INT157303
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
By immunoblot analysis, levels of LC3 in the membrane fraction were increased and Cathepsin D was reduced in the ? | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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Previous studies have demonstrated that the detection of increased LC3-II levels in the brain is very difficult, as neurons appear to clear autophagosomes very efficiently (29). | |||||||||||||||
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This also allowed us to demonstrate that this increase in LC3-II levels results from an increase in synthesis rather than a decrease in degradation of autophagosomes, as increased levels were also seen in the presence of bafilomycin A1, an autophagy inhibitor that blocks autophagosome-lysosome fusion and therefore LC3-II degradation (27) (Fig. 1E and F). | |||||||||||||||
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Double-labeling studies showed that mTor and LC3 were abundant in neurons displaying ? | |||||||||||||||
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Compared to control mice, in the APP tg mice, levels of LC3 were elevated while levels of Cathepsin D were unchanged in the membrane fraction (Figure S2A, C). | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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In addition, rapamycin increased the levels of LC3 and Cathepsin D immunoreactivity (Figure 8O, P). | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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In contrast to the results obtained in liver and brain [19], LC3 protein expression in CCDWT was very low, and cathepsin D deficiency was associated with increased expression of both light (LC3II, membrane-bound) and heavy (LC3I, cytosolic) forms of LC3. | |||||||||||||||
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Transfection of mutant CHMP2B into HEK-293 and COS-7 cells resulted in the formation of large cytoplasmic vacuoles, aberrant lysosomal localisation demonstrated by CD63 staining and impairment of autophagy indicated by increased levels of LC3-II protein. | |||||||||||||||
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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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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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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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H9c2 cells transfected with GFP-LC3 adenovirus were treated with or without anthrax lethal toxin. | |||||||||||||||
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The JNK inhibitor SP600125 down-regulated the expression of IRE1, Chop, and LC3II induced by DHC, thapsigargin, and MG132 [N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal]. | |||||||||||||||
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General Comments
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