ライフサイエンスコーパス: ACAT

1 ACAT activity has been implicated in the regulation of t

2 ACAT activity is found in many tissues, including macrop

3 ACAT inhibition is not an effective strategy for limitin

4 ACAT inhibitor reduced plasma cholesterol and triglyceri

5 ACAT inhibitors delayed the trafficking of immature APP

6 ACAT inhibitors have recently emerged as promising drug

7 ACAT-1 and ACAT-2 do not form hetero-oligomeric complexe

8 ACAT-1 may function as an allosteric enzyme.

9 ACAT-1 protein is located mainly in the ER.

10 ACAT-2 was expressed primarily in mouse liver and small

11 d by acyl-CoA cholesterol acyltransferase-1 (ACAT-1) enzyme.

12 itive (S58035) and non-competitive (DuP 128) ACAT inhibitors.

13 , or acyl-CoA cholesterol acyltransferase 2 (ACAT-2).

14 types resulted in the production of abundant ACAT activity which was sensitive to ACAT inhibitors.

15 E+/+/ACAT1+/+ (wild type), apoE+/+/ACAT1-/- (ACAT-/-), apoE-/-/ACAT1+/+ (apoE-/-), and apoE-/-/ACAT1-

16 In contrast to LDL SU, oleic acid, ACAT inhibition, U18666A, or beta-CD had no effects on H

17 erol ratio; increased hepatic ACAT activity, ACAT-2 mRNA, and ACAT-2 protein; and reduced LDL recepto

18 ), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES).

19 Acyl coenzyme A:cholesterol acyltransferase (ACAT) (EC 2.3.1.26) is an enzyme, located in the endopla

20 Acyl CoA:cholesterol acyltransferase (ACAT) 2 is the major cholesterol-esterifying enzyme in m

21 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) activity in the intestine may be largely derived f

22 ent of acyl-CoA:cholesterol acyltransferase (ACAT) activity.

23 enzyme acyl-CoA:cholesterol acyltransferase (ACAT) are present in the nonhuman primate hepatocyte; on

24 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) catalyzes intracellular esterification of choleste

25 Acyl-COA:cholesterol acyltransferase (ACAT) converts cholesterol to cholesteryl esters.

26 sis by acyl CoA:cholesterol acyltransferase (ACAT) enzymes in intestinal and hepatic cholesterol meta

27 acyl-coenzyme A:cholesterol acyltransferase (ACAT) esterifies cholesterol in a variety of tissues.

28 acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much attention.

29 ors of acyl CoA:cholesterol acyltransferase (ACAT) have attracted considerable interest as a potentia

30 acyl-coenzyme A:cholesterol acyltransferase (ACAT) in homogenates should have access only to choleste

31 zed by acyl-CoA:cholesterol acyltransferase (ACAT) in the endoplasmic reticulum (ER).

32 mes to acyl-CoA/cholesterol acyltransferase (ACAT) in the endoplasmic reticulum.

33 acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition led to impaired APP processing.

34 ed as acyl CoA: cholesterol acyltransferase (ACAT) inhibitors, comparison of in vivo potency with in

35 rol by acyl-CoA:cholesterol acyltransferase (ACAT) is a key element in maintaining cholesterol homeos

36 Acyl-CoA:cholesterol acyltransferase (ACAT) is a key enzyme in cellular cholesterol homeostasi

37 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is a membrane protein located in the endoplasmic r

38 Acyl-CoA:cholesterol acyltransferase (ACAT) is a membrane-bound enzyme that produces cholester

39 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is an enzyme involved in cellular cholesterol home

40 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is an integral membrane protein located in the end

41 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is an intracellular enzyme that produces cholester

42 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) plays important roles in cellular cholesterol home

43 Acyl-CoA:cholesterol acyltransferase (ACAT) plays important roles in cellular cholesterol home

44 Acyl-CoA:cholesterol acyltransferase (ACAT) plays important roles in cellular cholesterol home

45 acyl-coenzyme A:cholesterol acyltransferase (ACAT) was also defective in ASM knockout macrophages.

