Ask about this productRelated genes to: ACAT2 Blocking Peptide
- Gene:
- ACAT2 NIH gene
- Name:
- acetyl-CoA acetyltransferase 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 6q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-04-15
- Date modifiied:
- 2014-11-19
- Gene:
- SOAT2 NIH gene
- Name:
- sterol O-acyltransferase 2
- Previous symbol:
- -
- Synonyms:
- ACAT2
- Chromosome:
- 12q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-29
- Date modifiied:
- 2015-08-26
Related products to: ACAT2 Blocking Peptide
Related articles to: ACAT2 Blocking Peptide
- Acyl-coenzyme A cholesterol acyltransferase (ACAT) is a membrane-binding enzyme localized in the endoplasmic reticulum. ACAT2 can promote the development of colon cancer, but its efficacy in lung adenocarcinoma (LUAD) remains uncertain. - Source: PubMed
Publication date: 2024/01/11
Wang ZhongchaoCao ZhugenDai Zhaoxia - - Source: PubMed
Publication date: 2022/02/10
Romeo Stefano - Sterol O-acyltransferase 2 (Soat2) encodes acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2), which synthesizes cholesteryl esters in hepatocytes and enterocytes fated either to storage or to secretion into nascent triglyceride-rich lipoproteins. - Source: PubMed
Publication date: 2022/01/13
Pramfalk CamillaAhmed OsmanPedrelli MatteoMinniti Mirko ELuquet SergeDenis Raphaël GpOlin MariaHärdfeldt JenniferVedin Lise-LotteSteffensen Knut RRydén MikaelHodson LeanneEriksson MatsParini Paolo - In contrast to human hepatocytes in vivo, which solely express acyl-coenzyme A:cholesterol acyltransferase (ACAT) 2, both ACAT1 and ACAT2 (encoded by SOAT1 and SOAT2) are expressed in primary human hepatocytes and in human hepatoma cell lines. Here, we aimed to create hepatocyte-like cells expressing the ACAT2, but not the ACAT1, protein to generate a model that - at least in this regard - resembles the human condition in vivo and to assess the effects on lipid metabolism. Using the Clustered Regularly Interspaced Short Palindromic Repeats technology, we knocked out SOAT1 in HepG2 and Huh7.5 cells. The wild type and SOAT2-only-cells were cultured with fetal bovine or human serum and the effects on lipoprotein and lipid metabolism were studied. In SOAT2-only-HepG2 cells, increased levels of cholesterol, triglycerides, apolipoprotein B and lipoprotein(a) in the cell media were detected; this was likely dependent of the increased expression of key genes involved in lipid metabolism (e.g. MTP, APOB, HMGCR, LDLR, ACACA, and DGAT2). Opposite effects were observed in SOAT2-only-Huh7.5 cells. Our study shows that the expression of SOAT1 in hepatocyte-like cells contributes to the distorted phenotype observed in HepG2 and Huh7.5 cells. As not only parameters of lipoprotein and lipid metabolism but also some markers of differentiation/maturation increase in the SOAT2-only-HepG2 cells cultured with HS, this cellular model represent an improved model for studies of lipid metabolism. - Source: PubMed
Publication date: 2020/02/11
Pramfalk CamillaJakobsson TomasVerzijl Cristy R CMinniti Mirko EObensa ClaraRipamonti FedericoOlin MariaPedrelli MatteoEriksson MatsParini Paolo - Cholesterol plays essential structural and signaling roles in mammalian cells, but too much cholesterol can cause cytotoxicity. Acyl-CoA:cholesterol acyltransferases 1 and 2 (ACAT1/2) convert cholesterol into its storage form, cholesteryl esters, regulating a key step in cellular cholesterol homeostasis. Adipose tissue can store >50% of whole-body cholesterol. Interestingly, however, almost no ACAT activity is present in adipose tissue, and most adipose cholesterol is stored in its free form. We therefore hypothesized that increased cholesterol esterification may have detrimental effects on adipose tissue function. Here, using several approaches, including protein overexpression, quantitative RT-PCR, immunofluorescence, and various biochemical assays, we found that ACAT1 expression is significantly increased in the adipose tissue of the / mice. We further demonstrated that ACAT1/2 overexpression partially inhibited the differentiation of 3T3-L1 preadipocytes. In mature adipocytes, increased ACAT activity reduced the size of lipid droplets (LDs) and inhibited lipolysis and insulin signaling. Paradoxically, the amount of free cholesterol increased on the surface of LDs in ACAT1/2-overexpressing adipocytes, accompanied by increased LD localization of caveolin-1. Moreover, cholesterol depletion in adipocytes by treating the cells with cholesterol-deficient media or β-cyclodextrins induced changes in cholesterol distribution that were similar to those caused by ACAT1/2 overexpression. Our results suggest that ACAT1/2 overexpression increases the level of free cholesterol on the LD surface, thereby impeding adipocyte function. These findings provide detailed insights into the role of free cholesterol in LD and adipocyte function and suggest that ACAT inhibitors have potential utility for managing disorders associated with extreme obesity. - Source: PubMed
Publication date: 2019/11/14
Xu YanqingDu XimingTurner NigelBrown Andrew JYang Hongyuan