ライフサイエンスコーパス: jasplakinolide

1 en demonstrated in a formal synthesis of (+)-jasplakinolide.

2 withdrawal, nor did it modify sensitivity to jasplakinolide.

3 within 3 minutes of treatment with 1 microM jasplakinolide.

4 rption, we used the F-actin stabilizing drug jasplakinolide.

5 was blocked by the actin-polymerizing agent, jasplakinolide.

6 be reversed by the actin-polymerizing agent jasplakinolide.

7 retreated with the actin filament stabilizer jasplakinolide.

8 MEK1/2 and ERK1/2 activation is nullified by jasplakinolide.

9 formation is inhibited by cytochalasin D and jasplakinolide.

10 dulation of skeletal protein architecture by jasplakinolide.

11 lly when actin filaments are stabilized with jasplakinolide.

12 essentially identical to those obtained with jasplakinolide.

13 ith latrunculin B, C. difficile toxin B, and jasplakinolide.

14 ntrast, increasing actin polymerization with jasplakinolide (0.5 microm) increased SM22 and SM alpha-

15 This led to the isolation of jasplakinolide (1) and eleven jasplakinolide analogues (

16 ied using cell-permeable actin polymerizing (jasplakinolide, 2 microm) or depolymerizing agents (latr

17 ids, and the former is a known source of (+)-jasplakinolide (7), which is inactive as a 15-HLO inhibi

18 king myofibrillar filamentous (F)-actin with jasplakinolide, a cell-permeant F-actin-binding toxin, b

19 In contrast, jasplakinolide, a drug that enhances actin polymerizatio

20 Jasplakinolide, a drug that prevents actin filament disa

21 tively depolymerizes actin and is blocked by jasplakinolide, a drug which stabilizes actin filaments.

22 Jasplakinolide, a membrane-permeable actin-polymerizing

23 ilized by culturing elongating bristles with jasplakinolide, a membrane-permeant inhibitor of actin f

24 ent of an actin filament stabilizing regent, jasplakinolide, abrogated arsenic-induced NADPH oxidase

25 We found that latrunculin A (LatA) and jasplakinolide, actin drugs that release mDia1 from acti

26 Jasplakinolide also induced internalization of Trp3 and

27 ngly, however, stabilization of F-actin with jasplakinolide also resulted in a dose-dependent inhibit

28 tion of actin polymerization (latrunculin-A, jasplakinolide) also collapsed the actomyosin network.

29 alasin B, cytochalasin D, latrunculin A, and jasplakinolide, also inhibited Ebola virus GP-mediated e

30 e the actin cytoskeleton (cytochalasin D and jasplakinolide) altered the plasma membrane mobility of

31 Jasplakinolide, an actin polymerizing agent known to cau

32 Jasplakinolide, an actin polymerizing agent, mimics the

33 Finally, treatment with jasplakinolide, an inhibitor of actin turnover, resulted

34 e isolation of jasplakinolide (1) and eleven jasplakinolide analogues (3-13) including seven new anal

35 is study was to isolate and study additional jasplakinolide analogues from two taxonomically distinct

36 eloped, dolastatin 11 was twice as active as jasplakinolide and 4-fold more active than phalloidin.

37 es of the actin-stabilizing natural products jasplakinolide and chondramide C.

38 ed optical tweezers to analyze the effect of jasplakinolide and cyclodextrin on the force exerted by

39 -permeant actin cytoskeleton-modifying drugs jasplakinolide and latrunculin A to investigate the acti

40 Jasplakinolide and latrunculin B did not prevent inhibit

41 somato/dendritic release was also blocked by jasplakinolide and latrunculin, suggesting that priming

42 However, in contrast to jasplakinolide and phalloidin, dolastatin 11 did not inh

43 as demonstrated by stiffening in response to jasplakinolide and the abrogation of spreading.

44 statin 11 was qualitatively more active than jasplakinolide and, in a quantitative assay we developed

45 cific actin ligands such as latrunculin B or jasplakinolide, antibody to the actin regulatory protein

46 emia are blocked by actin stabilization with jasplakinolide, as well as proteasome inhibition with MG

47 Jasplakinolide B (11) exhibited potent cytotoxicity (GI(

48 ith a greatly reduced ability to bind actin, jasplakinolide B, did not enhance apoptosis.

