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Gene Review

Ucp3  -  uncoupling protein 3 (mitochondrial,...

Rattus norvegicus

Synonyms: Mitochondrial uncoupling protein 3, Slc25a9, Solute carrier family 25 member 9, UCP 3
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Disease relevance of Ucp3

  • The influence of sepsis, another condition characterized by muscle cachexia, on UCP3 expression and activity is not known [1].
  • UCP3 is upregulated in various conditions characterized by skeletal muscle atrophy, including hyperthyroidism, fasting, denervation, diabetes, cancer, lipopolysaccharide (LPS), and treatment with glucocorticoids (GCs) [1].
  • Our results point to the existence of sex-associated differences in the control of muscle UCP3 expression in response to overweight and fasting, with an impaired induction in female rats under both conditions [2].
  • Concurrently, left ventricular UCP3 mRNA levels were significantly decreased with hypoxia (p<0.05) while UCP2 levels remained unchanged versus controls [3].
  • The correlation of abdominal muscle UCP3 mRNA expression with overweight in males could be related to their relative resistance to gain weight after chronic overeating of a cafeteria diet, by the purported role of UCP3 in the regulation of lipid utilization [2].

Psychiatry related information on Ucp3

  • By contrast, in the gastrocnemius muscle (a mixed fiber type muscle with a high capacity to shift between glucose and lipids as fuel substrate), mRNA expression of both UCP2 and UCP3 mRNA was found to be markedly up-regulated during food deprivation (when this tissue's thermogenesis is also decreased but its lipid fuel utilization is increased) [4].

High impact information on Ucp3


Chemical compound and disease context of Ucp3

  • Therefore, amelioration of obesity by NO-1886 in OVX rats is possibly because of an the increased expression of fatty acid oxidation-related enzymes and UCP3, both of which are related to fatty acid transfer and fat use [7].
  • The troglitazone-dependent decrease in UCP3 gene expression was accompanied by an increased weight gain in obese rats, while no such effect was observed in lean rats [8].

Biological context of Ucp3

  • Leptin induced an upregulation of UCP3 mRNA in muscle, with no changes in BAT UCP1 mRNA [9].
  • In contrast to BAT, UCP3 expression in skeletal muscle was increased in fasted rats and decreased during lactation [10].
  • In rats fed high-fat diet the UCP-3 gene expression was augmented 2-fold in the skeletal muscle while UCP-2 mRNA levels were increased significantly (1.6-fold) in the epididymal WAT [11].
  • The uncoupling protein homologs UCP2 and UCP3 have been proposed as candidate genes for the regulation of lipid metabolism [12].
  • The present study examined the effect of chronic activation of 5'-AMP-activated protein kinase (AMPK) on the metabolic profile, including uncoupling protein-3 (UCP-3) and myosin heavy chain (MHC)-based fibre phenotype of rodent fast-twitch tibialis anterior muscle [13].

Anatomical context of Ucp3


Associations of Ucp3 with chemical compounds

  • RA (7.5 mg/kg) increased UCP1 mRNA but decreased UCP2 and UCP3 mRNA by 50%, whereas methylprednisolone (65 mg/kg, two doses 24 h apart) suppressed all three uncoupling proteins by greater than 60% [19].
  • Within the context of this hypothesis, we have compared, from fed and fasted rats, changes in gene expression of skeletal muscle UCP2 and UCP3 with those of carnitine palmitoyltransferase I and medium-chain acyl-CoA dehydrogenase, two key enzymes regulating lipid flux across the mitochondrial beta-oxidation pathway [12].
  • Sterol regulatory element binding protein-1c expression and action in rat muscles: insulin-like effects on the control of glycolytic and lipogenic enzymes and UCP3 gene expression [15].
  • RESULTS: Independent of which TZD was injected (50 micromol/kg), UCP-3 expression in gastrocnemius muscle was distinctly increased after 6 h (increase vs vehicle-injected control: pioglitazone, 10.3+/-3.2-fold, p=0.03; rosiglitazone, 8.7+/-1.2-fold, p=0.001; RWJ241947, 9.5+/-2.7-fold, p=0.03) [16].
  • To elucidate the mechanism, here we compared the level of glucose transporter 4 (GLUT4) protein, uncoupling protein (UCP) 1 and UCP3 mRNA and protein expressions in the BAT under the same conditions [20].

Regulatory relationships of Ucp3


Other interactions of Ucp3

  • The reduction in mRNAs was reflected by a lowered UCP1 protein level, and to some extent, UCP3 protein [10].
  • The present study provides evidence, for the first time, of the induction of UCP3 mRNA expression in skeletal muscle by leptin in nongenetically obese animals [9].
  • The results support the view that mitochondrial energy conversion in heart changes during ontogeny and suggest the involvement of UCP3 and/or ANT1 in the control mechanism [14].
  • Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARgamma and key enzymes of lipid oxidation [12].
  • Hypoxia-induced decrease of UCP3 gene expression in rat heart parallels metabolic gene switching but fails to affect mitochondrial respiratory coupling [3].

