SOAT1

From Wikipedia, the free encyclopedia

Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1

Identifiers

SOAT1; ACAT1; ACAT; ACACT; RP11-215I23.2; SOAT; STAT

External IDs

OMIM: 102642 MGI: 104665 HomoloGene: 2333

Gene ontology
Molecular Function:	• sterol O-acyltransferase activity • acyltransferase activity • transferase activity
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• lipid metabolic process • circulation • steroid metabolic process • cholesterol metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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]

[edit] References

^ ^a ^b Entrez Gene: SOAT1 sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1.

[edit] 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.