Acyl coenzyme A:cholesterol acyltransferase (ACAT) is an intracellular enzyme that catalyzes the formation of cholesterol esters from cholesterol and long-chain fatty acyl-coenzyme A. It is believed that ACAT plays a key role in lipoprotein metabolism and atherogenesis. Recently our laboratory succeeded in molecular cloning and functional expression of human macrophage ACAT cDNA. We have now mapped the ACAT gene to chromosome 1, band q25 by using fluorescence in situ hybridization to metaphase chromosomes, and by Southern blotting analysis of human--hamster somatic cell hybrid panels.

Download full-text PDF

Source
http://dx.doi.org/10.1007/BF02257489DOI Listing

Publication Analysis

Top Keywords

acyl coenzyme
8
coenzyme acholesterol
8
acholesterol acyltransferase
8
localization acyl
4
acyltransferase gene
4
gene human
4
human chromosome
4
chromosome 1q25
4
1q25 acyl
4
acat
4

Similar Publications

Ergosterol alleviates hepatic steatosis and insulin resistance via promoting fatty acid β-oxidation by activating mitochondrial ACSL1.

Cell Rep

January 2025

State Key Laboratory of Natural Medicines, School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing, Jiangsu, China. Electronic address:

Sterols target sterol-sensing domain (SSD) proteins to lower cholesterol and circulating and hepatic triglyceride levels, but the mechanism remains unclear. In this study, we identify acyl-coenzyme A (CoA) synthetase long-chain family member 1 (ACSL1) as a direct target of ergosterol (ES). The C-terminal domain of ACSL1 undergoes conformational changes from closed to open, and ES may target the drug-binding pocket in the acetyl-CoA synthetase-like domain 1 (ASLD1) of ACSL1 to stabilize the closed conformation and maintain its activity.

View Article and Find Full Text PDF

De novo lipogenesis protects dormant breast cancer cells from ferroptosis and promotes metastasis.

Redox Biol

December 2024

Department of Genomic Medicine, GENYO, Centre for Genomics and Oncology, Pfizer-University of Granada and Andalusian Regional Government, PTS, Granada, Spain; Department of Physiology, Institute of Nutrition and Food Technology "José Mataix Verdú", Biomedical Research Center, University of Granada, Granada, Spain. Electronic address:

Dormant disseminated tumor cells (DTCs) remain viable for years to decades before establishing a clinically overt metastatic lesion. DTCs are known to be highly resilient and able to overcome the multiple biological hurdles imposed along the metastatic cascade. However, the specific metabolic adaptations of dormant DTCs remain to be elucidated.

View Article and Find Full Text PDF

Advancing de novo lipogenesis: Genetic and metabolic insights.

Cell Metab

January 2025

Section of Endocrinology, Diabetes, and Metabolism, Department of Medicine, Baylor College of Medicine, Houston, TX, USA. Electronic address:

De novo lipogenesis (DNL) is the process whereby cells synthesize fatty acids from acetyl-CoA, contributing to steatosis in fatty liver disease. Two new studies, using genetic mouse models, metabolomics, and pharmacology, identified alternative pathways in DNL and unexpected physiological effects when targeting key enzymes in this pathway.

View Article and Find Full Text PDF

Supernatants from Newly Isolated P4 Ameliorate Adipocyte Metabolism in Differentiated 3T3-L1 Cells.

Biomedicines

December 2024

Department of Biochemistry, Microbiology and Physics, Faculty of Agriculture, Trakia University, 6000 Stara Zagora, Bulgaria.

() strains and their postbiotics show potential for managing metabolic disorders such as diabetes and obesity. Two newly isolated strains, M2.1 and P4, were yielded from anthills in Sinite Kamani National Park, Bulgaria.

View Article and Find Full Text PDF

Lysine succinylation, and its reversal by sirtuin-5 (SIRT5), is known to modulate mitochondrial fatty acid β-oxidation (FAO). We recently showed that feeding mice dodecanedioic acid, a 12-carbon dicarboxylic acid (DC) that can be chain-shortened four rounds to succinyl-CoA, drives high-level protein hypersuccinylation in the peroxisome, particularly on peroxisomal FAO enzymes. However, the ability of SIRT5 to reverse DC-induced peroxisomal succinylation, or to regulate peroxisomal FAO in this context, remained unexplored.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!