46 ity of acyl-CoA:cholesterol acyltransferase (ACAT), a key enzyme for maintaining the intracellular ho

47 e, and acyl-CoA:cholesterol acyltransferase (ACAT), ACAT2, small heterodimer partner, and low-density

48 cyl-coenzyme A: cholesterol acyltransferase (ACAT), an enzyme that regulates subcellular cholesterol

49 acyl-coenzyme A:cholesterol acyltransferase (ACAT), by monitoring the activity of purified human ACAT

50 zed by acyl-CoA:cholesterol acyltransferase (ACAT), competes for the incorporation of lipoprotein-der

51 zed by acyl-CoA:cholesterol acyltransferase (ACAT), plays a central role in cellular cholesterol home

52 acyl coenzyme A:cholesterol acyltransferase (ACAT), which catalyzes the formation of cholesterol este

53 acyl-coenzyme A-cholesterol acyltransferase (ACAT), which likely occurs slowly during lesion progress

54 acyl-coenzyme A:cholesterol acyltransferase (ACAT)-related enzyme (Are)2p, with 2 plasma membrane ATP

55 acyl coenzyme A:cholesterol acyltransferase (ACAT).

56 zed by acyl CoA:cholesterol acyltransferase (ACAT).

57 acyl-coenzyme A:cholesterol acyltransferase (ACAT).

58 e, and acyl-CoA:cholesterol acyltransferase (ACAT).

59 ors of acyl CoA:cholesterol acyltransferase (ACAT).

60 ity of acyl-CoA:cholesterol acyltransferase (ACAT).

61 ers by acyl-CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) is an important component of cellular

62 enzyme acyl-CoA:cholesterol acyltransferase (ACAT; EC 2.3.1.26) catalyzes the esterification of cellu

63 esterification by acyl-CoA acyltransferase (ACAT) and for inhibition of sterol regulatory element-bi

64 sferase (LCAT) and acyl CoA acyltransferase (ACAT).

65 y of acyl-CoA:cholesterol O-acyltransferase (ACAT) 2 to differentiate cholesterol from the plant ster

66 of acyl-CoA: cholesterol O-acyltransferase (ACAT) in vitro and for cholesterol lowering in cholester

67 bit acyl-CoA: cholesterol O-acyltransferase (ACAT) in vitro and to lower plasma total cholesterol in

68 bit acyl-CoA: cholesterol O-acyltransferase (ACAT) in vitro and to lower plasma total cholesterol in

69 +/- acyl-CoA:cholesterol O-acyltransferase (ACAT) inhibitor (compound 58035) for 20 h and assessed c

70 yme, acyl-CoA:cholesterol O-acyltransferase (ACAT), is thought to be critical, although the mechanism

71 yl-coenzyme A:cholesterol O-acyltransferase (ACAT).

72 acyl-coenzyme A:cholesterol acyltransferase, ACAT, the neutral cholesteryl ester hydrolase (nCEH) tha

73 s, demonstrate the presence of an additional ACAT (EC 2.1.3.26), termed ACAT2, which is localized to

74 ATP:co(I)rrinoid adenosyltransferase (ACAT) enzymes convert vitamin B12 to coenzyme B12.

75 ilies of ATP:corrinoid adenosyltransferases (ACATs) exist that are capable of converting vitamin B12

76 ATP:co(I)rrinoid adenosyltransferases (ACATs) are enzymes that catalyze the formation of adenos

77 ermed ATP:Co(I)rrinoid adenosyltransferases (ACATs), implicated in the biosynthesis of adenosylcobala

78 Although ACAT resides in the endoplasmic reticulum (ER), the chol

79 An ACAT inhibitor, Dup128, abolished FFA effects on SU, ind

80 of cholesterol esterification, either by an ACAT-1 inhibitor or by shRNA knockdown, significantly su

81 omogenates demonstrated that AKR mice had an ACAT protein with a lower molecular mass than other mous

82 rojects, has led to the identification of an ACAT gene family and provided molecular tools for determ

83 erols and undergo death in the absence of an ACAT inhibitor.

84 nts with coronary disease, treatment with an ACAT inhibitor did not improve the primary efficacy vari

85 -1-propanesulfonate, then proceeding with an ACAT-1 monoclonal antibody affinity column and an immobi

86 Infection of H5 insect cells with an ACAT-2 recombinant baculovirus resulted in expression of

87 Both ACAT-1 and ACAT-2 also catalyzed the esterification of the 3beta-hy

88 ACAT-1 and ACAT-2 do not form hetero-oligomeric complexes.

89 rol esterification activities for ACAT-1 and ACAT-2 exhibited different IC50 values when assayed in t

90 esterol pathways such as LDLR expression and ACAT activity may be crucial in the replication of norov

91 The KAS and ACAT activities were both sensitive to thiolactomycin in

92 ased hepatic ACAT activity, ACAT-2 mRNA, and ACAT-2 protein; and reduced LDL receptor, HDL receptor,

93 he relationship between adrenal toxicity and ACAT inhibition.

