INT237038
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
These include Ifi27, Ifih1, Irf7 and Oas1b which were upregulated at 72 hr and 96 hr post infection except Becn1 that was over-expressed only at 72 hr post infection, and Spn which was over-expressed at all time points.
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Levels of other components of the autophagy pathway such as Atg5, Atg10, Atg12 and Beclin-1 were not different in DLB compared to controls. | |||||||||||||||
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Beclin-1 was detected as a single band at 50 kDa that was more abundant in the membrane than the cytosolic fraction (Figure 1A, B). | |||||||||||||||
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The elevated expression of Beclin-1 and LC3-II following lethal toxin exposure was further substantiated by the overtly increased GFP-LC3 puncta staining in H9C2 cells following lethal toxin challenge. | |||||||||||||||
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Assessment of ER stress and autophagy revealed a significant increase in Bip, Beclin-1 and LC3-II expression following lethal toxin exposure, suggesting possible involvements of ER stress and autophagy. | |||||||||||||||
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Conversely, increasing Beclin 1 expression results in diminished amyloid pathology in these AD transgenic mice [57]. | |||||||||||||||
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One probable contributor to autophagy deficiency in AD appears to be Beclin 1, whose expression is strongly reduced in the brains of AD patients to levels that would be predicted to impair autophagosome synthesis [56]. | |||||||||||||||
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Genetic manipulations that decrease Beclin 1 levels in AD transgenic mice reduce neuronal autophagy, disrupt lysosomes, promote intracellular and extracellular A? | |||||||||||||||
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Recently, delivery of the Beclin 1 gene was shown to induce autophagy and reduce amyloid and ? | |||||||||||||||
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Our results revealed that lethal toxin produced subtle although significant upregulation in the expression of the ER stress maker BIP and the autophagy markers Beclin-1 and LC3-II without affecting the phospho-eIF2? | |||||||||||||||
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Neuronal overexpression of the autophagy protein Beclin1 confers resistance to Sindbis virus infections [7]. | |||||||||||||||
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BH2 mutant defective for apoptosis inhibition yet retaining Beclin1-binding and autophagy inhibition intact maintained viral genome loads equivalent to WT virus (Figure 7D, 7E, 7F down and S5D), arguing that the ? | |||||||||||||||
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These data collectively demonstrate that the BH2 domain of the hydrophobic groove of vBcl-2 is not essential for suppressing Beclin1-mediated autophagy and its elimination does not affect Beclin1 binding, whereas the elimination of ? | |||||||||||||||
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In contrast, 3T3 cells infected with the Beclin1-binding-deficient vBcl-2 mutant viruses (? | |||||||||||||||
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To analyze the interactions between the Beclin1 and vBcl-2 mutants, yeast strain AH109, expressing the BH3-like domain of Beclin1 fused to the Gal4 activation domain in the pGADT7 plasmid, was used to transform pGBKT7 plasmids containing the mutants of vBcl-2, and the transformants then assayed for ? | |||||||||||||||
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To analyze the interactions between the Beclin1 and vBcl-2 mutants, yeast strain AH109, expressing the BH3-like domain of Beclin1 fused to the Gal4 activation domain in the pGADT7 plasmid, was used to transform pGBKT7 plasmids containing the mutants of vBcl-2, and the transformants then assayed for ? | |||||||||||||||
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Similar results were also observed with endogenous Beclin1 in 293T cells, in that removal of the ? | |||||||||||||||
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(F) The superoxide generating agent menadione increases LC3-II and phosphorylation of JNK and Bcl-2, but has no effect on mTOR substrates or Beclin-1 expression. | |||||||||||||||
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Previous work has shown that oxidative stress in the form of hydrogen peroxide can increase the expression of Beclin-1 and thus induce autophagy (27). | |||||||||||||||
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We did not find that thiol antioxidants or vitamin E had any significant effect on levels of Beclin-1 (Fig. 6D and E). | |||||||||||||||
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General Comments
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