Source:http://linkedlifedata.com/resource/pubmed/id/11250929
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2001-3-19
|
| pubmed:abstractText |
We previously showed that angiotensin II (ang II) infusion in the rat produces cachexia and decreases circulating insulin-like growth factor I (IGF-I). The weight loss derives from an anorexigenic response and a catabolic effect of ang II. In these experiments we assessed potential catabolic mechanisms and the involvement of the IGF-I system in these responses to ang II. Ang II infusion caused a significant decrease in body weight compared with that of pair-fed control rats. Kidney and left ventricular weights were significantly increased by ang II, whereas fat tissue was unchanged. Skeletal muscle mass was significantly decreased in the ang II-infused rats, and a reduction in lean muscle mass was a major reason for their overall loss of body weight. In skeletal muscles, ang II did not significantly decrease protein synthesis, but overall protein breakdown was accelerated; inhibiting lysosomal and calcium-activated proteases did not reduce the ang II-induced increase in muscle proteolysis. Circulating IGF-I levels were 33% lower in ang II rats vs. control rats, and this difference was reflected in lower IGF-I messenger RNA levels in the liver. Moreover, IGF-I, IGF-binding protein-3, and IGF-binding protein-5 messenger RNAs in the gastrocnemius were significantly reduced. To investigate whether the reduced circulating IGF-I accounts for the loss in muscle mass, we increased circulating IGF-I by coinfusing ang II and IGF-I, but this did not prevent muscle loss. Our data suggest that ang II causes a loss in skeletal muscle mass by enhancing protein degradation probably via its inhibitory effect on the autocrine IGF-I system.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0013-7227
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
142
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1489-96
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:11250929-Angiotensin II,
pubmed-meshheading:11250929-Animals,
pubmed-meshheading:11250929-Autocrine Communication,
pubmed-meshheading:11250929-Blotting, Northern,
pubmed-meshheading:11250929-Blotting, Western,
pubmed-meshheading:11250929-Body Weight,
pubmed-meshheading:11250929-Down-Regulation,
pubmed-meshheading:11250929-Insulin-Like Growth Factor I,
pubmed-meshheading:11250929-Liver,
pubmed-meshheading:11250929-Male,
pubmed-meshheading:11250929-Muscle, Skeletal,
pubmed-meshheading:11250929-Muscle Proteins,
pubmed-meshheading:11250929-Nuclease Protection Assays,
pubmed-meshheading:11250929-Organ Size,
pubmed-meshheading:11250929-RNA, Messenger,
pubmed-meshheading:11250929-Radioimmunoassay,
pubmed-meshheading:11250929-Rats,
pubmed-meshheading:11250929-Rats, Sprague-Dawley,
pubmed-meshheading:11250929-Wasting Syndrome
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Angiotensin II induces skeletal muscle wasting through enhanced protein degradation and down-regulates autocrine insulin-like growth factor I.
|
| pubmed:affiliation |
Division of Cardiology, University Hospital of Geneva, CH-1211 Geneva, Switzerland. marijke.brink@dim.hcuge.ch
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|