Analytical, diagnostic and therapeutic context of Ucp3


  1. Expression of uncoupling protein 3 is upregulated in skeletal muscle during sepsis. Sun, X., Wray, C., Tian, X., Hasselgren, P.O., Lu, J. Am. J. Physiol. Endocrinol. Metab. (2003) [Pubmed]
  2. Positive correlation of skeletal muscle UCP3 mRNA levels with overweight in male, but not in female, rats. Rodríguez, A.M., Roca, P., Bonet, M.L., Picó, C., Oliver, P., Palou, A. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2003) [Pubmed]
  3. Hypoxia-induced decrease of UCP3 gene expression in rat heart parallels metabolic gene switching but fails to affect mitochondrial respiratory coupling. Essop, M.F., Razeghi, P., McLeod, C., Young, M.E., Taegtmeyer, H., Sack, M.N. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  4. Role of UCP homologues in skeletal muscles and brown adipose tissue: mediators of thermogenesis or regulators of lipids as fuel substrate? Samec, S., Seydoux, J., Dulloo, A.G. FASEB J. (1998) [Pubmed]
  5. Assessment of mitochondrial energy coupling in vivo by 13C/31P NMR. Jucker, B.M., Dufour, S., Ren, J., Cao, X., Previs, S.F., Underhill, B., Cadman, K.S., Shulman, G.I. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  6. Uncoupling proteins prevent glucose-induced neuronal oxidative stress and programmed cell death. Vincent, A.M., Olzmann, J.A., Brownlee, M., Sivitz, W.I., Russell, J.W. Diabetes (2004) [Pubmed]
  7. NO-1886 (ibrolipim), a lipoprotein lipase-promoting agent, accelerates the expression of UCP3 messenger RNA and ameliorates obesity in ovariectomized rats. Kano, S., Doi, M. Metab. Clin. Exp. (2006) [Pubmed]
  8. UCP3 gene expression does not correlate with muscle oxidation rates in troglitazone-treated Zucker fatty rats. Oberkofler, H., Neschen, S., Esterbauer, H., Waldhäusl, W., Patsch, W., Fürnsinn, C. Biochim. Biophys. Acta (2000) [Pubmed]
  9. Leptin, but not a beta 3-adrenergic agonist, upregulates muscle uncoupling protein-3 messenger RNA expression: short-term thermogenic interactions. Gómez-Ambrosi, J., Frühbeck, G., Martínez, J.A. Cell. Mol. Life Sci. (1999) [Pubmed]
  10. Inhibition of uncoupling protein expression during lactation: role of leptin. Xiao, X.Q., Grove, K.L., Grayson, B.E., Smith, M.S. Endocrinology (2004) [Pubmed]
  11. Cloning of rat uncoupling protein-3 and uncoupling protein-2 cDNAs: their gene expression in rats fed high-fat diet. Matsuda, J., Hosoda, K., Itoh, H., Son, C., Doi, K., Tanaka, T., Fukunaga, Y., Inoue, G., Nishimura, H., Yoshimasa, Y., Yamori, Y., Nakao, K. FEBS Lett. (1997) [Pubmed]
  12. Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARgamma and key enzymes of lipid oxidation. Samec, S., Seydoux, J., Russell, A.P., Montani, J.P., Dulloo, A.G. Pflugers Arch. (2002) [Pubmed]
  13. AMPK activation increases uncoupling protein-3 expression and mitochondrial enzyme activities in rat muscle without fibre type transitions. Putman, C.T., Kiricsi, M., Pearcey, J., MacLean, I.M., Bamford, J.A., Murdoch, G.K., Dixon, W.T., Pette, D. J. Physiol. (Lond.) (2003) [Pubmed]
  14. Expression of mitochondrial uncoupling protein 3 and adenine nucleotide translocase 1 genes in developing rat heart: putative involvement in control of mitochondrial membrane potential. Skárka, L., Bardová, K., Brauner, P., Flachs, P., Jarkovská, D., Kopecký, J., Ostádal, B. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  15. Sterol regulatory element binding protein-1c expression and action in rat muscles: insulin-like effects on the control of glycolytic and lipogenic enzymes and UCP3 gene expression. Guillet-Deniau, I., Mieulet, V., Le Lay, S., Achouri, Y., Carré, D., Girard, J., Foufelle, F., Ferré, P. Diabetes (2002) [Pubmed]
  16. Expression of uncoupling protein-3 mRNA in rat skeletal muscle is acutely stimulated by thiazolidinediones: an exercise-like effect? Brunmair, B., Gras, F., Wagner, L., Artwohl, M., Zierhut, B., Waldhäusl, W., Fürnsinn, C. Diabetologia (2004) [Pubmed]
  17. Exercise induces an increase in muscle UCP3 as a component of the increase in mitochondrial biogenesis. Jones, T.E., Baar, K., Ojuka, E., Chen, M., Holloszy, J.O. Am. J. Physiol. Endocrinol. Metab. (2003) [Pubmed]
  18. Changes in FAT/CD36, UCP2, UCP3 and GLUT4 gene expression during lipid infusion in rat skeletal and heart muscle. Vettor, R., Fabris, R., Serra, R., Lombardi, A.M., Tonello, C., Granzotto, M., Marzolo, M.O., Carruba, M.O., Ricquier, D., Federspil, G., Nisoli, E. Int. J. Obes. Relat. Metab. Disord. (2002) [Pubmed]
  19. Modulation of uncoupling protein 2 and uncoupling protein 3: regulation by denervation, leptin and retinoic acid treatment. Scarpace, P.J., Matheny, M., Moore, R.L., Kumar, M.V. J. Endocrinol. (2000) [Pubmed]
  20. Opposite regulation of uncoupling protein 1 and uncoupling protein 3 in vivo in brown adipose tissue of cold-exposed rats. Jakus, P.B., Sipos, K., Kispal, G., Sandor, A. FEBS Lett. (2002) [Pubmed]
  21. Long-term caloric restriction increases UCP3 content but decreases proton leak and reactive oxygen species production in rat skeletal muscle mitochondria. Bevilacqua, L., Ramsey, J.J., Hagopian, K., Weindruch, R., Harper, M.E. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  22. Chronic low-frequency stimulation upregulates uncoupling protein-3 in transforming rat fast-twitch skeletal muscle. Putman, C.T., Dixon, W.T., Pearcey, J.A., Maclean, I.M., Jendral, M.J., Kiricsi, M., Murdoch, G.K., Pette, D. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2004) [Pubmed]
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