ライフサイエンスコーパス: I-FABP

1 I-FABP remained at baseline through day 5 (range 0-50 ng

2 I-FABP Trp displayed two rotational correlation times, 6

3 I-FABP was released into the peripheral circulation earl

4 I-FABP was repetitively measured in nine intestinal tran

5 CRP, TNF, sIL-6R, I-FABP, sCD14, D-dimer, and HA levels were elevated in a

6 4 I-FABP is highly homologous to that of A54 I-FABP, with the same overall three-dimensional fold tha

7 .001); progressors also had higher IL-6 and I-FABP levels over the 5-year study period (P = .02 and

8 CRP, IL-6, and I-FABP were not associated with worse cognitive performa

9 d for PCTV budding activity; only L-FABP and I-FABP (23% the activity of L-FABP) were active.

10 iver fatty acid-binding protein (L-FABP) and I-FABP.

11 testinal fatty acid-binding proteins (L- and I-FABP) as well as four other proteins.

12 ciations between sCD14 and both HIV load and I-FABP, shedding new light on the relationships between

13 he correlations between HIV load, sCD14, and I-FABP.

14 esidues V26-N35, S53-R56, and A73-T76 of apo I-FABP were characterized by rapid hydrogen exchange, lo

15 and in the NOE-derived NMR structures of apo I-FABP.

16 holo-I-FABP, the structure ensemble for apo-I-FABP exhibited variability in a discrete region of the

17 ability represented backbone disorder in apo-I-FABP.

18 re, the 1.2-A X-ray crystal structure of apo-I-FABP did not exhibit this backbone disorder.

19 Average interval between I-FABP determination and biopsy was 3.4 days (SD=4.2 day

20 on, release, and targeting of fatty acids by I-FABP within the cell.

21 bility, while oleoyl CoA and CoASH decreased I-FABP Trp limiting anisotropy (order).

22 perative days 3 (baseline), 6 or 7 (elevated I-FABP), 10, and 14 (sacrifice).

23 somatic cell hybrids selected for endogenous I-FABP expression (hBRIE 380i cells) demonstrated a 5-fo

24 e amino acid mutants of the intestinal FABP (I-FABP) and determined the rate constants for binding an

25 ), liver FABP (L-FABP), and intestinal FABP (I-FABP).

26 ciation constants (K(FA)) of fatty acids for I-FABP.

27 A-FABP interactions were quite different for I-FABP and A-FABP proteins.

28 y a reflection of larger kappa on values for I-FABP and smaller kappa off values for H-FABP.

29 assay, we monitored the competition for free I-FABP between ANS and fatty acids and thereby extracted

30 P) was exploited to devise an assay for free I-FABP.

31 that the absolute rate of AOFA transfer from I-FABP is faster than from L-FABP.

32 The rate of AOFA transfer from I-FABP is independent of ionic strength, directly depend

33 rongly suggest that fatty acid transfer from I-FABP to membranes occurs by direct collisional interac

34 centrations (P < .001) and marginally higher I-FABP than other groups (P = .07).

35 The amide 1H/15N resonances for apo and holo I-FABP were assigned at 25 degrees C, and gradient- and

36 ajority of the residues in both apo and holo I-FABP were characterized by relatively slow hydrogen ex

37 However, unlike holo-I-FABP, the structure ensemble for apo-I-FABP exhibited

38 exerts on the functional properties of human I-FABP.

39 Immunoreactive I-FABP appears to hold significant potential as a bioche

40 reduce affinities by about 100-fold, but in I-FABP, R106A increases affinities up to 30-fold.

41 80i cells) demonstrated a 5-fold increase in I-FABP transcripts in response to PYY (within 6 h) that

42 Minor increases in I-FABP were often associated with histologically normal

43 However, oleic acid and CoASH increased I-FABP Trp segmental mobility, while oleoyl CoA and CoAS

44 Early ART was associated with increased I-FABP levels but normalization of TNF, sIL-6R, and D-di

45 yte fatty acid binding proteins, intestinal (I-FABP) and liver (L-FABP), was examined by time-resolve

46 yte (A-FABP), heart (H-FABP), and intestine (I-FABP) were determined by using stopped-flow fluorometr

47 infants had higher sCD14 and IL-6 but lower I-FABP than HIV-exposed and HIV-unexposed infants (P < .

48 linear correlation with the concentration of I-FABP, a protein that is thought to transport fatty aci

49 The sustained expression of I-FABP transcripts in the villar tips suggests (unlike L

50 tion in physical terms of the interaction of I-FABP with fatty acids.

51 ve therapy initiated when elevated levels of I-FABP were detected in the serum resulted in graft salv

52 g with acrylodan the Leu72 --> Ala mutant of I-FABP.

53 on correlated with the expression pattern of I-FABP mRNA in the hBRIE 380i cells where changes in tra

54 transition has implications for the role of I-FABP in cellular fatty acid transport and targeting.

55 equired element of the beta-clam topology of I-FABP.

56 -less, essentially all-beta-sheet variant of I-FABP and that the helical domain is not a required ele

57 e helical domain, we engineered a variant of I-FABP by deleting residues 15-31 and inserting a Ser-Gl

58 s study, we employed a helix-less variant of I-FABP known as delta 17-SG to investigate the role of t

59 Only I-FABP mRNA was detected in the villus tips.

60 l CoA, oleic acid, nor CoASH altered overall I-FABP rotational correlation time.

