Acyl‐coenzyme A:cholesterol acyltransferases

Chang, Ta-Yuan; Li, Bo-Liang; Chang, Catherine C. Y.; Urano, Yasuomi

doi:10.1152/ajpendo.90926.2008

Cited by 443

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Acyl‐coenzyme A:cholesterol acyltransferases

Chang, Ta-Yuan, Li, Bo-Liang, Chang, Catherine C. Y., Urano, Yasuomi·2009·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.90926.2008

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Abstract

The enzymes acyl-coenzyme A (CoA):cholesterol acyltransferases (ACATs) are membrane-bound proteins that utilize long-chain fatty acyl-CoA and cholesterol as substrates to form cholesteryl esters. In mammals, two isoenzymes, ACAT1 and ACAT2, encoded by two different genes, exist. ACATs play important roles in cellular cholesterol homeostasis in various tissues. This chapter summarizes the current knowledge on ACAT-related research in two areas: 1) ACAT genes and proteins and 2) ACAT enzymes as drug targets for atherosclerosis and for Alzheimer's disease.

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Cholesterol storage is predominantly driven by ACAT1, which catalyzes the esterification of cholesterol to produce cholesteryl esters (CEs).
“Cholesterol storage is predominantly driven by the resident endoplasmic reticulum protein Acyl‐coenzymeA: Cholesterol Acyltransferase 1 (ACAT1), 4 which catalyzes the esterification of cholesterol to produce cholesteryl esters (CEs). 5 , 6”
From Inhibition of Acyl‐CoenzymeA: Cholesterol Acyltransferase 1 promotes shedding of soluble triggering receptor on myeloid cells 2 (TREM2) and low‐density lipoprotein receptor 1 (LRP1)‐dependent phagocytosis of amyloid beta protein in microglia (2025) · cites this paper as [4]
ACAT catalyzes intracellular cholesterol esterification, reducing the ER-free cholesterol pool by forming cholesteryl esters stored as lipid droplets.
“The endoplasmic reticulum (ER)-resident ACAT catalyzes intracellular cholesterol esterification, critical in this context as it reduces the ER-free cholesterol (ER-FC) pool by the formation of CE stored as LD [56].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [56]

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Authors: Chang, T.-Y., Li, B.-L., Chang, C. C. Y., & Urano, Y.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2009-07
Volume: 297
Issue: 1
Pages: E1-E9
ISSN: 0193-1849
1522-1555
DOI: 10.1152/ajpendo.90926.2008
Cited by: 443
References: 2
Language: en

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Acyl‐coenzyme A:cholesterol acyltransferases

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