94 ACAT activity can be immunodepleted by anti-ACAT-2.

95 thesis, we produced specific polyclonal anti-ACAT-2 antibodies that quantitatively immunodepleted hum

96 By using specific anti-ACAT-1 antibodies in immunodepletion studies, we previou

97 aluated for bioactivity in vivo and arterial ACAT inhibition in a cell-based macrophage ACAT assay.

98 irst gene encoding the enzyme, designated as ACAT-1, was identified in 1993 through an expression clo

99 In the presence of cosubstrate ATP, ACATs raise the Co(II)/Co(I) reduction potential of thei

100 e further insight into the interplay between ACAT activation and inhibition of SREBP cleavage by 25-h

101 Both ACAT-1 and ACAT-2 also catalyzed the esterification of t

102 Sterol esterification by ACAT or homologous enzymes is conserved in evolution dat

103 cholesterol available for esterification by ACAT was a strong, independent predictor of MACE and dea

104 sterols are relatively poorly esterified by ACAT, and so they may cause macrophage death and plaque

105 Thus, inhibition of palAPP formation by ACAT or specific palmitoylation inhibitors would appear

106 ing intestinal enterocyte-like Caco-2 cells, ACAT-2 protein content increases by 5-10-fold in 6 days,

107 In hepatocyte-like HepG2 cells, ACAT-1 comprises 85-90% of the total ACAT activity, with

108 wered hepatic ACAT activity without changing ACAT-2 mRNA or protein.

109 In contrast, ACAT-2 is evident in fetal but not adult hepatocytes.

110 culate that the ability of serum to decrease ACAT activity depends on ATP binding cassette transporte

111 erparts, presumably because of the decreased ACAT activity in the macrophages.

112 e a second mammalian ACAT enzyme, designated ACAT-2, that is 44% identical to the first cloned mouse

113 rst cloned mouse ACAT (henceforth designated ACAT-1).

114 and provided molecular tools for determining ACAT's functions in vivo.

115 tine may be largely derived from a different ACAT protein.

116 s are identified, ARE1 and ARE2, that encode ACAT-related enzymes in yeast.

117 inese hamster ovary cells lacking endogenous ACAT.

118 inese hamster ovary cells lacking endogenous ACAT.

119 d that unsaturated fatty acids, by enhancing ACAT activity, reduce the amount of free cholesterol in

120 Cholesterol esterification activities for ACAT-1 and ACAT-2 exhibited different IC50 values when a

121 The recent cloning of a human cDNA for ACAT, together with genome sequencing projects, has led

122 Therefore, cysteine is not essential for ACAT catalysis.

123 phobic peptide segment, may be essential for ACAT catalysis.

124 te active site residue, is not essential for ACAT catalysis.

125 Disruption of the gene for ACAT (Acact) in mice resulted in decreased cholesterol e

126 e cysteine-free ACAT1 will facilitate future ACAT structure function studies.

127 eins, we transiently overexpressed human (h) ACAT-1 in the livers of low density lipoprotein (LDL) re

128 Because hepatic ACAT-2 is markedly upregulated in NS, we tested the hypo

129 -to-HDL cholesterol ratio; increased hepatic ACAT activity, ACAT-2 mRNA, and ACAT-2 protein; and redu

130 o-HDL cholesterol ratio, and lowered hepatic ACAT activity without changing ACAT-2 mRNA or protein.

131 However, how ACAT inhibitors act in the brain has so far remained unc

132 Human ACAT expressed in sat1 sat2 mutant cells can catalyze es

133 Human ACAT had a broad acyl-CoA substrate specificity, the oth

134 y was detected from strains expressing human ACAT when cholesterol was equilibrated with the microsom

135 Four human ACAT-1 mRNAs (7.0, 4.3, 3.6, and 2.8 kilobases (kb)) sha

136 ies that quantitatively immunodepleted human ACAT-2, a 46-kDa protein expressed in Chinese hamster ov

137 that stably expresses the recombinant human ACAT-1 protein bearing an N-terminal hexahistidine tag.

138 The results show that human ACAT-1 in the ER contains seven transmembrane domains.

139 various hydrophilic regions within the human ACAT-1 protein and used immunofluorescence microscopy to

140 her and exhibit 23 percent identity to human ACAT.

