(1) This change in cholesterol esterification appears to be the result of reductions in the activity of acyl-CoA:cholesterol acyltransferase (ACAT) in the endoplasmic reticulum of the macrophages incubated with the n-3 polyunsaturated fatty acids.
(2) Acaterin also inhibited ACAT activity in the rat liver microsomes by 50% at a concentration of 120 microM.
(3) This mechanism, which is activated by changes in culture density, coordinately regulates the activities of HMG-CoA reductase and acyl-CoA:cholesterol acyltransferase (ACAT).
(4) These results suggest that ACAT activity in microsomes was affected not only by the amount of microsomal cholesterol, but also by an extra-microsomal soluble protein such as lipoproteins.
(5) ACAT activity was also determined in microsomes prepared from twenty human liver samples obtained at surgery with in vivo warm ischaemia times ranging from 5-120 min.
(6) In sterol-free medium, if sterol synthesis is blocked by specific enzyme inhibitors or through mutation, the ACAT activation by cycloheximide is again abolished.
(7) Kinetic studies indicate that DL-MA is an uncompetitive inhibitor of ACAT.
(8) The results suggest that ACAT activity in CaCo-2 cells is stimulated by cholesterol delivered to the cells by way of taurocholate micelles.
(9) Furthermore, the large beta-VLDL had a higher ACAT-stimulatory potential than the smaller beta-VLDL.
(10) A decrease in HMG-CoA reductase and an increase ACAT activity was observed compared with the corresponding values from both the groups fed on a standard diet and a fat supplemented diet with no cholesterol.
(11) The IC50 values of enniatins D, E and F for ACAT activity in an enzyme assay using rat liver microsomes were calculated to be 87, 57 and 40 microM, respectively.
(12) Except in adult rats, the HG diet always raises hepatic ACAT activity more than the HCO diet or the Purina Chow.
(13) In contrast, ACAT activity in NPD fibroblasts (cell lines from four different patients) began to increase between 6 and 12 h after serum addition, reaching levels up to 50% of normal values at 24 h. ACAT activity in NPC and NPD cell extracts could not be stimulated by preincubation with normal cell homogenates, nor was complementation between NPC and NPD homogenates observed.
(14) Apparent ACAT activity levels increased significantly in nude mouse tumours and in foetal and postnatal rat pancreata and also in postnatal liver.
(15) A 5% cholesterol diet for 3 hr produced an increase in the microsomal and plasmatic cholesterol content, a decrease in HMG-CoA reductase activity and a concomitant increase in ACAT activity.
(16) The effect of CDCA, UDCA and the cyclopropyl analogues was also tested with respect to HMG-CoA reductase and acylCoA cholesterol acyltransferase (ACAT) activities.
(17) The structure of purpactins, novel acyl-CoA:cholesterol acyltransferase (ACAT) inhibitors, was determined by spectroscopic analyses.
(18) The enhanced ACAT activity obtained by freezing was at least partly explained by a transfer of unesterified cholesterol to the microsomal fraction and possibly also by making the substrate(s) more available to the enzyme.
(19) Under these experimental conditions, treatment with insulin or with the ACAT inhibitor CL-277082 significantly reduced the plasma cholesterol to levels measured in nondiabetic rats fed the same high fat diet.
(20) DL-MA inhibited acyl CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) activity in the mucosal microsomes, with 50% inhibition occurring at approximately 0.5 microM.
Acates
Definition:
(n. pl.) See Cates.
Example Sentences:
(1) This change in cholesterol esterification appears to be the result of reductions in the activity of acyl-CoA:cholesterol acyltransferase (ACAT) in the endoplasmic reticulum of the macrophages incubated with the n-3 polyunsaturated fatty acids.
(2) Acaterin also inhibited ACAT activity in the rat liver microsomes by 50% at a concentration of 120 microM.
(3) This mechanism, which is activated by changes in culture density, coordinately regulates the activities of HMG-CoA reductase and acyl-CoA:cholesterol acyltransferase (ACAT).
(4) These results suggest that ACAT activity in microsomes was affected not only by the amount of microsomal cholesterol, but also by an extra-microsomal soluble protein such as lipoproteins.
(5) ACAT activity was also determined in microsomes prepared from twenty human liver samples obtained at surgery with in vivo warm ischaemia times ranging from 5-120 min.
(6) In sterol-free medium, if sterol synthesis is blocked by specific enzyme inhibitors or through mutation, the ACAT activation by cycloheximide is again abolished.
(7) Kinetic studies indicate that DL-MA is an uncompetitive inhibitor of ACAT.
(8) The results suggest that ACAT activity in CaCo-2 cells is stimulated by cholesterol delivered to the cells by way of taurocholate micelles.
(9) Furthermore, the large beta-VLDL had a higher ACAT-stimulatory potential than the smaller beta-VLDL.
(10) A decrease in HMG-CoA reductase and an increase ACAT activity was observed compared with the corresponding values from both the groups fed on a standard diet and a fat supplemented diet with no cholesterol.
(11) The IC50 values of enniatins D, E and F for ACAT activity in an enzyme assay using rat liver microsomes were calculated to be 87, 57 and 40 microM, respectively.
(12) Except in adult rats, the HG diet always raises hepatic ACAT activity more than the HCO diet or the Purina Chow.
(13) In contrast, ACAT activity in NPD fibroblasts (cell lines from four different patients) began to increase between 6 and 12 h after serum addition, reaching levels up to 50% of normal values at 24 h. ACAT activity in NPC and NPD cell extracts could not be stimulated by preincubation with normal cell homogenates, nor was complementation between NPC and NPD homogenates observed.
(14) Apparent ACAT activity levels increased significantly in nude mouse tumours and in foetal and postnatal rat pancreata and also in postnatal liver.
(15) A 5% cholesterol diet for 3 hr produced an increase in the microsomal and plasmatic cholesterol content, a decrease in HMG-CoA reductase activity and a concomitant increase in ACAT activity.
(16) The effect of CDCA, UDCA and the cyclopropyl analogues was also tested with respect to HMG-CoA reductase and acylCoA cholesterol acyltransferase (ACAT) activities.
(17) The structure of purpactins, novel acyl-CoA:cholesterol acyltransferase (ACAT) inhibitors, was determined by spectroscopic analyses.
(18) The enhanced ACAT activity obtained by freezing was at least partly explained by a transfer of unesterified cholesterol to the microsomal fraction and possibly also by making the substrate(s) more available to the enzyme.
(19) Under these experimental conditions, treatment with insulin or with the ACAT inhibitor CL-277082 significantly reduced the plasma cholesterol to levels measured in nondiabetic rats fed the same high fat diet.
(20) DL-MA inhibited acyl CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) activity in the mucosal microsomes, with 50% inhibition occurring at approximately 0.5 microM.