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Gene Review

Soat1  -  sterol O-acyltransferase 1

Rattus norvegicus

Synonyms: ACAT-1, Acact, Acat, Acyl-coenzyme A:cholesterol acyltransferase 1, Cholesterol acyltransferase 1, ...
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Disease relevance of Soat1


Psychiatry related information on Soat1


High impact information on Soat1


Chemical compound and disease context of Soat1

  • The induction of intestinal ACAT activity in diabetic rats, its modulation by insulin, and the hypocholesterolemic effects of insulin or CL-277082 treatment clearly indicate that ACAT activity plays a major role in the initiation of diabetes-associated hypercholesterolemia [6].
  • Investigations utilizing the macrophage assay as an indicator for adrenal toxicity led to the identification of compounds 1g (FR190809) and 1k (FR186485, or FR195249 as its hydrochloride salt) as potent, nonadrenotoxic, orally efficacious ACAT inhibitors irrespective of the administration method [7].
  • Acaterin, a novel inhibitor of acyl-CoA: cholesterol acyltransferase produced by Pseudomonas sp. A92 [8].
  • To confirm this hypothesis, effects of a potent ACAT inhibitor, FR145237, on diet-induced hypercholesterolemia were examined in streptozotocin (STZ)-induced diabetic rats [9].
  • Thyroxine treatment reversed these effects of hypothyroidism on ACAT activity in both organs [10].

Biological context of Soat1


Anatomical context of Soat1


Associations of Soat1 with chemical compounds

  • Elevated ACAT in NS can contribute to dysregulation of cholesterol biosynthesis and catabolism by limiting the normal cholesterol signaling involved in regulation of these processes [1].
  • ACBP and cholesterol differentially alter fatty acyl CoA utilization by microsomal ACAT [17].
  • METHODS: Hepatic tissue ACAT mRNA (Northern blot), protein (Western blot) and enzymatic activity were determined in rats with puromycin-induced NS, placebo-treated control rats and Nagase hypoalbuminemic (NAG) rats [1].
  • Rat ACAT cDNA, having a coding region of 1635 bp with its deduced protein sequence of 545 amino acids and two typical motifs such as signature sequences and leucine heptad motif, showed 83, 92 and 90% identity with human, mouse, and hamster ACAT, respectively [11].
  • The data suggest that intestinal HMG-CoA reductase and ACAT activities are regulated by plasma lipoproteins independently of luminal factors [5].

