ライフサイエンスコーパス: ABCG8

1 and the cholesterol efflux genes (eg, ABCG5, ABCG8).

2 ansporter G5 (ABCG5) and ABC transporter G8 (ABCG8).

3 LXR-regulated transcripts, CYP7A1, ABCG5, or ABCG8.

4 endent post-translational N-glycosylation of ABCG8.

5 tors of disease-associated transporter ABCG5/ABCG8.

6 activity (3.2-fold, P = 0.003) only for the ABCG8-19H variant, which was also superior in nested log

7 decreased the level of high mannose form of ABCG8, a protein that heterodimerizes with ABCG5 to cont

8 ng ABCC3, ABCB6, ABCD1, ABCG1, ABCG4, ABCG5, ABCG8, ABCE1, ABCF1, ABCF2, and ABCF3, were expressed at

9 cholesterol metabolism related genes Abcg5, Abcg8, Abcg11, Cyp7a1 and Cyp8b1; and (6) induced higher

10 (1)), suggesting that expression of ABCG5 or ABCG8 alone yielded nonfunctional transporters.

11 bsorption is associated with risk alleles in ABCG8 and ABO and with CVD.

12 Variants in ABCG8 and ABO have been associated with circulating plan

13 nts a cardiovascular risk factor and to link ABCG8 and ABO variants to cardiovascular disease (CVD).

14 s may therefore mediate the relationships of ABCG8 and ABO variants with CVD.

15 ions of 6 single nucleotide polymorphisms in ABCG8 and ABO with CR in the LURIC (LUdwisghafen RIsk an

16 ic patients with a defect in either ABCG5 or ABCG8 and in either Abcg5/g8 double- or single-knockout

17 e (ABC) transporter family (six mutations in ABCG8 and one in ABCG5) in nine patients with sitosterol

18 -density lipoprotein (HDL) into bile in male Abcg8(-/-) and wild-type mice.

19 wnregulation of hepatic expression of ABCG5, ABCG8, and ABCB11 biliary transporters.

20 hepatic mRNA and protein levels of ABCG5 and ABCG8, and in hepatic mRNA levels of Niemann-Pick C1-Lik

21 Both gallstone disease and p.D19H of ABCG8 are associated with diminished cholesterol absorpt

22 ABCG5 and ABCG8 are both half-size transporters that have been pro

23 ABCG5 and ABCG8 are half-size ABC transporters that function as he

24 These data indicate that ABCG5 and ABCG8 are required for efficient secretion of cholestero

25 Thus Abcg5 and Abcg8 are required for LXR agonist-associated changes in

26 entified the hepatic cholesterol transporter ABCG8 as a locus associated with risk for gallstone dise

27 llstone disease is associated with p.D19H of ABCG8 as well as alterations of cholesterol and bile aci

28 g5 (ATP-binding cassette transporter G5) and Abcg8, but not Npc1l1 (Niemann-Pick C1 like 1), were sig

29 (canalicular) membrane when coexpressed with ABCG8, but not when expressed alone.

30 ia is caused by mutations in either ABCG5 or ABCG8, but simultaneous mutations of these genes have ne

31 Mutations in either ABCG5 or ABCG8 cause sitosterolemia, a recessive disorder charact

32 s in either ATP-binding cassette (ABC) G5 or ABCG8 cause sitosterolemia, an autosomal recessive disor

33 The mature, glycosylated forms of ABCG5 and ABCG8 coimmunoprecipitated, consistent with heterodimeri

34 The sterolin locus (ABCG5/ABCG8) confers susceptibility for cholesterol gallstone

35 ariants: ABCG5-R50C (P = 4.94 x 10(-9) ) and ABCG8-D19H (P = 1.74 x 10(-10) ) in high pairwise linkag

36 Sitosterolemia induced in Abcg5- and Abcg8-deficient mice fed a high plant sterol diet result

37 APOA5, LCAT) and two associated with LDL-C (ABCG8, DHODH).

38 n ATP-binding cassette subfamily G member 8 (ABCG8) did not associate with LDL cholesterol lowering.

39 Mutations in ABCG5 (encoding sterolin-1) or ABCG8 (encoding sterolin-2) cause this disease.

40 Mutations in two tandem ABC genes, ABCG5 and ABCG8, encoding sterolin-1 and -2, respectively, are now

41 , whereas reductions in Gata4 diminish Abcg5/Abcg8 expression and biliary cholesterol excretion.

42 importance of the 19H variant on intestinal ABCG8 feature remains to be clarified.

