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Developmental regulation of tissue-specific isoforms of subunit VIa of beef cytochrome c oxidase.

作者信息

Schillace R, Preiss T, Lightowlers R N, Capaldi R A

机构信息

Institute of Molecular Biology, University of Oregon, Eugene 97403.

出版信息

Biochim Biophys Acta. 1994 Dec 30;1188(3):391-7. doi: 10.1016/0005-2728(94)90060-4.

Abstract

The switching of the subunit VIa isoforms of cytochrome c oxidase has been followed in heart tissue during bovine development both by transcript levels and in terms of the incorporation of L- (liver) and H- (heart) polypeptides into mitochondria. In early fetuses, e.g., 60-days development, there are high levels of VIaL transcript and high levels of the VIaL polypeptide incorporated into mitochondria. In late fetuses (after 200 days), the levels of VIaL transcript are still high, with less but still significant amounts of VIaL polypeptide present in comparison to adult heart in which the amount of this isoform is negligible. As the proportion of VIaL transcript is reduced, the proportion of VIaH transcript increases along with the amount of the VIaH isoform in mitochondria. These data indicate isoform switching during late fetal development. The presence of COLBP (cytochrome oxidase liver isoform binding protein) (Preiss, T. and Lightowlers, R.N. (1993) J. Biol. Chem. 268, 10659-10667) was examined at different developmental stages. COLBP binding activity was observed in hearts of late fetuses but not found in adult heart tissue, providing a correlation between the presence of this factor and the presence of the VIaL polypeptide in mitochondria.

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