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Results: 5

1.
Fig. 5

Fig. 5. From: Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies.

ABri1-34 oligomers are weak inducers of XBP1 splicing. (a, b) Unconventional XBP1 splicing in SY5Y cells treated with ABri1-34 oligomers, fibers and monomers at 2 μM. All the samples revealed low levels of XBP1s with no statistical differences. However, the oligomers accumulated significantly higher levels of XBP1u as confirmed by quantitation. c The S/U ratio was not significantly altered in any of the samples. *p < 0.05

Diana L. Castillo-Carranza, et al. Neurochem Res. 2012 August;37(8):1707-1717.
2.
Fig. 2

Fig. 2. From: Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies.

α-Syn, PrP106-126, and ABri1-34 oligomers induce cell death. Cell viability of SY5Y cells treated with oligomers, fibers, and monomers of α-Syn (blue), PrP106-126 (orange), and ABri1-34 (green) at 2 μM for 8 h. Oligomers for the three proteins (squared patterns) induced high toxicity resulting in around 50 % cell loss. Monomers (solid colors) did not affect cell viability, except for a slight, but significant reduction by PrP106-126. Fibers for each protein (dotted) reduced viability by about 10 %. *p < 0.05, **p < 0.01, ***p < 0.001 (Color figure online)

Diana L. Castillo-Carranza, et al. Neurochem Res. 2012 August;37(8):1707-1717.
3.
Fig. 4

Fig. 4. From: Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies.

PrP106-126 oligomers are weak inducers of XBP1 splicing. a Unconventional XBP1 splicing in SY5Y cells treated with PrP106-126 oligomers, fibers and monomers at 2 μM. All the samples had low levels of XBP1s, although both oligomers and fibers showed slightly stronger bands. b Quantitation of three experiments confirmed that XBP1s is significantly elevated only in samples treated with oligomers. Fibers induced a 50 % increase in XBP1s that was not statistically significant (p = 0.07). However, both oligomers and fibers induced the accumulation of higher levels of XBP1u. c The S/U ratio was mildly (less than double), but significantly elevated in cells treated with oligomers. *p < 0.05, **p < 0.01

Diana L. Castillo-Carranza, et al. Neurochem Res. 2012 August;37(8):1707-1717.
4.
Fig. 3

Fig. 3. From: Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies.

α-Syn oligomers are strong inducers of XBP1 splicing. a Unconventional XBP1 splicing in SY5Y cells treated with α-Syn oligomers, fibers and monomers at 2 μM detected by RT-PCR. Untreated samples along with samples treated with monomers show high levels of XBP1u and very low levels of XBP1s. Samples treated with oligomers show the opposite, with higher levels of XBP1s than XBP1u. Samples treated with fibers show a subtle increase in XBP1s. b Quantitation of three independent experiments confirmed that monomers did not increase XBP1s, but fibers significantly increased XBP1s. However, oligomers had the largest effect by far, significantly reducing the levels of XBP1u. c The S/U ratio increases 24-fold in cells treated with α-Syn oligomers. Fibers double the S/U ratio, a significant difference with respect to untreated samples. α-Syn monomers do not affect the S/U ratio. *p < 0.05, **p < 0.01

Diana L. Castillo-Carranza, et al. Neurochem Res. 2012 August;37(8):1707-1717.
5.
Fig. 1

Fig. 1. From: Differential Activation of the ER Stress Factor XBP1 by Oligomeric Assemblies.

Detection of XBP1s by RT-PCR. a SY5Y cells treated with increasing concentrations of Aß42 oligomers induce XBP1 splicing and accumulation of XBP1s, which is visualized by diagnostic digestion of XBP1u by PstI. The non-digested samples that accumulate XBP1s contain a hybrid band that runs lower than XBP1u and XBP1s (red arrows). The PstI-treated samples can help quantify XBP1s by digestion of XBP1u, but incomplete digestions complicate this effort. b Sequence of the hybrid band purified from an agarose gel. The sequence in the electropherogram matches both XBP1 isoforms until it reaches the intron (red arrow). From this point, two overlapping peaks were detected corresponding to the XBP1u intron (red sequence) and XBP1s exon 2. c Elimination of the hybrid band in gel electrophoresis. Denaturing conditions such as formamide (left) and urea (center) did not eliminate the hybrid band even when combined with heat or SDS. The size for XBP1u (U) and XBP1s (S) is shown in the left gel. Resolving the PCR in polyacrylamide gels (PAGE) produced neat XBP1s and XBP1u bands. Upon digestion with PstI, a single XBP1s band was left (Color figure online)

Diana L. Castillo-Carranza, et al. Neurochem Res. 2012 August;37(8):1707-1717.

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