Immunohistochemical demonstration of four subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body.
We demonstrate, by means of immunohistochemistry, that type I cells of human, guinea pig, and rat carotid bodies react with antisera raised against the subunits p22phox, gp91phox, p47phox, and p67phox of the NAD(P)H oxidase isolated from human neutrophil granulocytes. The findings support previous photometric studies that indicate that carotid body type I cells possess a putative oxygen sensor protein that is similar to the neutrophil NAD(P)H oxidase and consists of a hydrogen peroxide generating low-potential cytochrome b558 with cofactors regulating the electron transfer to oxygen.
Kummer
W
W
Institut für Anatomie und Zellbiologie, Philipps-Universität, Marburg, Germany.
Acker
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002344:Carotid Body / Q000166:cytology / Q000201:enzymology*; D003573:Cytochrome b Group / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D005260:Female; D005455:Fluorescent Antibody Technique; D006168:Guinea Pigs; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D019255:NADPH Oxidases; D009504:Neutrophils / Q000201:enzymology*; D010101:Oxygen Consumption; D051381:Rats
D003573:Cytochrome b Group; C036888:cytochrome b558; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases