Retinoid X receptor α overexpression alleviates mitochondrial dysfunction-induced insulin resistance through transcriptional regulation of insulin receptor substrate 1

Molecules and Cells

Volumn 38, Issue 4, 2015, Pages 356-361

  Lee, Seung Eun ^a   Koo, Young Do ^a   Lee, Ji Seon ^a   Kwak, Soo Heon ^a   Jung, Hye Seung ^a   Cho, Young Min ^a   Park, Young Joo ^a   Chung, Sung Soo ^a   Park, Kyong Soo ^a  

^a Seoul National University College of Medicine   (South Korea)

Author keywords

Insulin receptor substrate 1; Insulin resistance; Itochondrial dysfunction; Retinoid X receptor

Indexed keywords

ALITRETINOIN; ANTIMYCIN A1; INSULIN; INSULIN RECEPTOR SUBSTRATE 1; MESSENGER RNA; RETINOID X RECEPTOR ALPHA; ROTENONE; INSULIN RECEPTOR SUBSTRATE; IRS1 PROTEIN, HUMAN;

ARTICLE; CELL FUNCTION; CONTROLLED STUDY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; HUMAN; HUMAN CELL; INSULIN RESISTANCE; MITOCHONDRION; MYOTUBE; OXIDATIVE PHOSPHORYLATION; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION; ANIMAL; BIOSYNTHESIS; CELL LINE; CHLOROCEBUS AETHIOPS; COS CELL LINE; GENETIC TRANSFECTION; GENETICS; HEK293 CELL LINE; METABOLISM; MOUSE; MUSCLE MITOCHONDRION; SKELETAL MUSCLE CELL;

ANIMALS; CELL LINE; CERCOPITHECUS AETHIOPS; COS CELLS; HEK293 CELLS; HUMANS; INSULIN RECEPTOR SUBSTRATE PROTEINS; INSULIN RESISTANCE; MICE; MITOCHONDRIA, MUSCLE; MUSCLE FIBERS, SKELETAL; RETINOID X RECEPTOR ALPHA; SIGNAL TRANSDUCTION; TRANSFECTION;

EID: 84950298063     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.14348/molcells.2015.2280     Document Type: Article

References (27)

