ライフサイエンスコーパス: lecithin cholesterol acyltransferase

1 core-containing particles by incubation with lecithin:cholesterol acyltransferase.

2 nd 9 contribute to the optimum activation of lecithin:cholesterol acyltransferase.

3 inus that is 32% identical to the vertebrate lecithin:cholesterol acyltransferase, a secreted phospho

4 pairs lipid binding, cholesterol efflux, and lecithin-cholesterol acyltransferase activities of the l

5 sterol efflux, and also had markedly reduced lecithin cholesterol acyltransferase activity.

6 ion, alpha-helicity, cholesterol efflux, and lecithin-cholesterol acyltransferase activity of the rec

7 efflux activity and approximately 90% lower lecithin-cholesterol acyltransferase activity relative t

8 apoA-I form with 88.1 +/- 8.5% reduction in lecithin-cholesterol acyltransferase activity, a finding

9 changed despite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward end

10 cholesterol delivery to hepatocytes, support lecithin:cholesterol acyltransferase activity, and suppr

11 Lecithin:cholesterol acyltransferase analysis, using rec

12 Only in the absence of both lecithin cholesterol acyltransferase and apolipoprotein

13 cture suggests the possible interaction with lecithin-cholesterol acyltransferase and may shed light

14 There were no significant lecithin:cholesterol acyltransferase and lysophospholipa

15 ma HDLs enriched in apoM, cholesteryl ester, lecithin:cholesterol acyltransferase, and S1P.

16 oliferator-activated receptor modulators and lecithin-cholesterol acyltransferase-based therapy, hold

17 A-I self-associates more and activates human lecithin-cholesterol acyltransferase better than mouse a

18 ail in mice and the roles of plasma factors (lecithin-cholesterol acyltransferase, cholesterol ester

19 lism (e.g., paraoxonase, apolipoprotein A-I, lecithin:cholesterol acyltransferase, cholesterol ester

20 cle number (p = 0.0008, CI 95%: 1.58, 5.33); lecithin: cholesterol acyltransferase concentration (p =

21 discoidal particles reminiscent of those in lecithin/cholesterol acyltransferase deficiency and chol

22 Patients with lecithin: cholesterol acyltransferase deficiency have bo

23 ion of disc-associated apoA-I that binds the lecithin-cholesterol acyltransferase enzyme is well stru

24 Administration of lecithin-cholesterol acyltransferase has the potential t

25 Lecithin-cholesterol acyltransferase is a rate-limiting

26 Plasma lecithin:cholesterol acyltransferase is unchanged despit

27 sma phospholipid transfer protein (PLTP) and lecithin cholesterol acyltransferase (LCAT) activities w

28 complex than other acyltransferases such as lecithin cholesterol acyltransferase (LCAT) and acyl CoA

29 ATP-binding cassette transfer protein A1 and lecithin cholesterol acyltransferase (LCAT) gene loci.

30 Expression of human lecithin cholesterol acyltransferase (LCAT) in mice (LCA

31 Lecithin cholesterol acyltransferase (LCAT) is an enzyme

32 Binding of lecithin cholesterol acyltransferase (LCAT) to lipoprote

33 els in plasma but reduces atherosclerosis in lecithin cholesterol acyltransferase (LCAT) transgenic (

34 We show that certain proteins such as lecithin cholesterol acyltransferase (LCAT), phospholipi

35 inding to and agonizing a circulating enzyme lecithin cholesterol acyltransferase (LCAT).

36 Lecithin-cholesterol acyltransferase (LCAT) catalyzes th

37 Our previous studies have indicated that lecithin-cholesterol acyltransferase (LCAT) contributes

38 ances have been made in our understanding of lecithin-cholesterol acyltransferase (LCAT) function.

39 nzymatic and interfacial binding activity of lecithin-cholesterol acyltransferase (LCAT) is affected

40 Although the major function of lecithin-cholesterol acyltransferase (LCAT) is cholester

41 shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction.

42 rmation for protein-protein interaction with lecithin-cholesterol acyltransferase (LCAT) the enzyme f

43 CE fraction in blood is closely regulated by lecithin-cholesterol acyltransferase (LCAT) which is pro

44 The interaction of lecithin-cholesterol acyltransferase (LCAT) with apolipo

45 cholesterol acyltransferase (ACAT1), but not lecithin-cholesterol acyltransferase (LCAT), and to diff

46 ipoproteins, and had minimal reactivity with lecithin-cholesterol acyltransferase (LCAT), compared wi

47 Two naturally occurring mutants of human lecithin-cholesterol acyltransferase (LCAT), T123I and N

48 eatment of cholesterol-containing r-HDL with lecithin-cholesterol acyltransferase (LCAT), to form cho

49 Human lecithin-cholesterol acyltransferase (LCAT), which is no

50 econstituted HDL and plasma from control and lecithin-cholesterol acyltransferase (LCAT)-deficient su

51 as scavenger receptor B-1 (SRB-1) and plasma lecithin-cholesterol acyltransferase (LCAT).

52 Cholesterol binding, esterification by lecithin/cholesterol acyltransferase (LCAT) and transfer

53 ells but had diminished capacity to activate lecithin/cholesterol acyltransferase (LCAT) in vitro.

