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Journal of Applied Physiology, Vol 78, Issue 5 1904-1909, Copyright © 1995 by American Physiological Society
ARTICLES |
W. Kummer and H. Acker
Institut fur Anatomie und Zellbiologie, Philipps-Universitat, Marburg, Germany.
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.
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