49 ally consistent with the localization of the jasplakinolide-binding site at an interface of three act

50 Because jasplakinolide both decreases the amount of sequestered

51 Ouabain, an Na(+)-K(+)-ATPase inhibitor, and jasplakinolide both prevent approximately 50% of the ATP

52 to but fails to depolymerize phalloidin- or jasplakinolide-bound actin filaments.

53 underlying force generation were reduced by jasplakinolide but not by cyclodextrin.

54 to those of the sponge-derived depsipeptide jasplakinolide, but dolastatin 11 was about 3-fold more

55 Treatment of these cells with jasplakinolide caused rapid and dramatic effects on the

56 tent, whereas polymerization of F-actin with jasplakinolide causes VSM contraction and decreased G-ac

57 This effect of jasplakinolide correlated with its ability to stabilize

58 inolide were found to be separable; 1 microM jasplakinolide could permeate cells, bind cellular filam

59 Experiments with mycalolide B and jasplakinolide demonstrate that neuropeptidergic DCV mot

60 Blocking actin dynamic turnover with jasplakinolide demonstrates that dynamic actin is requir

61 s and G-actin depletion, by the marine toxin jasplakinolide, destabilised the endogenous PPP1R15A-PP1

62 Actin modulation by latrunculin or jasplakinolide did not affect AQP4-M23 diffusion, but de

63 In live, permeabilised cells, jasplakinolide did not inhibit filament assembly from su

64 We also demonstrate that an actin inhibitor, jasplakinolide, diminishes spin-mediated enhancement.

65 Like jasplakinolide, dolastatin 11 induced the hyperassembly

66 Like jasplakinolide, (-)-doliculide caused the hyperassembly

67 experiments inducing actin stabilisation by Jasplakinolide, emphasising that the actin cytoskeleton

68 tin stabilization by the cell permeant agent jasplakinolide enhanced cell death upon interleukin (IL)

69 is, the actin modifying drugs phalloidin and jasplakinolide enhanced secretion, while latrunculin-A i

70 Expected consequences of jasplakinolide function are consistent with the experime

71 Jasplakinolide had no effect on HCO3- absorption in tubu

72 ore, the stabilization of actin network with jasplakinolide had no effect on virus yields.

73 did not change the rate of mean disassembly, Jasplakinolide halted it completely, indicating that the

74 ed unchanged when applying Latrunculin A and Jasplakinolide in low doses, except that additional freq

75 atin 11 was about 3-fold more cytotoxic than jasplakinolide in the cells studied.

76 Treatment of CTLL-20 cells with jasplakinolide, in the presence or absence of recombinan

77 itive stimulation, whereas actin polymerizer jasplakinolide increases the number of active boutons in

78 Jasplakinolide-induced actin polymerization synergizes w

79 These jasplakinolide-induced filaments decorated with myosin s

80 broblasts, there was a delay in the onset of jasplakinolide-induced inhibition of lamellipodium protr

81 ends of actin filaments by model fitting of jasplakinolide-induced temporal changes in G-actin conce

82 t assembly/disassembly with latrunculin-A or jasplakinolide induces an approximately twofold increase

83 eters in vitro define the mechanism by which jasplakinolide induces polymerization of monomeric actin

84 nsulin secretion, whereas stabilization with jasplakinolide inhibited secretion, consistent with the

85 Latrunculin significantly enhanced, and jasplakinolide inhibited, high-K(+)-evoked somato/dendri

86 Jasplakinolide inhibits actin disassembly, and latruncul

87 eation, the enhancement of polymerization by jasplakinolide is amplified in the presence of actin-mon

88 Jasplakinolide is the only readily available drug that s

89 parasites with the filament-stabilizing drug jasplakinolide (JAS) and monitored the distribution of a

90 Here, we report the near-atomic structure of jasplakinolide (JAS)-stabilized PfAct1 filaments determi

91 e actin-stabilizing and depolymerizing drugs jasplakinolide (Jasp) and latrunculin B, we demonstrate

