PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2002 | 49 | 4 |

Tytuł artykułu

Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolisme: cDNA cloning sequencing and functional expression

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells re­sulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic ap­proaches.

Wydawca

-

Rocznik

Tom

49

Numer

4

Opis fizyczny

p.937-945,fig.

Twórcy

autor
  • ST.Marianna University School of Medicine, Kanagawa 216-8511, Japan
autor
autor

Bibliografia

  • Berge RK, Aarsland A, Bakke OM, Farstad M. (1983) Hepatic enzymes, CoASH and long-chain acyl-CoA in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum. Int J Biochem.; 15: 191-204
  • Broustas CG, Larkins LK, Uhler MD, Hajra AK. (1996) Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase. J Biol Chem.; 271: 10470-6
  • Ebisuno S, Isohashi F, Nakanishi Y, Sakamoto Y. (1988) Acetyl-CoA hydrolase: relation between activity and cholesterol metabolism in rat. Am J Physiol.; 255: R724-30
  • Ebisuno S, Isohashi F, Nakanishi Y, Higashi T, Sakamoto Y. (1989) The biphasic change of cytosolic acetyl-CoA hydrolase in rat liver during 3'-methyl-4-dimethylaminoazobenzene hepatocarcinogenesis. J pn J Cancer Res.; 80: 132-5
  • Horie S, Isobe M, Suga T. (1986) Changes in CoA pools in hepatic peroxisomes of the rat under various conditions. J Biochem.; 99: 1345-52
  • Hunt MC, Nousiainen SE, Huttunen MK, Orii KE, Svensson LT, Alexson EH. (1999) Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism. J Biol Chem.; 274: 34317-26
  • Isohashi F, Nakanishi Y, Sakamoto Y. (1983a) Effects of nucleotides on a cold labile acetyl-CoA hydrolase from the supernatant fraction of rat liver. Biochemistry.; 22: 584-90
  • Isohashi F, Nakanishi Y, Sakamoto Y. (1983b) Factors affecting the cold inactivation of an acetyl-coenzyme-A hydrolase purified from the supernatant fraction of rat liver. Eur J Biochem.; 134: 447-52
  • Isohashi F, Nakanishi Y, Matsunaga T, Sakamoto Y. (1984) A cold-labile acetyl-coenzyme-A hydrolase from the supernatant fraction of rat liver: reactivation and reconstitution of the active species from the inactive monomer. Eur J Biochem.; 142: 177-81
  • Kozak M. (1987) At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J Mol Biol.; 196: 947-50
  • Kozak M. (1991) Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem.; 266: 19867-70
  • Lakshmanan MR, Nepokroeff CM, Ness GC, Dugan RE, Porter JW. (1973) Stimulation by insulin of rat liver beta- hydroxy- beta-methylglutaryl coenzyme A reductase and choresterol-synthesizing activities. Biochem Biophys Res Commun.; 50: 704-10
  • Lee F-JS, Lin L-W, Smith JA. (1990) A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces cerevisiae. J Biol Chem.; 265: 7413-8
  • Mannaerts GP, Debeer LJ, Thomas J, De Schepper PJ. (1979) Mitochondrial and peroxisomal fatty acid oxidation in liver homogenates and isolated hepatocytes from control and clofibrate-treated rats. J Biol Chem.; 254: 4585-95
  • Matsunaga T, Isohashi F, Nakanishi Y, Sakamoto Y. (1985) Physiological changes in the activities of extramitochondrial acetyl-CoA hydrolase in the liver of rats under various metabolic conditions. Eur J Biochem.; 152: 331-6
  • Nakanishi Y, Isohashi F, Ebisuno S, Sakamoto Y. (1988) Binding of nucleotides to an extramitochondrial acetyl-CoA hydrolase from rat liver. Biochemistry..; 27: 4822-6
  • Nakanishi Y, Okamoto K, Isohashi F. (1993) Effects of chronic administration of the peroxisome proliferator, Clofibrate, on cytosolic acetyl-CoA hydrolase in rat liver Biochem Pharmacol.; 45: 1403-7
  • Nakanishi Y, Okamoto K, Isohashi F. (1994) Subcellular distribution of ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase in livers from control and clofibrate-treated rats: comparison of the cytosolic and peroxisomal enzyme. J Biochem.; 115: 328-32
  • Prass RL, Isohashi F, Utter MF. (1980) Purification and characterization of an extramitochondrial acetyl coenzyme A hydrolase from rat liver. J Biol Chem.; 255: 5215-23
  • Simon EJ, Shemin D. (1953) The preparation of S-succinyl coenzyme A. J Am Chem Soc.; 75: 2520.
  • Soling H-D, Rescher C. (1985) On the regulation of cold-labile cytosolic and of mitochondrial acetyl-CoA hydrolase in rat liver. Eur J Biochem.; 147: 111-7
  • Suematsu N, Okamoto K, Isohashi F. (1996) Effects of various proteins or peptides on reactivation of cold-inactivated acetyl-CoA hydrolase from rat liver. St Marianna Med J.; 24: 691-7.
  • Suematsu N, Okamoto K, Shibata K, Nakanishi Y, Isohashi F. (2001) Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase. Eur J Biochem.; 268: 2700-9

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-07b4d74f-5679-4f35-87a9-6195bff61a96
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.