SOAT1
Not to be confused with Acetyl-Coenzyme A acetyltransferase.
Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1, also known as SOAT1, is an enzyme that in humans is encoded by the SOAT1 gene.[1]
Function
Acyl-coenzyme A:cholesterol acyltransferase (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).[1]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
Statin Pathway edit
- ↑ The interactive pathway map can be edited at WikiPathways: "Statin_Pathway_WP430".
See also
- Acyl-CoA:cholesterol acyltransferase
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. doi:10.1097/00041433-200106000-00008. 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. doi:10.1007/BF02257489. 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. doi:10.1074/jbc.273.41.26765. 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. doi:10.1074/jbc.274.16.11060. 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. doi:10.1074/jbc.274.33.23276. 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. doi:10.1016/S0002-9440(10)64723-2. PMC 1868616. 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. PMC 139241. 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. doi:10.1093/abbs/36.4.259. 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. PMC 528928. 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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