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 inhibition is not an effective strategy for limitin

3 ACAT inhibitor reduced plasma cholesterol and triglyceri

4 ACAT inhibitors delayed the trafficking of immature APP

5 ACAT inhibitors have recently emerged as promising drug

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

7 ACAT-1 may function as an allosteric enzyme.

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

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

10 ACATs have gained attention as potential drug targets fo

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

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

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

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

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

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

41 Acyl-CoA:cholesterol acyltransferase (ACAT) mediates cellular cholesterol esterification.

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 ion of acyl-CoA:cholesterol acyltransferase (ACAT) triggered rapid internalization of a biochemically

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

47 alized acyl-CoA:cholesterol acyltransferase (ACAT) which leads to the depletion of accessible cholest

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

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

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

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

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

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

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

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

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

57 acyl coenzyme A:cholesterol acyltransferase (ACAT).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

72 cyl-coenzyme A:cholesterol acyltransferases (ACATs) catalyse the transfer of an acyl group from acyl-

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 o mobilize accessible cholesterol through an ACAT-dependent mechanism.

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

86 -1-propanesulfonate, then proceeding with an ACAT-1 monoclonal antibody affinity column and an immobi

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

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

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

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

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

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

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

94 sequence kernel association test (SKAT), and ACAT-V.

95 he relationship between adrenal toxicity and ACAT inhibition.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

118 inese hamster ovary cells lacking endogenous ACAT.

119 inese hamster ovary cells lacking endogenous ACAT.

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

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

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

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

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

125 Therefore, cysteine is not essential for ACAT catalysis.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

141 her and exhibit 23 percent identity to human ACAT.

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

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

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

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

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

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

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

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

150 In mature adipocytes, increased ACAT activity reduced the size of lipid droplets (LDs) a

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

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

153 bly act nonselectively against the two known ACATs.

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

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

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

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 In atherosclerotic plaque macrophages, ACAT promotes cholesteryl ester accumulation, resulting

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

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

163 Mechanically, ACAT-1 inhibition increased intracellular free cholester

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

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

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

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

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

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

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

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

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

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

174 Interestingly, however, almost no ACAT activity is present in adipose tissue, and most adi

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

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

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

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

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

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

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

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

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

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

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

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

187 ors can selectively target specific forms of ACAT.

188 owledge concerning the molecular genetics of ACAT.

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

190 or expression via a mechanism independent of ACAT.

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

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

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

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

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

196 ned whether short-term partial inhibition of ACAT, in combination with an enhanced systemic FC accept

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

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

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

200 to determine the subcellular localization of ACAT in macrophages.

201 e embedded in the dense reticular network of ACAT.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

218 Partial ACAT inhibition may have therapeutic potential in the cl

219 evious studies showed that long-term partial ACAT inhibition, achieved by dietary supplementation wit

220 , these results show that short-term partial ACAT inhibition, coupled to increased cholesterol efflux

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

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

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

224 2 (ACAT2), earlier shown to be the principal ACAT enzyme within primate hepatocytes, as a regulator o

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

226 ma membrane cholesterol pool before reaching ACAT.

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

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

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

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

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

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

233 h as the aggregated Cauchy association test (ACAT) can also be utilized.

234 opose an aggregated Cauchy association test (ACAT), a general, powerful, and computationally efficien

235 , we use ACAT to construct a set-based test (ACAT-V) that is particularly powerful in the presence of

236 s, we use ACAT to construct an omnibus test (ACAT-O) that combines the strength of multiple complimen

237 ments the SKAT and the burden test, and that ACAT-O has a substantially more robust and higher power

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

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

240 ommunities (ARIC) study, we demonstrate that ACAT-V complements the SKAT and the burden test, and tha

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

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

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

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

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

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

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

248 n LD and adipocyte function and suggest that ACAT inhibitors have potential utility for managing diso

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

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

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

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

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

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

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

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

257 Mutation of these serines inactivated the ACAT enzymes.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

273 bundant ACAT activity which was sensitive to ACAT inhibitors.

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

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

276 ant parasites are particularly vulnerable to ACAT inhibitors.

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

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

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

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

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

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

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

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

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

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

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

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

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

290 EutT is the least understood ACAT.

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

292 by combining variant-level p values, we use ACAT to construct a set-based test (ACAT-V) that is part

293 different variant-set-level p values, we use ACAT to construct an omnibus test (ACAT-O) that combines

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

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

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

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

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

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

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