15 research outputs found

    Specific proteins expression in bear serum.

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    <p>Western immunoblots and histograms of the mean + standard error of the mean (n = 8) protein expression (arbitrary units as a proportion of pooled reference black bear serum) between pre-hibernating (“Pre”) and hibernating (“Hib”) black bears using antibodies against A) α1-antitrypsin (A1AT), B) α2-macroglobulin (A2M), C) apolipoprotein A1 (ApoA1), D) haptoglobin (Hp), E) kininogen 1 (KNG), and F) transferrin (Tf). Changes in protein expression between hibernation states of individual bears are overlaid on top of the histogram. A representative western blot is shown inset, and the left and right wells are loaded with pre-hibernation and hibernation serum samples, respectively. Statistically significant differences (p<0.05, paired 1-way ANOVA) between hibernation states are indicated with asterisks. A2M was significant at p = 0.07.</p

    Protein spots identified by tandem mass spectrometric analysis and MASCOT database searching.

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    <p>Spot IDs correspond to labeled spots in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066119#pone-0066119-g001" target="_blank">Figure 1</a>.</p><p>p-values from the 1-way RMANOVA and False Discovery Rate (FDR) for each protein are shown. Fold changes are relative change in protein spot volume from pre-hibernation to hibernation.</p

    Bear serum proteomics.

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    <p>Representative images of a Cy2-stained black bear serum proteins separated by difference gel electrophoresis, utilizing a pH 4–7 (left to right) immobilized pH gradient isoelectric focusing gel strip for the 1<sup>st</sup>, horizontal separation and a 12% SDS-PAGE gel in the 2<sup>nd</sup>, vertical separation. Protein spots significantly (p<0.05) up-regulated (yellow) and down-regulated (green) proteins are indicated by colour. Protein spots that were subsequently identified by tandem mass spectrometry are indicated by numbers, which correspond to spot IDs in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066119#pone-0066119-t002" target="_blank">table 2</a>. Estimated protein molecular weights in kiloDaltons (kDa) are indicated on the right edge of the image, and estimated isoelectric points are on the bottom edge.</p

    Representative fluorescent micrograph.

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    <p>Image illustrates single (line with one arrowhead) and double-labeled surfaces (line with two arrowheads) in trabecular bone.</p

    Active Osteosarcoma at the study endpoint.

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    <p>a) Rat. Distal Metaphysis of Femur. (H&E. 200x). Replacing normal trabecular architecture are poorly differentiated neoplastic cells that are polygonal to spindle shaped with lightly eosinophilic cytoplasm. b) Rat. Distal Metaphysis of Femur. (H&E. 400x). Neoplastic cells are irregularly polygonal with indistinct cell borders and moderate amounts of cytoplasm. Nuclei contain multiple, distinct nucleoli and a mitotic figure is present (asterisk).</p

    Assessment of bone resorption over the region of interest.

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    <p>(a) There was no difference (p = 0.0627) between groups in osteoclast surface. (b) There was no difference (p = 0.1108) between groups in osteoclast number. (c) TRAP surface showed a statistically significant difference (p = 0.0152) between groups, however, pairwise comparisons (Dunn’s test) was not able to detect which groups.</p

    Radiograph severity score over time for each treatment group.

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    <p>There were no significant differences between treatment groups on any given day of imaging. There was a significant difference over all groups from Day 10 to Day 24 (p ≤ 0.001). Score shown as mean +/- SE.</p

    Micro-CT.

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    <p>3-D reconstructions of normal (top) and tumor-burdened (bottom) trabecular and cortical architecture in the distal metaphysis.</p
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