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Acot1  -  acyl-CoA thioesterase 1

Rattus norvegicus

Synonyms: ACH2, Acyl-CoA thioesterase 1, Acyl-coenzyme A thioesterase 1, CTE-I, Cte1, ...
 
 
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Disease relevance of Cte1

  • Recombinant expression of the mouse CTE-I cDNA in Escherichia coli resulted in production of immunoreactive protein that was mainly active with long-chain acyl-CoAs [1].
  • Thus, the constitutive m4 receptor on ACH2 cells is efficiently coupled to intracellular Ca2+ release by a pertussis toxin-sensitive mechanism [2].
  • Inductions by perfluoro-octanoic acid (PFOA) of hepatomegaly, peroxisomal beta-oxidation, microsomal 1-acylglycerophosphocholine acyltransferase and cytosolic long-chain acyl-CoA hydrolase were compared in liver between male and female rats [3].
 

High impact information on Cte1

  • However, the ACT mRNA was induced in the liver of rats that were fed Wy-14,643, a peroxisome proliferator and inducer of rodent liver cytosolic acyl-CoA thioesterase [4].
  • ACH2 cells were highly sensitive to ACh and the Ca2+ response in all cells was blocked by muscarinic antagonists [2].
  • Membranes from ACH2 exhibited muscarinic binding affinities which were not typical of M1, M2, or M3 receptors but were consistent with the profile of the putative m4 receptor [2].
  • Stimulation of the ACH2 cells by bradykinin (BK) evoked a Ca2+ response in 90% of the cells [2].
  • The subclone, ACH2, was isolated with a flow cytometer by selection of single cells that exhibited a strong intracellular Ca2+ response to acetylcholine (ACh) [2].
 

Biological context of Cte1

 

Anatomical context of Cte1

  • Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver [8].
  • Feeding clofibrate to rats and mice results in a strong induction of acyl-CoA thioesterase activity in the liver that is mainly due to increases in the enzyme activities in mitochondria and cytosol [1].
  • CTE-I mRNA was strongly expressed in kidney and brown adipose tissue and MTE-I mRNA was expressed mainly in brown adipose tissue and heart but was also expressed in kidney and white adipose tissue [1].
  • cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol [9].
  • Immunoblot analysis suggested the presence of the enzymes also in extrahepatic tissues, especially in the brain and testis (ACH1), and in the heart and kidney (ACH2) [10].
 

Associations of Cte1 with chemical compounds

 

Other interactions of Cte1

 

Analytical, diagnostic and therapeutic context of Cte1

References

  1. Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic acyl-CoA thioesterase from mouse and rat liver--recombinant expression in Escherichia coli, tissue expression, and nutritional regulation. Lindquist, P.J., Svensson, L.T., Alexson, S.E. Eur. J. Biochem. (1998) [Pubmed]
  2. Characterization of the m4 muscarinic receptor Ca2+ response in a subclone of PC-12 cells by single cell flow cytometry. Inhibition of the response by bradykinin. Ransom, J.T., Cherwinski, H.M., Delmendo, R.E., Sharif, N.A., Eglen, R. J. Biol. Chem. (1991) [Pubmed]
  3. Sex-related difference in the inductions by perfluoro-octanoic acid of peroxisomal beta-oxidation, microsomal 1-acylglycerophosphocholine acyltransferase and cytosolic long-chain acyl-CoA hydrolase in rat liver. Kawashima, Y., Uy-Yu, N., Kozuka, H. Biochem. J. (1989) [Pubmed]
  4. Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase. Broustas, C.G., Larkins, L.K., Uhler, M.D., Hajra, A.K. J. Biol. Chem. (1996) [Pubmed]
  5. Immunohistochemical localization of acyl-CoA hydrolase/thioesterase multigene family members to rat epithelia. Kuramochi, Y., Nishimura, S., Takagi-Sakuma, M., Watanabe, T., Kuroda, J., Hiratsuka, K., Nagae, Y., Suga, T., Yamada, J. Histochem. Cell Biol. (2002) [Pubmed]
  6. Modulating effect of sesamin, a functional lignan in sesame seeds, on the transcription levels of lipid- and alcohol-metabolizing enzymes in rat liver: a DNA microarray study. Tsuruoka, N., Kidokoro, A., Matsumoto, I., Abe, K., Kiso, Y. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  7. Heat shock induction of HIV production from chronically infected promonocytic and T cell lines. Stanley, S.K., Bressler, P.B., Poli, G., Fauci, A.S. J. Immunol. (1990) [Pubmed]
  8. Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver. Svensson, L.T., Engberg, S.T., Aoyama, T., Usuda, N., Alexson, S.E., Hashimoto, T. Biochem. J. (1998) [Pubmed]
  9. cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol. Yamada, J., Suga, K., Furihata, T., Kitahara, M., Watanabe, T., Hosokawa, M., Satoh, T., Suga, T. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  10. Purification and properties of long-chain acyl-CoA hydrolases from the liver cytosol of rats treated with peroxisome proliferator. Yamada, J., Matsumoto, I., Furihata, T., Sakuma, M., Suga, T. Arch. Biochem. Biophys. (1994) [Pubmed]
  11. An adrenocorticotropin-regulated phosphoprotein intermediary in steroid synthesis is similar to an acyl-CoA thioesterase enzyme. Finkielstein, C., Maloberti, P., Mendez, C.F., Paz, C., Cornejo Maciel, F., Cymeryng, C., Neuman, I., Dada, L., Mele, P.G., Solano, A., Podestá, E.J. Eur. J. Biochem. (1998) [Pubmed]
  12. beta-Adrenergic stimulation controls the expression of a thioesterase specific for very-long-chain fatty acids in perfused hearts. Neuman, I., Maloberti, P., Lisdero, C., Colonna, C., Peralta, J., José, J.P., Podestá, E.J. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  13. Relationship between translocation of long-chain acyl-CoA hydrolase, phosphatidate phosphohydrolase and CTP:phosphocholine cytidylyltransferase and the synthesis of triglycerides and phosphatidylcholine in rat liver. Asiedu, D., Skorve, J., Demoz, A., Willumsen, N., Berge, R.K. Lipids (1992) [Pubmed]
  14. Purification, characterization and modulation of a microsomal carboxylesterase in rat liver for the hydrolysis of acyl-CoA. Mukherjee, J.J., Jay, F.T., Choy, P.C. Biochem. J. (1993) [Pubmed]
  15. Fatty acyl-CoA oxidase activity is induced before long-chain acyl-CoA hydrolase activity and acyl-CoA binding protein in liver of rat treated with peroxisome proliferating 3-thia fatty acids. Skorve, J., Rosendal, J., Vaagenes, H., Knudsen, J., Lillehaug, J.R., Berge, R.K. Xenobiotica (1995) [Pubmed]
  16. Characterization of acyl-CoA thioesterase activity in isolated rat liver peroxisomes. Partial purification and characterization of a long-chain acyl-CoA thioesterase. Wilcke, M., Alexson, S.E. Eur. J. Biochem. (1994) [Pubmed]
  17. Purification and characterization of a long-chain acyl-CoA hydrolase from rat liver microsomes. Berge, R.K. Biochim. Biophys. Acta (1979) [Pubmed]
 
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