29 research outputs found

    GAP, PPI, and startle only ratios from a representative tinnitus<sup>(+)</sup>, tinnitus<sup>(</sup><sup>βˆ’)</sup> and control rat.

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    <p>Gap-detection data showed tinnitus at 6–8 and 26–28 kHz in the tinnitus<sup>(+)</sup> rat (A), which was unaccompanied by same-frequency impairment in PPI (B), although PPI showed auditory detection impairment at 14–16 kHz. Neither the tinnitus<sup>(βˆ’)</sup> (C–D) nor the control rat (E–F) demonstrated tinnitus or auditory detection deficits. Error bars represent the standard error of the mean (SEM). * indicates p<0.05 between pre- and post-GAP, and p>0.05 between post-GAP and post-Stl-Only.</p

    Startle force for the tinnitus<sup>(+)</sup>, tinnitus<sup>(</sup><sup>βˆ’)</sup> and control groups.

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    <p>The tinnitus<sup>(+)</sup> group only demonstrated enhanced startle force during BBN background noise at 1 to 2 weeks post-exposure, but showed a dramatic increase during all carrier bands at 5 to 6 weeks (A). Enhanced startle force without background noise was also seen to a small extent at 1 to 2 weeks post-exposure, but to a much greater extent at 5 to 6 weeks (B). The tinnitus<sup>(βˆ’)</sup> group demonstrated no startle force changes (C–D) except for a decrease at 1 to 2 weeks near 26–28 kHz PPI (C–D). The control group showed no startle force changes (E–F) except for an increase at 5–6 weeks during BBN noise (E–F). The tinnitus<sup>(+)</sup> group by far showed the greatest change in startle force, suggesting hyperacusis-like behavior. All groups showed a sensitization to startle force during background noise, as evidenced by stronger startle force during gap-detection testing (background noise present) compared to PPI testing (background noise absent). For PPI tests, all startle only conditions were identical and were organized by the closest frequency of prepulse incidence to maintain similar comparison to gap-detection. Error bars represent SEM. * indicates p<0.05.</p

    Morris water maze escape latency and probe trial data.

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    <p>No significant differences were seen between the tinnitus<sup>(+)</sup>, tinnitus<sup>(βˆ’)</sup> and control groups in escape latency (A), probe trial target zone entries (B), probe trial target zone time (C), and velocity (D). This indicated similar spatial learning and memory across groups. Error bars represent SEM.</p

    Correlation between ABR thresholds and GAP ratios for tinnitus<sup>(+)</sup> (A), tinnitus<sup>(βˆ’)</sup> (B), and control (C) groups.

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    <p>No groups exhibited a significant correlation, suggesting that although tinnitus<sup>(+)</sup> rats had more overall hearing loss (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0075011#pone-0075011-g004" target="_blank">Figure 4</a>), it was not the only factor accounting for elevated GAP ratios and thus behavioral manifestation of tinnitus.</p

    Auditory brainstem responses from the exposed left ear (A) and unexposed right ear (B).

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    <p>In the exposed ear (A), both the tinnitus<sup>(+)</sup> and tinnitus<sup>(βˆ’)</sup> groups showed significant threshold shifts across tone-burst frequencies at 1 and 8 weeks post-exposure, with the strongest elevations occurring at 12 and 16 kHz. Overall, the tinnitus<sup>(+)</sup> group had significantly higher hearing thresholds than the tinnitus<sup>(βˆ’)</sup> group, although the thresholds were not significantly higher at any individual frequency or click. (B) No significant threshold shifts were seen in the unexposed ear for tinnitus<sup>(+)</sup> and tinnitus<sup>(βˆ’)</sup> groups. The control group showed no changes in either ear (A–B). Error bars represent SEM.</p

    Functional Study of miR-27a in Human Hepatic Stellate Cells by Proteomic Analysis: Comprehensive View and a Role in Myogenic Tans-Differentiation

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    <div><p>We previous reported that miR-27a regulates lipid metabolism and cell proliferation during hepatic stellate cells (HSCs) activation. To further explore the biological function and underlying mechanisms of miR-27a in HSCs, global protein expression affected by overexpression of miR-27a in HSCs was analyzed by a cleavable isotope-coded affinity tags (cICAT) based comparative proteomic approach. In the present study, 1267 non-redundant proteins were identified with unique accession numbers (score β‰₯1.3, i.e. confidence β‰₯95%), among which 1171 were quantified and 149 proteins (12.72%) were differentially expressed with a differential expression ratio of 1.5. We found that up-regulated proteins by miR-27a mainly participate in cell proliferation and myogenesis, while down-regulated proteins were the key enzymes involved in de novo lipid synthesis. The expression of a group of six miR-27a regulated proteins was validated and the function of one miR-27a regulated protein was further validated. The results not only delineated the underlying mechanism of miR-27a in modulating fat metabolism and cell proliferation, but also revealed a novel role of miR-27a in promoting myogenic tans-differentiation during HSCs activation. This study also exemplified proteomics strategy as a powerful tool for the functional study of miRNA.</p></div

    Functional Categories of Down-regulated Proteins in LX2/miR-27a Compared with LX2/miR-neg (H/L ≀0.6667).

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    <p>Proteins from LX2/miR-27a were labeled with heavy isotope (H) tagging and those from LX2/miR-neg were labeled with light isotope (L) tagging. Data were from two independent cICAT-based quantitative analyses.</p><p>Functional Categories of Down-regulated Proteins in LX2/miR-27a Compared with LX2/miR-neg (H/L ≀0.6667).</p

    Protein samples from LX2/miR-27a and LX2/miR-neg were compared by cleavable isotope-coded affinity tag (cICAT)-based quantitative proteomic analysis - identification and quantitation of ATP-citrate synthase.

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    <p>(A) Total ion chromatogram (TIC) indicating cICAT-labeled peptides eluting from a reverse phase column. (B) Expanded MS spectrum view of a pair of peaks showing the differential expression between peptides labeled with the isotopically light and heavy cICAT reagent. (C) MS/MS spectrum analysis of the light-cICAT labeled triply charged peptide (681.4 <i>m/z</i>) showed in (B) led to identification of a peptide with sequence GVTIIGPATVGGIKPGCFK (<a href="mailto:ICAT-C(C)@17" target="_blank">ICAT-C(C)@17</a>), unique to the ATP-citrate synthase (ACLY), a predicted target of miR-27a. The labels b and y designated the N- and C- terminal fragments, respectively, of the peptide produced by breakage at the peptide bond in the mass spectrometer. The number represents the number of N- or C- terminal residues present in the peptide fragment. (D) Venn diagram depicting the overlap of proteins identified in two independent cICAT experiments. Numbers in parentheses indicate the number of identified proteins for each sample. To examine the biological reproducibility, linear regression analyses were performed on H/L ratios (LX2/miR-27a/LX2/miR-neg) of two independent analyses. Pearson correlation coefficient between samples 1 and 2 was 0.8039, P<0.01.</p

    Overall distribution of miR-27a regulated proteins in LX2 cells.

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    <p>(A) Cell location and (B) Functional distribution of all the 134 differentially expressed proteins.</p

    Predicted miR-27a Targets among Down-regulated Proteins in LX2/miR-27a Identified by cICAT.

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    <p>* P<sub>CT,</sub> the probability of conserved targeting.</p><p>Predicted miR-27a Targets among Down-regulated Proteins in LX2/miR-27a Identified by cICAT.</p
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