43 ABCG5 and ABCG8 form a complex (G5G8) that opposes the absorption

44 ABCG5 and ABCG8 form a functional complex that limits dietary phyt

45 ABCG5 and ABCG8 form heterodimers that limit absorption of dietary

46 Mice expressing no ABCG5 and ABCG8 (G5G8(-/-) mice) and their littermate controls wer

47 n of plant sterols in mice lacking ABCG5 and ABCG8 (G5G8-/- mice) profoundly perturbs cholesterol hom

48 g cassette (ABC) transporters ABCG5 (G5) and ABCG8 (G8) and is stimulated by cholesterol and by the n

49 ABGG5 (G5) and ABCG8 (G8) are ABC half-transporters that dimerize withi

50 ABCG5 (G5) and ABCG8 (G8) are ATP-binding cassette (ABC) transporters t

51 ABCG5 (G5) and ABCG8 (G8) are ATP-binding cassette half-transporters th

52 Mutations in ABCG5 (G5) or ABCG8 (G8) cause sitosterolemia, an autosomal recessive

53 binding cassette transporters ABCG5 (G5) and ABCG8 (G8) form a heterodimer that transports cholestero

54 ng cassette half-transporters ABCG5 (G5) and ABCG8 (G8) promote secretion of neutral sterols into bil

55 Deletion of the Abcg8 gene alone significantly increases the mass of int

56 rs41360247, rs6576629, and rs4953023 of the ABCG8 gene and the minor allele of rs657152 of the ABO g

57 Polymorphism in the promoter for the ABCG8 gene has been linked to variations in response to

58 Here we demonstrate that the ABCG5 and ABCG8 genes are direct targets of the oxysterol receptor

59 ve expressed the recombinant human ABCG5 and ABCG8 genes in the yeast Pichia pastoris and purified th

60 ce doubly transgenic for the human ABCG5 and ABCG8 genes rescued platelet counts and volumes.

61 s, a P1 clone containing the human ABCG5 and ABCG8 genes was used to generate transgenic mice.

62 This haplotype spans the ABCG5/ABCG8 genes, is carried by 1.8% of the islanders, and re

63 assette subfamily G members 5 or 8 (ABCG5 or ABCG8) genes.

64 Purified ABCG5 and ABCG8 had very low ATPase activities (<5 nmol min(-)(1)

65 e that encodes the hepatobiliary transporter ABCG8 has been identified as a risk factor for gallstone

66 sive, but no longer; two intronic regions in ABCG8 have now been identified.

67 inding cassette (ABC) transporters ABCG5 and ABCG8 have recently been shown to cause the autosomal re

68 nding cassette (ABC) transporters, ABCG5 and ABCG8, have been proposed to limit sterol absorption and

69 o upregulates liver and intestinal ABCG5 and ABCG8, helping to promote biliary and fecal excretion of

70 The ABCG5/ABCG8 heterodimer (G5G8) mediates excretion of neutral s

71 recombinant, epitope-tagged mouse ABCG5 and ABCG8 in cultured cells.

72 afficking of sterols, we disrupted Abcg5 and Abcg8 in mice (G5G8(-/-)).

73 Overexpressing ABCG5 and ABCG8 in mice attenuates diet-induced atherosclerosis in

74 inding cassette (ABC) transporters ABCG5 and ABCG8 in patients with sitosterolemia suggests that thes

75 sults establish a central role for ABCG5 and ABCG8 in promoting cholesterol excretion in vivo.

76 NPC1L1 and increased expression of ABCG5 and ABCG8 in small intestine.

77 an disease Sitosterolemia, the role of ABCG5/ABCG8 in sterol trafficking and how newer data implicate

78 roles of hepatic versus intestinal ABCG5 and ABCG8 in sterol transport have not yet been investigated

79 epatic messenger RNA expression of Abcg5 and Abcg8 in strain PERA/Ei correlates positively with highe

80 he canalicular cholesterol transporter ABCG5/ABCG8 in the genetic susceptibility and pathogenesis of

81 sgenic mice that overexpress human ABCG5 and ABCG8 in the liver but not intestine (liver G5/G8-Tg) in

82 no effect on the T1317 induction of ABCG5 or ABCG8 in the rat hepatoma cell line, FTO-2B.

83 To elucidate the roles of ABCG5 and ABCG8 in the trafficking of sterols, we disrupted Abcg5

84 polypeptide (NTCP), OATP1, OATP2, ABCG5, and ABCG8) in the liver.

85 protein, termed "sterolin-2" and encoded by ABCG8, is mutated in the remaining pedigrees.

