Source:http://linkedlifedata.com/resource/pubmed/id/17127674
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2007-1-29
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pubmed:abstractText |
To study the peripheral effects of melanocortin on fuel homeostasis in skeletal muscle, we assessed palmitate oxidation and AMP kinase activity in alpha-melanocyte-stimulating hormone (alpha-MSH)-treated muscle cells. After alpha-MSH treatment, carnitine palmitoyltransferase-1 and fatty acid oxidation (FAO) increased in a dose-dependent manner. A strong melanocortin agonist, NDP-MSH, also stimulated FAO in primary culture muscle cells and C2C12 cells. However, [Glu6]alpha-MSH-ND, which has ample MC4R and MC3R agonistic activity, stimulated FAO only at high concentrations (10(-5) M). JKC-363, a selective MC4R antagonist, did not suppress alpha-MSH-induced FAO. Meanwhile, SHU9119, which has both antagonistic activity on MC3R and MC4R and agonistic activity on both MC1R and MC5R, increased the effect of alpha-MSH on FAO in both C2C12 and primary muscle cells. Small interference RNA against MC5R suppressed the alpha-MSH-induced FAO effectively. cAMP analogues mimicked the effect of alpha-MSH on FAO, and the effects of both alpha-MSH and cAMP analogue-mediated FAO were antagonized by a protein kinase A inhibitor (H89) and a cAMP antagonist ((Rp)-cAMP). Acetyl-CoA carboxylase activity was suppressed by alpha-MSH and cAMP analogues by phosphorylation through AMP-activated protein kinase activation in C2C12 cells. Taken together, these results suggest that alpha-MSH increases FAO in skeletal muscle, in which MC5R may play a major role. Furthermore, these results suggest that alpha-MSH-induced FAO involves cAMP-protein kinase A-mediated AMP-activated protein kinase activation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Melanocortin, Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-MSH
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:AnJuan JiJJ,
pubmed-author:BaikJa-HyunJH,
pubmed-author:ChaBong SooBS,
pubmed-author:HanDong-HeDH,
pubmed-author:HwangJung HeeJH,
pubmed-author:JinYoung-JunYJ,
pubmed-author:KimDol MiDM,
pubmed-author:KimSe HwaSH,
pubmed-author:LeeWon TaeWT,
pubmed-author:LimSung-KilSK,
pubmed-author:RheeYumieY
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2862-70
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pubmed:meshHeading |
pubmed-meshheading:17127674-Animals,
pubmed-meshheading:17127674-Cells, Cultured,
pubmed-meshheading:17127674-DNA Primers,
pubmed-meshheading:17127674-Fatty Acids,
pubmed-meshheading:17127674-Hindlimb,
pubmed-meshheading:17127674-Kinetics,
pubmed-meshheading:17127674-Male,
pubmed-meshheading:17127674-Mice,
pubmed-meshheading:17127674-Mice, Inbred C57BL,
pubmed-meshheading:17127674-Mitochondria, Muscle,
pubmed-meshheading:17127674-Muscle, Skeletal,
pubmed-meshheading:17127674-Myoblasts,
pubmed-meshheading:17127674-Oxidation-Reduction,
pubmed-meshheading:17127674-Receptor, Melanocortin, Type 1,
pubmed-meshheading:17127674-Recombinant Proteins,
pubmed-meshheading:17127674-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:17127674-alpha-MSH
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pubmed:year |
2007
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pubmed:articleTitle |
Peripheral effect of alpha-melanocyte-stimulating hormone on fatty acid oxidation in skeletal muscle.
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pubmed:affiliation |
Department of Internal Medicine & Endocrine Research Institute, Yonsei University College of Medicine, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul 120-752, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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