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Phosphorylation of beta subunit in F1F0 ATP synthase is associated with increased iron uptake in iron-overloaded heart mitochondria

Authors
Min, JungahKim, MisunKim, MiranLee, Myeong-SokSong, Eunsook
Issue Date
Dec-2013
Publisher
TAYLOR & FRANCIS LTD
Keywords
iron overload; subunit; F1F0 ATP synthase; heart; mitochondria
Citation
ANIMAL CELLS AND SYSTEMS, v.17, no.6, pp 406 - 412
Pages
7
Journal Title
ANIMAL CELLS AND SYSTEMS
Volume
17
Number
6
Start Page
406
End Page
412
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11155
DOI
10.1080/19768354.2013.867901
ISSN
1976-8354
2151-2485
Abstract
F1F0 ATP synthase was prepared from iron-overloaded heart mitochondria to study the effect of iron on mitochondria. As F1F0 ATP synthase was able to transport iron, proteoliposomes containing F1F0 ATP synthase were prepared to compare iron uptake between control and iron-overloaded mitochondria. A threefold increase in V-max (nmol/min/mg) (6.35 +/- 0.17 vs. 2.08 +/- 0.06) and an eightfold increase in K-m (mu M) (7.5 +/- 0.7 vs. 0.85 +/- 0.5) by F1F0 ATP synthase for iron uptake were observed in iron-overloaded mitochondria. Mitochondrial ATP synthase prepared from iron-overloaded heart has a canonical subunit composition in an altered stoichiometry compared to the control enzyme: the , , , OSCP, d, a, , and c subunits increased, but the b, e, A6L, and F6 subunits decreased significantly. In addition, the pattern of subunit isomers with different pIs changed. These isomers appeared to be associated with augmented phosphorylation by excess iron.
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