Chronic leptin treatment stimulates lipid oxidation in immortalized and primary mouse skeletal muscle cells

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1791, Issue 2, 2009, Pages 103-109

  Akasaka, Yunike ^a   Tsunoda, Masaki ^a   Ide, Tomohiro ^a   Murakami, Koji ^a  

^a KYORIN PHARMACEUTICAL CO LTD   (Japan)

Author keywords

JAK; Leptin; Lipid oxidation; Muscle cell; STAT

Indexed keywords

DACTINOMYCIN; JANUS KINASE 2; LEPTIN; LEPTIN RECEPTOR; LIPID; MESSENGER RNA; SMALL INTERFERING RNA; STAT3 PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL CULTURE; CELL DIFFERENTIATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; LIPID OXIDATION; MALE; MOUSE; MYOTUBE; NONHUMAN; PRIORITY JOURNAL; SKELETAL MUSCLE;

ANIMALS; BLOTTING, WESTERN; CADHERINS; CELLS, CULTURED; ION CHANNELS; JANUS KINASE 2; LEPTIN; LIPID PEROXIDATION; MALE; MICE; MICE, INBRED C57BL; MITOCHONDRIAL PROTEINS; MUSCLE FIBERS, SKELETAL; MUSCLE, SKELETAL; OXIDATION-REDUCTION; PHOSPHORYLATION; RNA, MESSENGER; RNA, SMALL INTERFERING; SIGNAL TRANSDUCTION; STAT3 TRANSCRIPTION FACTOR;

EID: 59049103288     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2008.11.003     Document Type: Article

References (42)

