Normal cytochrome C oxidase activity in prion protein gene-deficient mice.
Cytochrome c oxidases of prion protein (PrP) gene-deficient (Prnp(-/-)) and Prnp(+/+) mice were examined in vivo and in vitro. Non-invasive near-infrared spectra revealed that oxidation of copper and heme a+a(3) in cytochrome c oxidase of Prnp(-/-) mice was similar to that in Prnp(+/+) mice. Biochemical analysis of mitochondrial fractions also supported the results. PrP might not be involved in regulation of cytochrome c oxidase.
Sakudo
Akikazu
A
Department of Virology, Research Institute for Microbial Diseases, Osaka University, Yamadaoka, Suita, Osaka 565-0871, Japan. sakudo@biken.osaka-u.ac.jp
Taniuchi
Yojiro
Y
Kobayashi
Takanori
T
Onodera
Takashi
T
Ikuta
Kazuyoshi
K
D000818:Animals; D003300:Copper / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D051379:Mice; D008822:Mice, Transgenic; D008928:Mitochondria / Q000201:enzymology; D011328:Prions / Q000235:genetics*
D011328:Prions; D006418:Heme; D003300:Copper; D003576:Electron Transport Complex IV