61 on binding to intestinal fatty acid protein (I-FABP) was exploited to devise an assay for free I-FABP

62 t rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 degreesC, and, for comparison,

63 The intestinal fatty acid binding protein (I-FABP) belongs to a family of 15 kDa clamshell-like pro

64 human intestinal fatty acid binding protein (I-FABP) belongs to a family of intracellular lipid bindi

65 Intestinal fatty acid-binding protein (I-FABP) binds a single molecule of long-chain fatty acid

66 Intestinal fatty acid-binding protein (I-FABP) binds FFA and may be involved in their cytosolic

67 f rat intestinal fatty acid-binding protein (I-FABP) complexed with palmitate has been determined usi

68 d rat intestinal fatty acid-binding protein (I-FABP) exhibits a beta-clam topology comprised of two f

69 d rat intestinal fatty acid-binding protein (I-FABP) has been determined using triple-resonance three

70 d rat intestinal fatty acid-binding protein (I-FABP) have been characterized and compared using amide

71 , and intestinal fatty acid-binding protein (I-FABP) in order to determine the effect of soluble prot

72 serum intestinal fatty acid-binding protein (I-FABP) would result in graft salvage.

73 rker (intestinal fatty acid binding protein (I-FABP)) were measured in 253 women (73% HIV-infected).

74 f the intestinal fatty acid-binding protein (I-FABP), at locations in the fatty acid (FA) binding sit

75 tein, intestinal fatty acid binding protein (I-FABP), is detectable in serum only after intestinal in

76 lasma intestinal fatty acid binding protein (I-FABP), soluble CD14 (sCD14), interleukin 6 (IL-6), and

77 body, intestinal fatty acid-binding protein (I-FABP), soluble CD14 (sCD14), interleukin 6 (IL-6), int

78 n the intestinal fatty acid binding protein (I-FABP), we hypothesize that ligand binding in I-BABP is

79 , and intestinal fatty acid binding protein (I-FABP).

80 ls of intestinal fatty acid-binding protein (I-FABP/FABP2), a marker of gut damage, and of soluble CD

81 over (intestinal fatty acid binding protein [I-FABP]), lipopolysaccharide-induced monocyte activation

82 which shares 30% sequence identity with rat I-FABP.

83 iological concentrations of PYY can regulate I-FABP and place this peptide in a key position as part

84 associations between progression and sCD14, I-FABP, and IL-6 levels were unchanged in models control

85 nd nonprogressors, the association of sCD14, I-FABP, and IL-6 levels with liver disease progression s

86 Serum I-FABP levels do not predict clinical intestinal allogra

87 Serum I-FABP returned to baseline.

88 Serum I-FABP was measured daily until the time of sacrifice.

89 In untreated animals, serum I-FABP remained elevated for several days and then retur

90 Following transplantation baseline serum I-FABP (day 2 or 3) averaged < or = 10.0 ng/ml.

91 direct comparison between human A54 and T54 I-FABP has now been performed to help elucidate the stru

92 The solution structure of T54 I-FABP is highly homologous to that of A54 I-FABP, with

93 ghtly stronger binding of fatty acids to T54 I-FABP does not originate from residues in direct contac

94 formation are more sensitive to ligands than I-FABP.

95 The results clearly demonstrate that I-FABP is not essential for dietary fat absorption.

96 We tested the hypothesis that I-FABP serves an essential role in the assimilation of d

97 We propose that I-FABP functions as a lipid-sensing component of energy

98 In previously published work, we showed that I-FABP was not detectable in the serum of isografted Lew

99 Previous studies in animals suggest that I-FABP might be a useful marker of intestinal allograft

100 We obtained these constants for the I-FABP ligands oleic acid, arachidonic acid, and palmiti

101 with a more hydrophobic binding site for the I-FABP proteins.

102 parinaroyl CoA were much less ordered in the I-FABP ligand binding site than with L-FABP.

103 As, and/or CoASH differentially modulate the I-FABP and L-FABP dynamics, and the ligand binding sites

104 ith increasing FA solubility for most of the I-FABP as compared with the A-FABP proteins, consistent

105 lly, the A-FABP proteins, in contrast to the I-FABP proteins, reveal significant heat capacity change

106 atty acid is not rigidly anchored within the I-FABP binding pocket, but rather has considerable freed

107 r dichroism measurements indicated that this I-FABP variant, termed delta 17-SG, has a high beta-shee

108 Restriction of the analysis to I-FABP determinations 1 day before or on the day of biop

109 this study are consistent with FA binding to I-FABP involving an initial interaction with Arg-56 foll

110 we found in earlier work with ANS binding to I-FABP.

111 and can itself displace fatty acids bound to I-FABP.

112 These two I-FABP forms display differential binding and transport

113 pared and contrasted with those of wild-type I-FABP and a single-site mutant, R106T.

114 ion rates for both delta 17-SG and wild-type I-FABP increased with increasing oleate concentration, b

115 ociation rates for delta 17-SG and wild-type I-FABP that were comparable.

116 was less stable to denaturant than wild-type I-FABP, but the folding-unfolding transition was highly

117 erns similar to those observed for wild-type I-FABP, except for the selective absence of resonances a

118 y 20-100-fold higher than that for wild-type I-FABP.

119 ed cyclosporine (CsA, 15 mg/kg/d, p.o.) when I-FABP rose to > or = 80 ng/ml.

120 rafts, whereas rejection often occurred when I-FABP was not detectable.

121 he unbound fatty acid concentration, whereas I-FABP may be involved in the uptake and/or specific tar

122 Such effects were not observed with I-FABP.