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Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1
Identifiers
Symbols SOAT1; ACAT1; ACAT; ACACT; RP11-215I23.2; SOAT; STAT
External IDs OMIM: 102642 MGI104665 HomoloGene2333
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 6646 20652
Ensembl ENSG00000057252 ENSMUSG00000026600
Uniprot P35610 Q06EZ3
Refseq NM_003101 (mRNA)
NP_003092 (protein)
NM_009230 (mRNA)
NP_033256 (protein)
Location Chr 1: 177.53 - 177.59 Mb Chr 1: 158.27 - 158.31 Mb
Pubmed search [1] [2]

Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1, also known as SOAT1, is a human gene.[1]

Acyl-coenzyme A:cholesterol acyltransferase (ACACT; EC 2.3.1.26) is an intracellular protein located in the endoplasmic reticulum that forms cholesterol esters from cholesterol. Accumulation of cholesterol esters as cytoplasmic lipid droplets within macrophages and smooth muscle cells is a characteristic feature of the early stages of atherosclerotic plaques (Cadigan et al., 1988).[supplied by OMIM][1]

References

Further reading

  • Chang TY, Chang CC, Lin S, et al. (2001). "Roles of acyl-coenzyme A:cholesterol acyltransferase-1 and -2.". Curr. Opin. Lipidol. 12 (3): 289–96. PMID 11353332. 
  • Chang CC, Noll WW, Nutile-McMenemy N, et al. (1994). "Localization of acyl coenzyme A:cholesterol acyltransferase gene to human chromosome 1q25.". Somat. Cell Mol. Genet. 20 (1): 71–4. PMID 8197480. 
  • Chang CC, Huh HY, Cadigan KM, Chang TY (1993). "Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells.". J. Biol. Chem. 268 (28): 20747–55. PMID 8407899. 
  • Oelkers P, Behari A, Cromley D, et al. (1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes.". J. Biol. Chem. 273 (41): 26765–71. PMID 9756920. 
  • Li BL, Li XL, Duan ZJ, et al. (1999). "Human acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) gene organization and evidence that the 4.3-kilobase ACAT-1 mRNA is produced from two different chromosomes.". J. Biol. Chem. 274 (16): 11060–71. PMID 10196189. 
  • Lin S, Cheng D, Liu MS, et al. (1999). "Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains.". J. Biol. Chem. 274 (33): 23276–85. PMID 10438503. 
  • Sakashita N, Miyazaki A, Takeya M, et al. (2000). "Localization of human acyl-coenzyme A: cholesterol acyltransferase-1 (ACAT-1) in macrophages and in various tissues.". Am. J. Pathol. 156 (1): 227–36. PMID 10623671. 
  • Guo Z, Cromley D, Billheimer JT, Sturley SL (2001). "Identification of potential substrate-binding sites in yeast and human acyl-CoA sterol acyltransferases by mutagenesis of conserved sequences.". J. Lipid Res. 42 (8): 1282–91. PMID 11483630. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Zhang Y, Yu C, Liu J, et al. (2003). "Cholesterol is superior to 7-ketocholesterol or 7 alpha-hydroxycholesterol as an allosteric activator for acyl-coenzyme A:cholesterol acyltransferase 1.". J. Biol. Chem. 278 (13): 11642–7. doi:10.1074/jbc.M211559200. PMID 12533546. 
  • Wollmer MA, Streffer JR, Tsolaki M, et al. (2004). "Genetic association of acyl-coenzyme A: cholesterol acyltransferase with cerebrospinal fluid cholesterol levels, brain amyloid load, and risk for Alzheimer's disease.". Mol. Psychiatry 8 (6): 635–8. doi:10.1038/sj.mp.4001296. PMID 12851640. 
  • Smith JL, Rangaraj K, Simpson R, et al. (2004). "Quantitative analysis of the expression of ACAT genes in human tissues by real-time PCR.". J. Lipid Res. 45 (4): 686–96. doi:10.1194/jlr.M300365-JLR200. PMID 14729857. 
  • Hori M, Miyazaki A, Tamagawa H, et al. (2004). "Up-regulation of acyl-coenzyme A:cholesterol acyltransferase-1 by transforming growth factor-beta1 during differentiation of human monocytes into macrophages.". Biochem. Biophys. Res. Commun. 320 (2): 501–5. doi:10.1016/j.bbrc.2004.05.190. PMID 15219857. 
  • Yang L, Chen J, Chang CC, et al. (2004). "A stable upstream stem-loop structure enhances selection of the first 5'-ORF-AUG as a main start codon for translation initiation of human ACAT1 mRNA.". Acta Biochim. Biophys. Sin. (Shanghai) 36 (4): 259–68. PMID 15253151. 
  • Liang JJ, Oelkers P, Guo C, et al. (2004). "Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA:cholesterol acyltransferase 2 stimulates secretion of apolipoprotein B-containing lipoproteins in McA-RH7777 cells.". J. Biol. Chem. 279 (43): 44938–44. doi:10.1074/jbc.M408507200. PMID 15308631. 
  • Yang L, Lee O, Chen J, et al. (2004). "Human acyl-coenzyme A:cholesterol acyltransferase 1 (acat1) sequences located in two different chromosomes (7 and 1) are required to produce a novel ACAT1 isoenzyme with additional sequence at the N terminus.". J. Biol. Chem. 279 (44): 46253–62. doi:10.1074/jbc.M408155200. PMID 15319423. 
  • Yang L, Yang JB, Chen J, et al. (2005). "Enhancement of human ACAT1 gene expression to promote the macrophage-derived foam cell formation by dexamethasone.". Cell Res. 14 (4): 315–23. doi:10.1038/sj.cr.7290231. PMID 15353128. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Bertram L, Hsiao M, Mullin K, et al. (2005). "ACAT1 is not associated with Alzheimer's disease in two independent family-based samples.". Mol. Psychiatry 10 (6): 522–4. doi:10.1038/sj.mp.4001646. PMID 15768051. 

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