2P-0422 Acyl-coenzyme A: cholesterol acyltransferase-2 (ACAT-2) is responsible for elevated intestinal ACAT activity in streptozotocin (STZ)-induced diabetic rats

2003 ◽  
Vol 4 (2) ◽  
pp. 131
Author(s):  
M. Hori ◽  
M. Satoh ◽  
Y. Sakamoto ◽  
M. Sakai ◽  
A. Miyazaki ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Cholesterol Acyltransferase ◽  
Diabetic Rats ◽  
Acat Activity ◽  
Acyl Coenzyme A

Ontogeny of acyl-CoA: cholesterol acyltransferase in rat liver, intestine, and adipose tissue

1992 ◽  
Vol 262 (4) ◽  
pp. G599-G602
Author(s):  
M. T. Little ◽  
P. Hahn
Keyword(s):  
Adipose Tissue ◽  
Rat Liver ◽  
Animal Studies ◽  
Coenzyme A ◽  
Cholesterol Metabolism ◽  
Cholesterol Acyltransferase ◽  
Dietary Manipulation ◽  
Acat Activity ◽  
Brown Adipose ◽  
Acyl Coenzyme A

The development of acyl-coenzyme A: cholesterol acyltransferase (ACAT), was determined in the rat liver, intestine, and white (WAT) and brown adipose tissue (BAT). Animal studies have shown that dietary manipulation of cholesterol metabolism during an animal's early development can have persistent and permanent effects. Therefore it is important that the ontogeny of ACAT, one of the key enzymes in cholesterol metabolism, be clearly established. White Wistar rats were killed on day 21 of gestation, at birth, and on postnatal days 10, 14, 18, 21, 22, 25, 30, and 60. The tissues were rapidly excised, microsomes were prepared, and the activity of ACAT was measured as the rate of incorporation of [1-14C]oleoyl coenzyme A into cholesterol esters. Age-specific changes were observed in three of the four tissues investigated. Rat liver and intestine possess significant amounts of ACAT activity throughout development with marked variations in activity during this time. ACAT activity in BAT is low and variable throughout development with the exception of high activity noted in the adult animal. WAT contained little or no ACAT activity during development.

scholarly journals The effects of low-density lipoprotein and cholesterol on acyl-coenzyme A: cholesterol acyltransferase activity in membranes from cultured human fibroblasts

1983 ◽  
Vol 216 (1) ◽  
pp. 93-100 ◽  
Author(s):  
S J P Gavigan ◽  
B L Knight
Keyword(s):  
Coenzyme A ◽  
Low Density Lipoprotein ◽  
Cholesterol Acyltransferase ◽  
Density Lipoprotein ◽  
Low Density ◽  
Intact Cells ◽  
Cultured Fibroblasts ◽  
Normal Medium ◽  
Acat Activity ◽  
Acyl Coenzyme A

Membranes prepared from cultured fibroblasts were assayed for acyl-coenzyme A: cholesterol acyltransferase (ACAT) by a method that relied exclusively on the cholesterol already present on the membranes as the sterol substrate. Changes in membrane ACAT activity during incubation of fibroblasts under a variety of conditions were similar to the changes in the rate of incorporation of oleic acid into cholesteryl esters by the intact cells. The addition of low-density lipoprotein (LDL) to fibroblasts pre-incubated with lipoprotein-deficient serum led to a transient increase in membrane ACAT activity, which reached its peak after 7h and was related to the receptor-mediated uptake and degradation of the lipoprotein by the cells. However, after incubation of the membranes with a cholesterol-rich donor lipoprotein, which resulted in an equilibration of cholesterol between membranes and donor, each preparation exhibited the same activity. In contrast with these effects of LDL, incubation of the cells with non-esterified cholesterol produced a prolonged increase in ACAT activity and an increase in the activity observed after equilibration. Furthermore, ACAT activity in cells grown with linoleic acid was higher, both before and after the addition of LDL, than that of cells grown in normal medium or with palmitate. The increase in activity produced by LDL was also greater, reflecting the greater rate of degradation of LDL by the cells, and was associated with an increase in the activity observed after equilibration with donor. The results suggest that although fibroblasts can increase the amount of active enzyme on their membranes to accommodate an exceptionally high or prolonged supply of cholesterol, under normal circumstances the increase in membrane ACAT activity produced by LDL can be explained entirely by an increase in the amount of cholesterol in the substrate pool.

Localization of acyl-coenzyme A: Cholesterol acyltransferase-1 (ACAT-1) in macrophages and other various type cells of human tissues

2000 ◽  
Vol 151 (1) ◽  
pp. 292
Author(s):  
N. Sakashita ◽  
A. Miyazaki ◽  
M. Takeya ◽  
S. Horiuchi ◽  
C.C.Y. Chang ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Cholesterol Acyltransferase ◽  
Human Tissues ◽  
Acyl Coenzyme A

scholarly journals Regulation of Rabbit Intestinal Acyl Coenzyme A-Cholesterol Acyltransferase In Vivo and In Vitro

1982 ◽  
Vol 83 (4) ◽  
pp. 873-880 ◽  
Author(s):  
F. Jeffrey Field ◽  
Allen D. Cooper ◽  
Sandra K. Erickson
Keyword(s):  
Coenzyme A ◽  
Cholesterol Acyltransferase ◽  
Acyl Coenzyme A
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