141 results collectively suggest that in humans, ACAT-2 performs significant catalytic roles in the fetal

142 Moreover, we identified ACAT activity in T. gondii that can be modulated by phar

143 In ACAT-deficient SRD4, CHO cells stably transfected with h

144 Patients in the highest tertile of change in ACAT activity had a significantly higher risk for MACE (

145 serum samples that induce larger changes in ACAT activity contain increased levels of HDL particles

146 Serum-induced changes in ACAT activity did not correlate with HDL levels or the p

147 d in decreased cholesterol esterification in ACAT-deficient fibroblasts and adrenal membranes, and ma

148 dextrin, which leads to a marked increase in ACAT-mediated cholesterol esterification.

149 Genetic ablation of each individual ACAT results in parasite growth impairment whereas dual

150 In the small intestine, ACAT-2 is concentrated at the apices of the villi, where

151 bly act nonselectively against the two known ACATs.

152 yclic amides potently inhibited rabbit liver ACAT (IC50's = 0.014-0.11 microM), and the majority of c

153 In the human liver, ACAT-1 is present in both fetal and adult hepatocytes.

154 ntly inhibit liver microsomal and macrophage ACAT in vitro and exhibit good cholesterol lowering acti

155 l ACAT inhibition in a cell-based macrophage ACAT assay.

156 nds were evaluated for cell-based macrophage ACAT inhibition, bioactivity, and adrenal toxicity.

157 ing (36a-d), in general, improved macrophage ACAT inhibitory activity and provided excellent choleste

158 emarkably, another portion of the macrophage ACAT pattern did not overlap with PDI or ribophorin, but

159 In macrophages, ACAT is thought to participate in foam cell formation an

160 We now demonstrate that ACAT2 is the major ACAT in mouse small intestine and liver, and suggest tha

161 We now describe a second mammalian ACAT enzyme, designated ACAT-2, that is 44% identical to

162 Mechanically, ACAT-1 inhibition increased intracellular free cholester

163 tency with in vitro activity in a microsomal ACAT assay indicates no correlation between activity in

164 microM in an in vitro rat hepatic microsomal ACAT assay, ED50 = 0.72 mg/kg/day in cholesterol-fed ham

165 Liver microsomal ACAT activity was 2-3-fold higher in cynomolgus monkeys

166 ever, significantly reduced liver microsomal ACAT inhibitory activity (IC50 > 1 microM).

167 In some animal models, ACAT inhibitors have antiatherosclerotic effects.

168 Studies utilizing small molecule ACAT inhibitors show that ACAT plays a key role in PREG

169 ACAT1 or ACAT2 exhibited significantly more ACAT activity than their sitosterol-loaded counterparts.

170 t is 44% identical to the first cloned mouse ACAT (henceforth designated ACAT-1).

171 sion studies and the disruption of the mouse ACAT gene (Acact) have indicated that more than one ACAT

172 The mouse ACAT-2 gene (Acact2) maps to chromosome 15 in a region c

173 Our results identify a novel ACAT-dependent mechanism that regulates secretory traffi

174 Among the numerous ACAT inhibitors known, pyripyropene A (PPPA) is the only

175 Consistent with these observations, ACAT inhibition increased cell FC and reduced LDL SU by

176 re dishes, contained approximately 10-15% of ACAT on the cell surface.

177 lar cholesterol or the intrinsic activity of ACAT, neither of which was changed significantly by the

178 The identification and cloning of ACAT-2 will facilitate molecular approaches to understan

179 cations may reveal an important component of ACAT regulation and macrophage foam cell formation.

180 ch to investigate the subunit composition of ACAT-1.

181 anding possible physiological differences of ACAT in these locations may reveal an important componen

182 studies are needed to explore the effect of ACAT inhibition in nephrotic humans.

183 Expression of ACAT-1 showed a correlation with poor patient survival.

184 in activity (though not gene expression) of ACAT.

185 The form of ACAT in macrophages, ACAT1, contributes to foam cell for

186 ors can selectively target specific forms of ACAT.

187 owledge concerning the molecular genetics of ACAT.

188 ogical inhibition or genetic inactivation of ACAT decrease lipid raft palAPP levels by up to 76%, lik

189 or expression via a mechanism independent of ACAT.

190 ed during liver perfusion as an indicator of ACAT activity, was significantly higher in cynomolgus mo

191 Inhibition of ACAT activity decreases Abeta generation in cell- and an

192 ctive action in MC65 cells and inhibition of ACAT along with the upregulation of cholesterol transpor

193 we tested the hypothesis that inhibition of ACAT may improve cholesterol metabolism in NS.