Other interactions of Soat1


Analytical, diagnostic and therapeutic context of Soat1


  1. Up-regulation of acyl-coenzyme A:cholesterol acyltransferase (ACAT) in nephrotic syndrome. Vaziri, N.D., Liang, K. Kidney Int. (2002) [Pubmed]
  2. Upregulation of acyl-CoA: cholesterol acyltransferase in chronic renal failure. Liang, K., Vaziri, N.D. Am. J. Physiol. Endocrinol. Metab. (2002) [Pubmed]
  3. Acyl-CoA: cholesterol acyltransferase activity in the rat mammary gland: variation during pregnancy and lactation. Shand, J.H., West, D.W. Lipids (1991) [Pubmed]
  4. Regulation of rat biliary cholesterol secretion by agents that alter intrahepatic cholesterol metabolism. Evidence for a distinct biliary precursor pool. Stone, B.G., Erickson, S.K., Craig, W.Y., Cooper, A.D. J. Clin. Invest. (1985) [Pubmed]
  5. Regulation of acylcoenzyme A. Cholesterol acyltransferase and 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by lipoproteins in the intestine of parabiont rats. Purdy, B.H., Field, F.J. J. Clin. Invest. (1984) [Pubmed]
  6. Role of the intestinal acyl-CoA:cholesterol acyltransferase activity in the hyperresponse of diabetic rats to dietary cholesterol. Maechler, P., Wollheim, C.B., Bentzen, C.L., Niesor, E. J. Lipid Res. (1992) [Pubmed]
  7. Inhibitors of acyl-CoA:cholesterol O-acyltransferase. 3. Discovery of a novel series of N-alkyl-N-[(fluorophenoxy)benzyl]-N'-arylureas with weak toxicological effects on adrenal glands. Tanaka, A., Terasawa, T., Hagihara, H., Ishibe, N., Sawada, M., Sakuma, Y., Hashimoto, M., Takasugi, H., Tanaka, H. J. Med. Chem. (1998) [Pubmed]
  8. Acaterin, a novel inhibitor of acyl-CoA: cholesterol acyltransferase produced by Pseudomonas sp. A92. Naganuma, S., Sakai, K., Hasumi, K., Endo, A. J. Antibiot. (1992) [Pubmed]
  9. Effects of FR145237, an acyl-CoA:cholesterol acyltransferase inhibitor, on diet-induced hypercholesterolemia in diabetic rats. Sakuma, Y., Hagihara, H., Nagayoshi, A., Ohne, K., Mutoh, S., Ito, Y., Nakahara, K., Notsu, Y., Okuhara, M. Life Sci. (1997) [Pubmed]
  10. The effect of hypothyroidism and thyroxine replacement on hepatic and intestinal HMG-CoA reductase and ACAT activities and biliary lipids in the rat. Field, F.J., Albright, E., Mathur, S.N. Metab. Clin. Exp. (1986) [Pubmed]
  11. Molecular cloning, functional expression and tissue distribution of rat acyl-coenzyme A:cholesterol acyltransferase. Matsuda, H., Hakamata, H., Kawasaki, T., Sakashita, N., Miyazaki, A., Takahashi, K., Shichiri, M., Horiuchi, S. Biochim. Biophys. Acta (1998) [Pubmed]
  12. Dietary iron overload and induced lipid peroxidation are associated with impaired plasma lipid transport and hepatic sterol metabolism in rats. Brunet, S., Thibault, L., Delvin, E., Yotov, W., Bendayan, M., Levy, E. Hepatology (1999) [Pubmed]
  13. Hormone-sensitive lipase overexpression increases cholesteryl ester hydrolysis in macrophage foam cells. Escary, J.L., Choy, H.A., Reue, K., Schotz, M.C. Arterioscler. Thromb. Vasc. Biol. (1998) [Pubmed]
  14. The effect of progesterone on the regulatory mechanisms of biliary cholesterol secretion in the rat. Nervi, F.O., Del Pozo, R., Covarrubias, C.F., Ronco, B.O. Hepatology (1983) [Pubmed]
  15. Acyl-coenzyme A:cholesterol acyltransferase inhibitor, avasimibe, stimulates bile acid synthesis and cholesterol 7alpha-hydroxylase in cultured rat hepatocytes and in vivo in the rat. Post, S.M., Zoeteweij, J.P., Bos, M.H., de Wit, E.C., Havinga, R., Kuipers, F., Princen, H.M. Hepatology (1999) [Pubmed]
  16. The participation of sterol carrier protein2 in the conversion of cholesterol to cholesterol ester by rat liver microsomes. Gavey, K.L., Noland, B.J., Scallen, T.J. J. Biol. Chem. (1981) [Pubmed]
  17. ACBP and cholesterol differentially alter fatty acyl CoA utilization by microsomal ACAT. Chao, H., Zhou, M., McIntosh, A., Schroeder, F., Kier, A.B. J. Lipid Res. (2003) [Pubmed]
  18. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. Rusiñol, A.E., Cui, Z., Chen, M.H., Vance, J.E. J. Biol. Chem. (1994) [Pubmed]
  19. Cholesterol absorption in rat intestine: role of cholesterol esterase and acyl coenzyme A:cholesterol acyltransferase. Gallo, L.L., Clark, S.B., Myers, S., Vahouny, G.V. J. Lipid Res. (1984) [Pubmed]
  20. Effect of pregnancy and lactation on lipoprotein and cholesterol metabolism in the rat. Smith, J.L., Lear, S.R., Forte, T.M., Ko, W., Massimi, M., Erickson, S.K. J. Lipid Res. (1998) [Pubmed]
  21. Effects of aging on cholesterol content and cholesterol-metabolizing enzymes in the rat adrenal gland. Popplewell, P.Y., Azhar, S. Endocrinology (1987) [Pubmed]
  22. Cholesterol 7alpha-hydroxylase influences the expression of hepatic apoA-I in two inbred mouse strains displaying different susceptibilities to atherosclerosis and in hepatoma cells. Dueland, S., France, D., Wang, S.L., Trawick, J.D., Davis, R.A. J. Lipid Res. (1997) [Pubmed]
  23. Design, synthesis, and structure--activity relationship studies for a new imidazole series of J774 macrophage specific acyl-CoA:cholesterol acyltransferase (ACAT) inhibitors. Maduskuie, T.P., Wilde, R.G., Billheimer, J.T., Cromley, D.A., Germain, S., Gillies, P.J., Higley, C.A., Johnson, A.L., Pennev, P., Shimshick, E.J. J. Med. Chem. (1995) [Pubmed]
  24. Heterocyclic ureas: inhibitors of acyl-CoA:cholesterol O-acyltransferase as hypocholesterolemic agents. White, A.D., Creswell, M.W., Chucholowski, A.W., Blankley, C.J., Wilson, M.W., Bousley, R.F., Essenburg, A.D., Hamelehle, K.L., Krause, B.R., Stanfield, R.L., Dominick, M.A., Neub, M. J. Med. Chem. (1996) [Pubmed]
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