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Gene Review

UCP1  -  uncoupling protein 1 (mitochondrial,...

Bos taurus

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Disease relevance of UCP1


High impact information on UCP1

  • An uncoupling protein (UCP) has been identified in mitochondria from Acanthamoeba castellanii, a nonphotosynthetic soil amoeboid protozoon that, in molecular phylogenesis, appears on a branch basal to the divergence points of plants, animals, and fungi [2].
  • AcUCP was only weakly inhibited by purine nucleotides like UCP in plants [2].
  • This is in line with the very strong pH dependence of nucleoside triphosphate affinity above pH 7 with a delta pKD/delta pH = -2 as an important regulatory mechanism for the H+ transport activity of UCP [3].
  • It was demonstrated that UCP mRNA reached its highest level at birth in all bovine adipose tissues studied, except subcutaneous tissue [4].
  • However, despite uncoupling, neither UCP1 nor UCP2 altered superoxide formation [5].

Biological context of UCP1

  • UCP1 and UCP2 overexpression both increased the proton conductance of endothelial cell mitochondria, as rigorously determined by the kinetic relationship of respiration to inner membrane potential [5].
  • Mapping of the UCP1 locus to bovine chromosome 17 [6].
  • 5; n = 6 per group) was depleted of lipid in response to cold exposure, although UCP1 gene expression persisted [7].
  • In both breed types, a marked decrease in BAT UCP1 mRNA between 24 and 14 d prepartum was associated with a similar reduction in lipogenesis from palmitate and a noticeable change in BAT mitochondrial morphology, as the mitochondria became more elongated and the cristae became more elaborate [8].
  • Uncoupling protein-1 (UCP1) mRNA tripled during gestation in both breed types (P = 0.002), whereas mitochondrial cross-sectional area did not change (P = 0.14) during gestation [8].

Anatomical context of UCP1


Associations of UCP1 with chemical compounds

  • Therefore, a fully functional UCP1 was present and only partially inhibited in vivo by endogenous purine nucleotides [9].
  • Neither the breed nor the age x breed effect was significant (P > or = 0.24) for UCP1 mRNA concentration or mitochondrial cross-sectional area [8].
  • Lipogenesis from acetate and glucose in vitro decreased 97% during the last 96 d of gestation in both breed types, whereas the UCP1 gene expression tripled during gestation in both breed types [7].
  • Interval to the first increase in progesterone (ovulation) was less (P < .05) in OCW (14.7 +/- 3.4 d) and OCR (19.9 +/- 3.4 d) than in the OCP (35.0 +/- 2.9 d), UCP (38.0 +/- 3.4 d), and OCR + UCP (37.6 +/- 3.4 d) treatments [11].
  • Brown fat cells incubated for 24 h with or without NE showed no significant change in succinate dehydrogenase activity or uncoupling protein (UCP) content [12].

Regulatory relationships of UCP1

  • Finally, the level of uncoupling protein-1 (UCP1) RNA was found to be higher in dwarf mice and lower in giant animals relative to controls, suggesting that GH-mediated signaling may negatively regulate UCP1 gene expression in BAT [13].

Analytical, diagnostic and therapeutic context of UCP1


  1. Coenzyme Q is an obligatory cofactor for uncoupling protein function. Echtay, K.S., Winkler, E., Klingenberg, M. Nature (2000) [Pubmed]
  2. Identification and characterization of a protozoan uncoupling protein in Acanthamoeba castellanii. Jarmuszkiewicz, W., Sluse-Goffart, C.M., Hryniewiecka, L., Sluse, F.E. J. Biol. Chem. (1999) [Pubmed]
  3. Fluorescent nucleotide derivatives as specific probes for the uncoupling protein: thermodynamics and kinetics of binding and the control by pH. Huang, S.G., Klingenberg, M. Biochemistry (1995) [Pubmed]
  4. Sequential changes in the expression of mitochondrial protein mRNA during the development of brown adipose tissue in bovine and ovine species. Sudden occurrence of uncoupling protein mRNA during embryogenesis and its disappearance after birth. Casteilla, L., Champigny, O., Bouillaud, F., Robelin, J., Ricquier, D. Biochem. J. (1989) [Pubmed]
  5. Respiratory uncoupling by UCP1 and UCP2 and superoxide generation in endothelial cell mitochondria. Fink, B.D., Reszka, K.J., Herlein, J.A., Mathahs, M.M., Sivitz, W.I. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  6. Mapping of the UCP1 locus to bovine chromosome 17. Sonstegard, T.S., Kappes, S.M. Anim. Genet. (1999) [Pubmed]
  7. Brown adipose tissue development and metabolism in ruminants. Smith, S.B., Carstens, G.E., Randel, R.D., Mersmann, H.J., Lunt, D.K. J. Anim. Sci. (2004) [Pubmed]
  8. Ontogenic development of brown adipose tissue in Angus and Brahman fetal calves. Landis, M.D., Carstens, G.E., McPhail, E.G., Randel, R.D., Green, K.K., Slay, L., Smith, S.B. J. Anim. Sci. (2002) [Pubmed]
  9. Expression and regulation of mitochondrial uncoupling protein 1 from brown adipose tissue in Leishmania major promastigotes. Alvarez-Fortes, E., Ruiz-Pérez, L.M., Bouillaud, F., Rial, E., Rivas, L. Mol. Biochem. Parasitol. (1998) [Pubmed]
  10. Exclusive occurrence of thermogenin antigen in brown adipose tissue. Cannon, B., Hedin, A., Nedergaard, J. FEBS Lett. (1982) [Pubmed]
  11. Ad libitum suckling by an unrelated calf in the presence or absence of a cow's own calf prolongs postpartum anovulation. Lamb, G.C., Lynch, J.M., Grieger, D.M., Minton, J.E., Stevenson, J.S. J. Anim. Sci. (1997) [Pubmed]
  12. Norepinephrine does not stimulate protein and UCP synthesis in brown adipocytes of golden Syrian hamsters. Desautels, M., Dulos, R.A. Am. J. Physiol. (1993) [Pubmed]
  13. Enlargement of interscapular brown adipose tissue in growth hormone antagonist transgenic and in growth hormone receptor gene-disrupted dwarf mice. Li, Y., Knapp, J.R., Kopchick, J.J. Exp. Biol. Med. (Maywood) (2003) [Pubmed]
  14. The Uncoupling Protein 1 Gene (UCP1) Is Disrupted in the Pig Lineage: A Genetic Explanation for Poor Thermoregulation in Piglets. Berg, F., Gustafson, U., Andersson, L. PLoS Genet. (2006) [Pubmed]
  15. Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast. Douette, P., Navet, R., Bouillenne, F., Brans, A., Sluse-Goffart, C., Matagne, A., Sluse, F.E. Biochem. J. (2004) [Pubmed]
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