194 Pharmacological inhibition of ACAT reverses NS-induced LDL receptor, HDL receptor, and

195 m this series, 9f, was a potent inhibitor of ACAT in both the microsomal and cellular assays.

196 f NV proteins and RNA, whereas inhibitors of ACAT significantly reduced the replication of NV in repl

197 Despite a lower level of ACAT activity, the ACAT1-expressing cells esterified 4-f

198 In contrast, the livers of ACAT-deficient mice contained substantial amounts of cho

199 to determine the subcellular localization of ACAT in macrophages.

200 e embedded in the dense reticular network of ACAT.

201 microscopy, we found that a major portion of ACAT was in a dense reticular cytoplasmic network and in

202 utant, resulting in high level production of ACAT protein, but low in vivo esterification of ergoster

203 linking the presumed allosteric property of ACAT with cholesterol trafficking into and out of the en

204 inding will be useful in testing the role of ACAT and macrophage foam cell formation in atheroscleros

205 ular approaches to understanding the role of ACAT enzymes in mammalian biology.

206 derlines the important physiological role of ACAT enzymes to store cholesterol in a sterol-auxotrophi

207 pter include the pathophysiological roles of ACAT, the biochemistry and molecular biology of the ACAT

208 ope tag sequence was appended to a series of ACAT cDNAs truncated after each predicted transmembrane

209 used co-immunoprecipitation of both types of ACAT-1 proteins.

210 There are three families of ACATs, namely, CobA, EutT, and PduO.

211 One ACAT-1 genomic DNA insert covers exons 1-16 and a promot

212 ne (Acact) have indicated that more than one ACAT exists in mammals and specifically that another enz

213 This motif is absent in other ACAT families, suggesting that EutT employs a distinct m

214 tive enzyme; 2) a silent allele at the other ACAT locus that does not produce detectable mRNA; and 3)

215 utT is dimeric in solution, and unlike other ACATs, EutT catalyzes the reaction with sigmoidal kineti

216 Partial ACAT inhibition by F-1394 had antiatherogenic effects in

217 Partial ACAT inhibition may have therapeutic potential in the cl

218 dii that can be modulated by pharmacological ACAT inhibitors with a consequent detrimental effect on

219 how that without cholesterol, PREG is a poor ACAT substrate; with cholesterol, the V(max) for PREG es

220 l]diphenylacetamide (4a) was the most potent ACAT inhibitor identified (IC50 = 0.04 microM in an in v

221 2 (ACAT2), earlier shown to be the principal ACAT enzyme within primate hepatocytes, as a regulator o

222 Pure ACAT-1 dispersed in mixed micelles containing sodium tau

223 ma membrane cholesterol pool before reaching ACAT.

224 ol-induced macrophage death does not require ACAT dysfunction and so may occur in an accelerated fash

225 le, we identified and characterized a second ACAT-like enzyme, TgACAT2, which shares 56% identity wit

226 lues when assayed in the presence of several ACAT-specific inhibitors, demonstrating that ACAT inhibi

227 lesterol, the IC(50) value toward a specific ACAT inhibitor, and sensitivity toward heat inactivation

228 In summary, ACAT was found in several sites in macrophages: a cytopl

229 he untagged ACAT-1 or the 6-histidine-tagged ACAT-1 yielded a single radiolabeled band of predicted s

230 the monomer, supporting the conclusion that ACAT-1 is a homotetrameric enzyme.

231 In this study, we demonstrate that ACAT and cholesterol esters play a crucial role in the o

232 ACAT-specific inhibitors, demonstrating that ACAT inhibitors can selectively target specific forms of

233 odepletion studies, we previously found that ACAT-1, a 50-kDa protein, plays a major catalytic role i

234 These results support the hypothesis that ACAT is an allosteric enzyme regulated by cholesterol.

235 ll intestine, supporting the hypothesis that ACAT-2 contributes to cholesterol esterification in thes

236 Here we show that ACAT inhibition retains a fraction of APP molecules in t

237 ing small molecule ACAT inhibitors show that ACAT plays a key role in PREG esterification in various

238 These results show that ACAT-1 exists as homo-oligomers in intact Chinese hamste

239 The hydropathy plot suggests that ACAT-1 protein contains multiple transmembrane segments.

240 olecular biology of the ACAT protein and the ACAT gene, and the mode of regulation by sterol or nonst

241 ts: 1) a point mutation in one allele at the ACAT locus that changes codon 265 from Ser to Leu, resul

242 Cloning the ACAT gene provides the necessary tool to advance molecul

243 spite these coding sequence differences, the ACAT protein from the ald allele catalyzed cholesterol e

244 ycin-induced NS were treated with either the ACAT inhibitor CI-976 or placebo for 2 weeks.