1. Anderson, E.J., Lustig, M.E., Boyle, K.E., Woodlief, T.L., Kane, D.A., Lin, C.T., Price, J.W., 3rd, Kang, L., Rabinovitch, P.S., Szeto, H.H., et al. (2009). Mitochondrial H2O2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans. J. Clin. Invest. 119, 573-581.
2. Cesario, R.M., Klausing, K., Razzaghi, H., Crombie, D., Rungta, D., Heyman, R.A., and Lala, D.S. (2001). The rexinoid LG100754 is a novel RXR:PPARgamma agonist and decreases glucose levels in vivo. Mol. Endocrinol. 15, 1360-1369.
3. Chae, S., Ahn, B.Y., Byun, K., Cho, Y.M., Yu, M.H., Lee, B., Hwang, D., and Park, K.S. (2013). A systems approach for decoding mitochondrial retrograde signaling pathways. Sci. Signal. 6, rs4.
4. Egawa, K., Nakashima, N., Sharma, P.M., Maegawa, H., Nagai, Y., Kashiwagi, A., Kikkawa, R., and Olefsky, J.M. (2000). Persistent activation of phosphatidylinositol 3-kinase causes insulin resistance due to accelerated insulin-induced insulin receptor substrate-1 degradation in 3T3-L1 adipocytes. Endocrinology 141, 1930-1935.
5. Evans, R.M., and Mangelsdorf, D.J. (2014). Nuclear receptors, RXR, and the big bang. Cell 157, 255-266.
6. Fisher-Wellman, K.H., and Neufer, P.D. (2012). Linking mitohondrial bioenergetics to insulin resistance via redox biology. Trends Endocrinol. Metab. 23, 142-153.
7. Gianni, M., Tarrade, A., Nigro, E.A., Garattini, E., and Rochette-Egly, C. (2003). The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers. J. Biol. Chem. 278, 34458-34466.
8. Gual, P., Le Marchand-Brustel, Y., and Tanti, J.F. (2005). Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Biochimie 87, 99-109.
9. Heyman, R.A., Mangelsdorf, D.J., Dyck, J.A., Stein, R.B., Eichele, G., Evans, R.M., and Thaller, C. (1992). 9-cis retinoic acid is high affinity ligand for the retinoid X receptor. Cell 68, 397-406.
10. Kelley, D.E., He, J., Menshikova, E.V., and Ritov, V.B. (2002). Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes 51, 2944-2950.
11. Kelley, D.E., and Simoneau, J.A. (1994). Impaired free fatty acid utilization by skeletal muscle in non-insulin-dependent diabetes mellitus. J. Clin. Invest. 94, 2349-2356.
12. Kim, M., Ahn, B.Y., Lee, J.S., Chung, S.S., Lim, S., Park, S.G., Jung, H.S., Lee, H.K., and Park, K.S. (2009). The ginsenoside Rg3 has a stimulatory effect on insulin signaling in L6 myotubes. Biochem. Biophys. Res. Commun. 389, 70-73.
13. Kliewer, S.A., Umesono, K., Noonan, D.J., Heyman, R.A., and Evans, R.M. (1992). Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature 358, 771-774.
14. Leibowitz, M.D., Ardecky, R.J., Boehm, M.F., Broderick, C.L., Caragna, M.A., Crombie, D.L., D’Arrigo, J., Etgen, G.J., Faul, M.M., Grese, T.A., et al. (2006). Biological characterization of a heterodimer-selective retinoid X receptor modulator: potential benefits for the treatment of type 2 diabetes. Endocrinology 147, 1044-1053.
15. Lenhard, J.M., Lancaster, M.E., Paulik, M.A., Weiel, J.E., Binz, J.G., Sundseth, S.S., Gaskill, B.A., Lightfoot, R.M., and Brown, H.R. (1999). The RXR agonist LG100268 causes hepatomegaly, improves glycaemic control and decreases cardiovascular risk and cachexia in diabetic mice suffering from pancreatic beta-cell dysfunction. Diabetologia 42, 545-554.
16. Lowell, B.B., and Shulman, G.I. (2005). Mitochondrial dysfunction and type 2 diabetes. Science 307, 384-387.
17. Macotela, Y., Emanuelli, B., Bang, A.M., Espinoza, D.O., Boucher, J., Beebe, K., Gall, W., and Kahn, C.R. (2011). Dietary leucine-- an environmental modifier of insulin resistance acting on multiple levels of metabolism. PLoS One 6, e21187.
18. Martin, S.D., and McGee, S.L. (2014). The role of mitochondria in the aetiology of insulin resistance and type 2 diabetes. Biochim. Biophys. Acta 1840, 1303-1312.
19. Morino, K., Petersen, K.F., Dufour, S., Befroy, D., Frattini, J., Shatzkes, N., Neschen, S., White, M.F., Bilz, S., Sono, S., et al. (2005). Reduced mitochondrial density and increased IRS-1 serine phosphorylation in muscle of insulin-resistant offspring of type 2 diabetic parents. J. Clin. Invest. 115, 3587-3593.
20. Osburn, D.L., Shao, G., Seidel, H.M., and Schulman, I.G. (2001). Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions. Mol. Cell. Biol. 21, 4909-4918.
21. Pederson, T.M., Kramer, D.L., and Rondinone, C.M. (2001). Serine/threonine phosphorylation of IRS-1 triggers its degradation: possible regulation by tyrosine phosphorylation. Diabetes 50, 24-31.
22. Ritov, V.B., Menshikova, E.V., He, J., Ferrell, R.E., Goodpaster, B.H., and Kelley, D.E. (2005). Deficiency of subsarcolemmal mitochondria in obesity and type 2 diabetes. Diabetes 54, 8-14.
23. Ryu, H.S., Park, S.Y., Ma, D., Zhang, J., and Lee, W. (2011). The induction of microRNA targeting IRS-1 is involved in the development of insulin resistance under conditions of mitochondrial dysfunction in hepatocytes. PLoS One 6, e17343.
24. Simoneau, J.A., and Kelley, D.E. (1997). Altered glycolytic and oxidative capacities of skeletal muscle contribute t o insulinresistance in NIDDM. J. Appl. Physiol. 83, 166-171.
25. Singh, A.B., Guleria, R.S., Nizamutdinova, I.T., Baker, K.M., and Pan, J. (2012). High glucose-induced repression of RAR/RXR in cardiomyocytes is mediated through oxidative stress/JNK signaling. J. Cell. Physiol. 227, 2632-2644.
26. Sun, X.J., Goldberg, J.L., Qiao, L.Y., and Mitchell, J.J. (1999). Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway. Diabetes 48, 1359-1364.
27. Yuzefovych, L.V., Solodushko, V.A., Wilson, G.L., and Rachek, L.I .(2012). Protection from palmitate-induced mitochondrial DNA damage prevents from mitochondrial oxidative stress, mitochondrial dysfunction, apoptosis, and impaired insulin signaling in rat L6 skeletal muscle cells. Endocrinology 153, 92-100.