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Angiotensin II induced catabolic effect and muscle atrophy are redox dependent
► Angiotensin II increases NADPH oxidase-derived ROS in skeletal muscle. ► Deletion of p47 phox prevents Ang II-induced skeletal muscle weight loss. ► Ang II-induced proteasome activity in skeletal muscle is prevented in p47 phox−/− mice. Angiotensin II (Ang II) causes skeletal muscle wasting via an...
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Published in: | Biochemical and biophysical research communications 2011-06, Vol.409 (2), p.217-221 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | ► Angiotensin II increases NADPH oxidase-derived ROS in skeletal muscle. ► Deletion of p47
phox prevents Ang II-induced skeletal muscle weight loss. ► Ang II-induced proteasome activity in skeletal muscle is prevented in p47
phox−/− mice.
Angiotensin II (Ang II) causes skeletal muscle wasting via an increase in muscle catabolism. To determine whether the wasting effects of Ang II were related to its ability to increase NADPH oxidase-derived reactive oxygen species (ROS) we infused wild-type C57BL/6J or p47
phox
−/− mice with vehicle or Ang II for 7
days. Superoxide production was increased 2.4-fold in the skeletal muscle of Ang II infused mice, and this increase was prevented in p47
phox
−/− mice. Apocynin treatment prevented Ang II-induced superoxide production in skeletal muscle, consistent with Ang II increasing NADPH oxidase derived ROS. Ang II induced loss of body and skeletal muscle weight in C57BL/6J mice, whereas the reduction was significantly attenuated in p47
phox
−/− animals. The reduction of skeletal muscle weight caused by Ang II was associated with an increase of proteasome activity, and this increase was completely prevented in the skeletal muscle of p47
phox
−/− mice. In conclusion, Ang II-induced skeletal muscle wasting is in part dependent on NADPH oxidase derived ROS. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2011.04.122 |