86 inding cassette (ABC) transporters Abcg5 and Abcg8, is required for both the increase in sterol excre

87 transgene specifically in the intestine, and ABCG8-knockout mice.

88 inding cassette (ABC) transporters ABCG5 and ABCG8 lead to sitosterolemia, a disorder characterized b

89 g cassette (ABC) half-transporters, ABCG5 or ABCG8, lead to reduced secretion of sterols into bile, i

90 -binding cassette transporter 1 (ABCA1), and ABCG8 levels on the membrane, thus significantly reducin

91 The ABC transporters ABCG5 and ABCG8 limit absorption and promote excretion of dietary

92 for 2 single-nucleotide polymorphisms at the ABCG8 locus: rs11887534 (OR, 1.69; 95% confidence interv

93 ariants associated with LDL cholesterol near ABCG8, MAFB, HNF1A and TIMD4; with HDL cholesterol near

94 used by a genetic defect of sterolins (ABCG5/ABCG8) mapped to the STSL locus.

95 olved on pathogenesis, and the role of ABCG5/ABCG8 may extend into other metabolic processes by alter

96 cholesterol biosynthesis and promoting ABCG5/ABCG8-mediated cholesterol excretion.

97 We found that ABCG5(-/-)/G8(-/-) and ABCG8 (-/-) mice displayed the same biliary and gallston

98 male wild-type (WT), ABCG5(-/-)/G8(-/-), and ABCG8 (-/-) mice fed a lithogenic diet or varying amount

99 lstones in WT, but not ABCG5(-/-)/G8(-/-) or ABCG8 (-/-), mice.

100 etected in WT, but not ABCG5(-/-)/G8(-/-) or ABCG8 (-/-), mice.

101 40% and approximately 500%, respectively, in Abcg8(-/-) mice in the setting of constant intraduodenal

102 [(14)C]cholesterol were detected in bile of Abcg8(-/-) mice.

103 on of ABCA1 mRNA, and no change in ABCG5 and ABCG8 mRNA expression.

104 f the islanders are carriers of a frameshift ABCG8 mutation increasing PPS levels in carriers by 50%.

105 ABCG5 or ABCG8 mutations can cause sitosterolemia, in which patie

106 These data suggest that ABCG5 and ABCG8 normally cooperate to limit intestinal absorption

107 Immunoelectron microscopy revealed ABCG5 and ABCG8 on the plasma membrane of these cells.

108 anwhile, HRD1 increased the non-glycosylated ABCG8 regardless of its E3 activity, thereby suppressing

109 Mutations in either ABCG5 or ABCG8 result in an identical clinical phenotype, suggest

110 e biliary cholesterol transporters Abcg5 and Abcg8, resulting in an increase in biliary cholesterol s

111 ese data suggest that heterozygosity for the ABCG8 S107X mutation does not influence the action of di

112 nthesis) to daily PS supplementation in HET (ABCG8 S107X mutation) compared with a healthy control co

113 trate that increased expression of ABCG5 and ABCG8 selectively drives biliary neutral sterol secretio

114 RA/Ei), colocalizes with the genes Abcg5 and Abcg8 that encode the canalicular cholesterol transporte

115 -binding cassette transporter genes ABCG5 or ABCG8 that result in accumulation of xenosterols in the

116 To explore whether ABCG8, the sterol efflux (hemi-)transporter, plays a maj

117 The addition of ABCG5 and ABCG8 to the growing list of LXR target genes further su

118 balance or allelic splicing of the ABCG5 and ABCG8 transcripts in human liver limited the search to c

119 e confirmed a functional defect in the ABCG5/ABCG8 transport system.

120 ing cassette, subfamily G (WHITE), member 8 (ABCG8), two half-transporters that act as a heterodimeri

121 Both ABCG5 and ABCG8 underwent N-linked glycosylation.

122 ccelerated the degradation of both ABCG5 and ABCG8 via E3 activity-dependent manner.

123 y regulating the expression of Mtp and Abcg5/Abcg8 via Shp and Gata4.

124 To determine the site of action of ABCG5 and ABCG8, we expressed recombinant, epitope-tagged mouse AB

125 When ABCG5 and ABCG8 were coexpressed, the attached sugars were Endo H-

126 The Endo H-sensitive forms of ABCG5 and ABCG8 were confined to the endoplasmic reticulum (ER), w

127 we quantified the effect of rs4299376 (ABCG5/ABCG8), which affects the intestinal cholesterol absorpt

128 nown but involves the genes ABC1, ABCG5, and ABCG8, which are members of the ATP-binding cassette pro