1. Zhang Y., Proenca R., Maffei M., Barone M., Leopold L., and Friedman J.M. Positional cloning of the mouse obese gene and its human homologue. Nature 372 (1994) 425-432
2. Pelleymounter M.A., Cullen M.J., Baker M.B., Hecht R., Winters D., Boone T., and Collins F. Effects of the obese gene product on body weight regulation in ob/ob mice. Science 269 (1995) 540-543
3. Minokoshi Y., Alquier T., Furukawa N., Kim Y.B., Lee A., Xue B., Mu J., Foufelle F., Ferre P., Birnbaum M.J., Stuck B.J., and Kahn B.B. AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus. Nature 428 (2004) 569-574
4. Halaas J.L., Gajiwala K.S., Maffei M., Cohen S.L., Chait B.T., Rabinowitz D., Lallone R.L., Burley S.K., and Friedman J.M. Weight-reducing effects of the plasma protein encoded by the obese gene. Science 269 (1995) 543-546
5. Wang J.L., Chinookoswong N., Scully S., Qi M., and Shi Z.Q. Differential effects of leptin in regulation of tissue glucose utilization in vivo. Endocrinology 140 (1999) 2117-2124
6. Harris R.B., Zhou J., Redmann Jr. S.M., Smagin G.N., Smith S.R., Rodgers E., and Zachwieja J.J. A leptin dose-response study in obese (ob/ob) and lean (+/?) mice. Endocrinology 139 (1998) 8-19
7. Minokoshi Y., Kim Y.B., Peroni O.D., Fryer L.G., Muller C., Carling D., and Kahn B.B. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 415 (2002) 339-343
8. Muoio D.M., Dohm G.L., Fiedorek Jr. F.T., Tapscott E.B., and Coleman R.A. Leptin directly alters lipid partitioning in skeletal muscle. Diabetes 46 (1997) 1360-1363
9. Steinberg G.R., Parolin M.L., Heigenhauser G.J., and Dyck D.J. Leptin increases FA oxidation in lean but not obese human skeletal muscle: evidence of peripheral leptin resistance. Am. J. Physiol. Endocrinol. Metabol. 283 (2002) E187-E192
10. Solinas G., Summermatter S., Mainieri D., Gubler M., Pirola L., Wymann M.P., Rusconi S., Montani J.P., Seydoux J., and Dulloo A.G. The direct effect of leptin on skeletal muscle thermogenesis is mediated by substrate cycling between de novo lipogenesis and lipid oxidation. FEBS Lett. 577 (2004) 539-544
11. Muoio D.M., Dohm G.L., Tapscott E.B., and Coleman R.A. Leptin opposes insulin's effects on fatty acid partitioning in muscles isolated from obese ob/ob mice. Am. J. Physiol., Endocrinol. Metabol. 276 (1999) E913-E921
12. Ghilardi N., Ziegler S., Wiestner A., Stoffel R., Heim M.H., and Skoda R.C. Defective STAT signaling by the leptin receptor in diabetic mice. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 6231-6235.G.R
13. Fruhbeck G., Gomez-Ambrosi J., and Martinez J.A. Pre- and postprandial expression of the leptin receptor splice variants OB-Ra and OB-Rb in murine peripheral tissues. Physiol. Res. 48 (1999) 189-195
14. Sweeney G., Keen J., Somwar R., Konrad D., Garg R., and Klip A. High leptin levels acutely inhibit insulin-stimulated glucose uptake without affecting glucose transporter 4 translocation in l6 rat skeletal muscle cells. Endocrinology 142 (2001) 4806-4812
15. Steinberg G.R., Rush J.W.E., and Dyck D.J. AMPK expression and phosphorylation are increased in rodent muscle after chronic leptin treatment. Am. J. Physiol. Endocrinol. Metabol. 284 (2002) E654-E684
16. 12 myoblasts by changing the subcellular localization of the a2 form of AMP-activated protein kinase. Mol. Cell Biol. 27 (2007) 4317-4327
17. Muoio D.M., Seefeld K., Witters L.A., and Coleman R.A. AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target. Biochem. J. 338 Pt 3 (1999) 783-791
18. Winder W.W., and Hardie D.G. Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am. J. Physiol. 270 (1996) E299-E304
19. Harwood Jr. H.J., Petras S.F., Shelly L.D., Zaccaro D.A., Makowski M.R., Hargrove D.M., Martin K.A., Tracy W.R., Chapman J.G., Magee W.P., Dalvie D.K., Soliman V.F., Martin W.H., Mularski C.J., and Eisenbeis S.A. Isozyme-nonselective N-substituted bipiperidylcarboxamide acetyl-CoA carboxylase inhibitors reduce tissue malonyl-CoA concentrations, inhibit fatty acid synthesis, and increase fatty acid oxidation in cultured cells and in experimental animals. J. Biol. Chem. 278 (2003) 37099-37111
20. Bates S.H., Gardiner J.V., Jones R.B., Bloom S.R., and Bailey C.J. Acute stimulation of glucose uptake by leptin in l6 muscle cells. Horm. Metab. Res. 34 (2002) 111-115
21. Maroni P., Bendinelli P., and Piccoletti R. Intracellular signal transduction pathways induced by leptin in C2C12 cells. Cell Biol. Int. 29 (2005) 542-550
22. Zabeau L., Lavens D., Peelman F., Eyckerman S., Vandekerckhove J., and Tavernier J. The ins and outs of leptin receptor activation. FEBS Lett. 546 (2003) 45-50