54 ted to PREG esters (PE) by the plasma enzyme lecithin: cholesterol acyltransferase (LCAT), and by oth

55 resence of N-ethylmaleimide, an inhibitor of lecithin: cholesterol acyltransferase (LCAT), whereas CU

56 mino acid residues and domains implicated in lecithin:cholesterol acyltransferase (LCAT) activation o

57 Interestingly, lecithin:cholesterol acyltransferase (LCAT) activation r

58 asic motif responsible for lipid binding and lecithin:cholesterol acyltransferase (LCAT) activation.

59 Lecithin:cholesterol acyltransferase (LCAT) activity was

60 Total endogenous plasma lecithin:cholesterol acyltransferase (LCAT) activity was

61 her the altered secondary structure affected lecithin:cholesterol acyltransferase (LCAT) activity.

62 Our laboratory previously reported that lecithin:cholesterol acyltransferase (LCAT) and LDL rece

63 efflux capacity and 37% capacity to activate lecithin:cholesterol acyltransferase (LCAT) as compared

64 Lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a

65 is mutation dramatically reduces the rate of lecithin:cholesterol acyltransferase (LCAT) catalyzed ch

66 Lecithin:cholesterol acyltransferase (LCAT) catalyzes th

67 Lecithin:cholesterol acyltransferase (LCAT) deficiencies

68 resent study was to test the hypothesis that lecithin:cholesterol acyltransferase (LCAT) deficiency w

69 Lecithin:cholesterol acyltransferase (LCAT) is a key pla

70 unesterified cholesterol (UC) by the enzyme lecithin:cholesterol acyltransferase (LCAT) is cholester

71 Lecithin:cholesterol acyltransferase (LCAT) is the major

72 We recently reported that lecithin:cholesterol acyltransferase (LCAT) knock-out mi

73 Lecithin:cholesterol acyltransferase (LCAT) plays a key

74 Because lecithin:cholesterol acyltransferase (LCAT) possesses in

75 Further, plasma lecithin:cholesterol acyltransferase (LCAT) substrate re

76 Lecithin:cholesterol acyltransferase (LCAT) then drives

77 ements appear to show that the reactivity of lecithin:cholesterol acyltransferase (LCAT) with the mut

78 ed a unique T. gondii homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzym

79 Lecithin:cholesterol acyltransferase (LCAT), an importan

80 ein A-I (apoA-I) activates the plasma enzyme lecithin:cholesterol acyltransferase (LCAT), catalyzing

81 holesteryl ester transfer protein (CETP) and lecithin:cholesterol acyltransferase (LCAT), on chromoso

82 f 7alpha-hydroxylase, Scavenger receptor B1, lecithin:cholesterol acyltransferase (LCAT), or apoA-I i

83 This pathway is critically dependent on lecithin:cholesterol acyltransferase (LCAT), which rapid

84 rately detect the esterification activity of lecithin:cholesterol acyltransferase (LCAT).

85 of the sterol esterifying enzymes, ACAT1 and lecithin:cholesterol acyltransferase (LCAT).

86 rties, apoA-I structure, and reactivity with lecithin:cholesterol acyltransferase (LCAT).

87 plasma lipoprotein particles is catalyzed by lecithin:cholesterol acyltransferase (LCAT).

88 o acid sequences identical to those of human lecithin:cholesterol acyltransferase-like lysophospholip

89 In this work, the functions of lecithin:cholesterol acyltransferase-like PLAs (LCAT-PLA

90 macrophages, due primarily to an increase in lecithin:cholesterol acyltransferase-mediated (LCAT-medi

91 human cholesteryl ester transfer protein and lecithin:cholesterol acyltransferase only function optim

92 s and cholesteryl ester transfer protein and lecithin-cholesterol acyltransferase (phosphatidylcholin

93 lipase, cholesteryl ester transfer protein, lecithin:cholesterol acyltransferase (phosphatidylcholin

94 poA-I were of similar size, composition, and lecithin:cholesterol acyltransferase reactivity when com

95 apoA-I to apoA-I(-/-) HDL in the presence of lecithin cholesterol acyltransferase reorganized the lar

96 particle types toward a major plasma enzyme, lecithin:cholesterol acyltransferase responsible for the

97 ntrast, deletion of LRO1, a homolog of human lecithin cholesterol acyltransferase, resulted in a dram

98 nd conformation, apoA-I activates the enzyme lecithin:cholesterol acyltransferase stimulating the for

99 MEDI6012 is a recombinant human lecithin-cholesterol acyltransferase that increases high

100 encoding enzymes that esterify cholesterol (lecithin : cholesterol acyltransferase), transfer choles

101 Lecithin cholesterol acyltransferase treatment alone or

102 Lecithin-cholesterol acyltransferase was unaffected by p

103 The plasma cholesterol esterification enzyme lecithin:cholesterol acyltransferase was also compared.

104 However, apoA-V was a poor activator of lecithin:cholesterol acyltransferase where the activity

105 kinetic parameters of the lipophilic enzyme lecithin:cholesterol acyltransferase, which binds to pho