92 We used jasplakinolide (jasp), a cell-permeable macrocyclic pept

93 Treatment of murine ovaries with muM Jasplakinolide (JASP), an actin polymerization-promoting

94 when actin depolymerization was inhibited by jasplakinolide, LPL peptide-induced adhesion was inhibit

95 y, enriching the cortical cytoskeleton using jasplakinolide maintained raft probe co-clustering, CD45

96 Jasplakinolide markedly enhances the rate of actin filam

97 with cytochalasin D or stabilizing them with jasplakinolide negates the effects of suppressing or act

98 Neither jasplakinolide nor cyclodextrin affected force or veloci

99 A detailed analysis of the effects of jasplakinolide on the kinetics of actin polymerization s

100 e anti-CD3 antibodies, treatment with either jasplakinolide or latrunculin A abolished granule exocyt

101 Disrupting actin filament dynamics with jasplakinolide or latrunculin A arrested fusion at a lat

102 50% by slowing actin filament turnover with jasplakinolide or latrunculin A.

103 Jasplakinolide paradoxically stabilizes actin filaments

104 or analysis, we compared (-)-doliculide with jasplakinolide, phalloidin, and chondramide C to gain in

105 Jasplakinolide prevented amiloride-induced actin remodel

106 y contrast, stabilizing actin filaments with jasplakinolide prevented cytochalasin D-, latrunculin A-

107 Jasplakinolide prevents the carbachol inhibition of ilea

108 a membrane-permeable stabilizer of F-actin, jasplakinolide, prevents antigen-stimulated changes in D

109 trunculin B and the actin stabilization drug jasplakinolide rapidly disrupted transport of secretory

110 In addition, (-)-doliculide, like jasplakinolide, readily displaced a fluorescent phalloid

111 genes have been deleted, rendering normally jasplakinolide-resistant yeast cells sensitive to its ef

112 clear ERK, whereas actin polymerization with jasplakinolide restored nuclear translocation of activat

113 and disassembly cycle with latrunculin A or jasplakinolide results in near complete cessation of all

114 le inhibition of microfilament dynamics with jasplakinolide results in reduced numbers of viral antig

115 Stabilization of F-actin by jasplakinolide significantly reduced the ability of glut

116 Jasplakinolide stabilization of the actin cytoskeleton i

117 Like phalloidin, jasplakinolide stabilizes F-actin and promotes actin pol

118 L, and stabilization of polymerized actin by jasplakinolide suppressed the morphological conversion.

119 Conversely, treating with jasplakinolide to enhance actin polymerization increased

120 Using cytochalasin D and jasplakinolide to selectively inhibit actin retrograde f

121 ted cells compared with control and 1 microM jasplakinolide-treated cells.

122 Jasplakinolide-treated tachyzoites were unable to invade

123 Inhibition of actin polymerization alone by jasplakinolide treatment failed to reproduce the inhibit

124 to treatment with the actin-binding compound jasplakinolide upon IL-2 deprivation.

125 tion induced by the actin polymerizing agent jasplakinolide was not altered by deletion of Dicer, sug

126 Jasplakinolide was not toxic to CTLL-20 cells, nor was a

127 When jasplakinolide was used to overcome the severing action

128 In cells the two activities of jasplakinolide were found to be separable; 1 microM jasp

129 these biochemical assays (-)-doliculide and jasplakinolide were quantitatively virtually identical i

130 formation is unaffected by cytochalasin D or jasplakinolide, whereas its ability to inhibit MEK1/2 an

131 d, and is assessed here using the actin drug jasplakinolide, which has two known activities - inhibit

132 We found that 25 nM of jasplakinolide, which is known to inhibit actin filament

133 n B was partially blocked by the addition of jasplakinolide, which promotes actin assembly.

134 Unlike store-mediated Ca2+ entry, jasplakinolide, which reorganises actin filaments into a

135 Jasplakinolide, which stabilizes F-actin, or latrunculin

136 tin, as treatment with a synthetic analog of jasplakinolide with a greatly reduced ability to bind ac

137 ithin 1-5 minutes of treatment with 1 microM jasplakinolide, without any perturbation of actin organi