23. Ghilardi N., and Skoda R.C. The leptin receptor activates janus kinase 2 and signals for proliferation in a factor-dependent cell line. Mol. Endocrinol. 11 (1997) 393-399
24. Bjorbaek C., Uotani S., da Silva B., and Flier J.S. Divergent signaling capacities of the long and short isoforms of the leptin receptor. J. Biol. Chem. 272 (1997) 32686-32695
25. Bahrenberg G., Behrmann I., Barthel A., Hekerman P., Heinrich P.C., Joost H.G., and Becker W. Identification of the critical sequence elements in the cytoplasmic domain of leptin receptor isoforms required for Janus kinase/signal transducer and activator of transcription activation by receptor heterodimers. Mol. Endocrinol. 16 (2002) 859-872
26. Cui Y., Huang Lu., Elefteriou F., Yang G., Shelton J.M., Giles J.E., Oz O.K., Pourbahrami T., Lu C.Y.H., Richardson J.A., Karsenty G., and Li C. Essential role of STAT3 in body weight and glucose homeostasis. Mol. Cell Biol. 24 (2004) 258-269
27. Bates S.H., Dundon T.A., Seifert M., Carlson M., Maratos-Flier E., and Myers Jr. M.G. LRb-STAT3 signaling is required for the neuroendocrine regulation of energy expenditure by leptin. Diabetes 53 (2004) 3067-3073
28. Bates S.H., Kulkarni R.N., Seifert M., and Myers Jr. M.G. Roles for leptin receptor/STAT3-dependent and -independent signals in the regulation of glucose homeostasis. Cell Metab. 1 (2005) 169-178
29. Buettner C., Pocai A., Muse E.D., Etgen A.M., Myers Jr. M.G., and Rossetti L. Critical role of STAT3 in leptin's metabolic actions. Cell Metab. 4 (2006) 49-60
30. 12 muscle cells by activation of ERK2. Mol. Cell Endocrinol. 157 (1999) 121-130
31. Maroni P., Bendinelli P., and Piccoletti R. Early intracellular events induced by in vivo leptin treatment in mouse skeletal muscle. Mol. Cell Endocrinol. 201 (2003) 109-121
32. Meydan N., Grunberger T., Dadi H., Shahar M., Arpaia E., Lapidot Z., Leeder J.S., Freedman M., Cohen A., Gazit A., Levitzki A., and Roifman C.M. Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature 379 (1996) 645-648
33. Tesseraux I., Gulden M., and Wassermann O. Cultured myotubes from skeletal muscle of adult rats. Characterization and action of Anemonia sulcata toxin II. Naunyn-Schmiedeberg's Arch. Pharmacol. 336 (1987) 232-239
34. Ide T., Tsunoda M., Mochizuki T., and Murakami K. Enhancement of insulin signaling through inhibition of tissue lipid accumulation by activation of peroxisome proliferator-activated receptor (PPAR) alpha in obese mice. Med. Sci. Monit. 10 (2004) BR388-BR395
35. Ide T., Shimano H., Yoshikawa T., Yahagi N., Amemiya-Kudo M., Matsuzaka T., Nakakuki M., Yatoh S., Iizuka Y., Tomita S., Ohashi K., Takahashi A., Sone H., Gotoda T., Osuga J., Ishibashi S., and Yamada N. Cross-talk between peroxisome proliferator-activated receptor (PPAR) alpha and liver X receptor (LXR) in nutritional regulation of fatty acid metabolism. II. LXRs suppress lipid degradation gene promoters through inhibition of PPAR signaling. Mol. Endocrinol. 17 (2003) 1255-1267
36. Murakami K., Tobe K., Ide T., Mochizuki T., Ohashi M., Akanuma Y., Yazaki Y., and Kadowaki T. A novel insulin sensitizer acts as a coligand for peroxisome proliferator-activated receptor-alpha (PPAR-alpha) and PPAR-gamma: effect of PPAR-alpha activation on abnormal lipid metabolism in liver of Zucker fatty rats. Diabetes 47 (1998) 1841-1847
37. Ramsay T.G. Porcine leptin inhibits protein breakdown and stimulates fatty acid oxidation in C2C12 myotubes. J. Anim. Sci. 81 (2003) 3046-3051
38. Liang C.P., and Tall A.R. Transcriptional profiling reveals global defects in energy metabolism, lipoprotein, and bile acid synthesis and transport with reversal by leptin treatment in ob/ob mouse liver. J. Biol. Chem. 276 (2001) 49066-49076
39. Zhou Y.T., Shimabukuro M., Koyama K., Lee Y., Wang M.Y., Trieu F., Newgard C.B., and Unger R.H. Induction by leptin of uncoupling protein-2 and enzymes of fatty acid oxidation. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 6386-6390
40. McClelland G.B., Kraft C.S., Michaud D., Russell J.C., Mueller C.R., and Moyes C.D. Leptin and the control of respiratory gene expression in muscle. Biochim. Biophys. Acta 1688 (2004) 86-93
41. Inoue H., Ogawa W., Ozaki M., Haga S., Matsumoto M., Furukawa K., Hashimoto N., Kido Y., Mori T., Sakaue H., Teshigawara K., Jin S., Iguchi H., Hiramatsu R., LeRoith D., Takeda K., Akira S., and Kasuga M. Role of STAT-3 in regulation of hepatic gluconeogenic genes and carbohydrate metabolism in vivo. Nat. Med. 10 (2004) 168-174
42. Cernkovich E.R., Deng J., Bond M.C., Combs T.P., and Harp J.B. Adipose-specific disruption of signal transducer and activator of transcription 3 (STAT3) increases body weight and adiposity. Endocrinology 149 (2008) 1581-1590