245 ng sites; the structural requirement for the ACAT activator site is more stringent than it is for the

246 or site is more stringent than it is for the ACAT substrate site.

247 Mutation of these serines inactivated the ACAT enzymes.

248 tion, suggesting that Cys467 may be near the ACAT active site(s).

249 In adult intestines, most of the ACAT activity can be immunodepleted by anti-ACAT-2.

250 Correction of the ACAT deficiency by transfection of a wild-type cDNA fail

251 omes and not due to direct inhibition of the ACAT enzyme.

252 the structures and mechanisms of two of the ACAT families have been studied extensively, little is k

253 and human genes, an additional number of the ACAT gene family was identified in humans.

254 he biochemistry and molecular biology of the ACAT protein and the ACAT gene, and the mode of regulati

255 tients were randomly assigned to receive the ACAT inhibitor pactimibe (100 mg per day) or matching pl

256 y 25-hydroxycholesterol, indicating that the ACAT deficiency and the sterol regulatory defect are cau

257 ll specific manner, and furthermore that the ACAT reactions exhibit differential FFA utilization.

258 We used the ACAT inhibitor avasimibe, which was previously tested in

259 for cholesteryl ester (CE) synthesis via the ACAT reaction.

260 tern-type diet without (control) or with the ACAT inhibitor F-1394 (effective against ACAT1 and ACAT2

261 ogenic lipoprotein, did not overlap with the ACAT label, but rather were embedded in the dense reticu

262 Full-length cDNA clones for these ACAT related gene products (ARGP) 1 and 2 were isolated

263 T activity, with the remainder attributed to ACAT-2.

264 ase (ASAT) which are functionally related to ACAT.

265 bundant ACAT activity which was sensitive to ACAT inhibitors.

266 First, LDL cholesterol transport to ACAT can be blocked without inhibiting the movement of c

267 Second, LDL cholesterol transport to ACAT is normal in a Chinese hamster ovary mutant with de

268 ant parasites are particularly vulnerable to ACAT inhibitors.

269 ary mutant with defective plasma membrane-to-ACAT movement.

270 significantly correlated to microsomal total ACAT activity in both species; ACAT1 mass was less well

271 cells, ACAT-1 comprises 85-90% of the total ACAT activity, with the remainder attributed to ACAT-2.

272 acyl coenzyme A (acyl-CoA):ACP transacylase (ACAT) activity in a 1:0.12 ratio.

273 lso catalyzes the acyl-CoA:ACP transacylase (ACAT) reaction typically exhibited by KASIII enzymes, bu

274 by the acylCoA:cholesterol acyl transferase (ACAT) reaction.

275 nzyme A (CoA): cholesterol acyl transferase (ACAT).

276 Two ACAT genes (ACAT1 and ACAT2) have been identified.

277 Two ACAT genes have been identified; ACAT1 is expressed ubiq

278 In mammals, two ACAT genes (ACAT1 and ACAT2) have been identified.

279 To explore the hypothesis that the two ACAT enzymes have separate functions, the membrane topol

280 utants retained 20% or more of the wild-type ACAT activity.

281 analogous to that utilized by the PduO-type ACATs, where in both cases the polar coordination of the

282 EutT is the least understood ACAT.

283 cipitations of cells expressing the untagged ACAT-1 or the 6-histidine-tagged ACAT-1 yielded a single

284 When ACAT-1 with two different tags were co-expressed in the

285 anoid suppression was markedly enhanced when ACAT was inhibited and prevented when late endosomal/lys

286 nt increases by 5-10-fold in 6 days, whereas ACAT-1 protein content remains relatively constant.

287 entrated at the apices of the villi, whereas ACAT-1 is uniformly distributed along the villus-crypt a

288 indicated that membranes not associated with ACAT did not contribute cholesterol to this reaction.

289 ence that the adrenal toxicity observed with ACAT inhibitors may not be mechanism related.

290 P was reduced in brains of mice treated with ACAT inhibitors, and strongly correlated with reduced br