neutrophils have, in the presence of arachidonic acid, an NADPH oxidase activity similar to that of PMA-stimulated cells, except that it is independent of cytochrome b-559.
Amit
N
N
INSERM U.294, CHU Xavier Bichat, Université Paris VII, France.
Huu
T P
TP
Sourbier
P
P
Marquetty
C
C
Hakim
J
J
D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000097:blood*; D002462:Cell Membrane / Q000201:enzymology; D003573:Cytochrome b Group / Q000097:blood*; D004789:Enzyme Activation; D006801:Humans; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*; D019255:NADPH Oxidases; D009504:Neutrophils / Q000502:physiology*; D045332:Photosystem II Protein Complex; D013481:Superoxides / Q000378:metabolism
D001095:Arachidonic Acids; D003573:Cytochrome b Group; D045332:Photosystem II Protein Complex; D013481:Superoxides; D016718:Arachidonic Acid; C019313:cytochrome b559; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases