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1.

Figure 7.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Increased urokinase-type plasminogen activator receptor (uPAR) expression in lungs from mice challenged with LPS in vivo. (A) Lung sections (5 μm) from WT and uPA−/− mice challenged with phosphate-buffered saline or LPS were stained with anti-uPAR antibody. Representative fields from one of three mice for each condition are shown at 200× magnification. The negative control (−Ve) shows lung sections from LPS-challenged WT mice incubated with nonimmune rabbit IgG. (B) Lung sections (5 μm) from WT and uPA−/− mice challenged with phosphate-buffered saline (C, control) or LPS were stained with hematoxylin and eosin. Representative fields illustrating the findings of all of the mice for each condition are shown at 200× magnification.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
2.
<b>Figure 6.</b>

Figure 6.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

The role of urokinase-type plasminogen activator (uPA) in LPS-induced uPA receptor (uPAR) expression by alveolar epithelial cells isolated from mouse lungs. Membrane proteins (100 μg/lane) extracted from alveolar epithelial cells of phosphate-buffered saline or LPS-challenged WT or uPA−/− mice were separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) under nonreducing conditions. The resolved proteins were then electrotransferred to nitrocellulose membranes and immunoblotted with anti-uPAR antibody. The same membranes were then stripped and developed with β-actin antibody to confirm equal loading. The bar graph shows the results (mean + SD) from three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
3.
<b>Figure 8.</b>

Figure 8.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Effect of LPS on phosphoglycerate kinase (PGK) phosphorylation and its interaction with urokinase-type plasminogen activator receptor (uPAR) mRNA coding region (CDR). PGK isolated from lung homogenates of WT and uPA−/− mice challenged with phosphate-buffered saline (PBS) or LPS, as described in Figure 6, were separated on 8% sodium dodecyl sulfate–polyacrylamide gels under nonreducing conditions. PGK was transferred to nitrocellulose membranes. The membranes were analyzed for PGK-uPAR mRNA CDR interaction by Northwestern assay using a 32P-labeled uPAR mRNA CDR probe. The same membranes were later stripped and analyzed for tyrosine phosphorylation and total PGK expression by Western blotting using anti-phosphotyrosine and anti-PGK antibodies, respectively. The bar graph shows mean and (+ SD) densitometric values from three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
4.
<b>Figure 5.</b>

Figure 5.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Role of urokinase-type plasminogen activator (uPA) in LPS-induced uPA receptor (uPAR) expression in mouse lungs. (A) Membrane proteins (100 μg/lane) isolated from lung homogenates of phosphate-buffered saline or LPS-challenged wild-type (WT) or uPA−/− mice were separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) under nonreducing conditions and transferred to nitrocellulose membranes. The membranes were immunoblotted with anti-uPAR antibody. The same membranes were later stripped and developed with β-actin antibody for equal loading. The bar graph shows the results (mean + SD) from three independent experiments. (B) Total RNA (20 μg) isolated from lung homogenates of the above-treated mice was separated on 1% agarose/formaldehyde gels and subjected to Northern blotting using 32P-labeled uPAR cDNA and β-actin cDNA probes. The results shown are representative of three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
5.
<b>Figure 2.</b>

Figure 2.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Stabilization of urokinase-type plasminogen activator receptor (uPAR) mRNA by LPS. Beas2B cells were incubated with phosphate-buffered saline (PBS) or LPS for 12 hours to induce maximum expression of uPAR mRNA. Ongoing transcription was later blocked by adding 5, 6-dichloro-1-β-D-ribofuranosyl benzamidazole (DRB) (20 μg/ml) to the same media. Total RNA was isolated and uPAR mRNA level was measured at predefined time points after addition of DRB by Northern blot using a 32P-labeled uPAR cDNA probe, followed by hybridization with a β-actin probe to assess for equal loading. The line graph represents the percentage of mRNA decay relative to Time 0 (designated 100%), calculated from the mean values obtained by integrating the densities of individual bands from two independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
6.
<b>Figure 9.</b>

Figure 9.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

The role of LPS on hnRNPC binding to urokinase-type plasminogen activator receptor (uPAR) mRNA 3′ untranslated region (UTR) and hnRNPC tyrosine phosphorylation. hnRNPC protein isolated from crude lung extracts of WT and uPA−/− mice challenged with phosphate-buffered saline or LPS were separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) under nonreducing conditions and transferred to nitrocellulose membranes. The membranes were later analyzed for uPAR 3′ UTR mRNA interaction by Northwestern assay using a 32P-labeled uPAR mRNA 3′ UTR probe. The same membranes were stripped and analyzed for tyrosine phosphorylation and total hnRNPC expression by Western blotting using anti-phosphotyrosine and anti-hnRNPC antibodies, respectively. The bar graph represents the data (mean + SD) from three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
7.
<b>Figure 3.</b>

Figure 3.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Effect of LPS on the interaction of phosphoglycerate kinase (PGK) with urokinase-type plasminogen activator receptor (uPAR) mRNA coding region (CDR) in Beas2B cells. (A) Beas2B cells grown in culture plates to near confluence were incubated with phosphate-buffered saline or LPS (20 μg/ml) for 0 and 24 hours. PGK was isolated from these cells, as described in the methods, separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE), and transferred to nitrocellulose membranes. The membranes were then hybridized with 32P-labeled uPAR CDR mRNA. The same membranes were later stripped and analyzed for PGK protein by Western blot analysis using anti-PGK antibody. The line graph represents the ratio of uPAR CDR mRNA binding activity to PGK protein from three independent experiments shown as the mean ± SD. (B) Beas2B cells grown in culture plates to near confluence were incubated with LPS (20 μg/ml) for 0–24 hours. PGK was isolated from these cells, separated by SDS-PAGE and transferred to nitrocellulose membranes. The membranes were processed as described above. The line graph presents results from three independent experiments shown as the mean ± SD.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
8.
<b>Figure 4.</b>

Figure 4.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

Effect of LPS on heterogeneous nuclear ribonucleoprotein C (hnRNPC) and urokinase-type plasminogen activator receptor (uPAR) mRNA 3′ UTR binding in Beas2B cells. (A) Beas2B cells grown in culture plates were incubated with phosphate-buffered saline or LPS for 0 and 24 hours, as described in Figure 3. hnRNPC proteins were isolated from these cell lysates, and processed as described above. The line graph represents the mean and SD from three independent experiments. (B) Beas2B cells grown in culture plates were incubated with LPS for 0–24 hours, as described above. hnRNPC proteins were isolated from these cell lysates, separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE), and transferred to nitrocellulose membranes. The membranes were later incubated with [32P]uPAR mRNA 3′ untranslated region. Western blot analysis using anti-hnRNPC antibody was performed on the same membranes after stripping. The line graph represents the mean and SD from three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.
9.
<b>Figure 1.</b>

Figure 1.. From: Post-Transcriptional Regulation of Urokinase-type Plasminogen Activator Receptor Expression in Lipopolysaccharide-induced Acute Lung Injury.

LPS induces urokinase-type plasminogen activator (uPA) receptor (uPAR) expression in lung epithelial cells: (A) Beas2B cells were exposed to phosphate-buffered saline (PBS) or LPS (20 μg/ml) for 0–24 hours in serum-free media. The membrane proteins were separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) and transferred to nitrocellulose membranes. The membranes were analyzed for uPAR protein using anti-uPAR antibody. The same membranes were stripped and analyzed for β-actin protein to assess equal loading. (B) Total RNA isolated from Beas2B cells exposed to LPS, as in (A) using TRI-reagent, was analyzed for uPAR mRNA expression by Northern blotting using a 32P-labeled uPAR cDNA probe. The same membranes were later stripped and hybridized with a β-actin probe to affirm loading equality. The experiments were repeated three times. In (A) and (B), results from a representative experiment are shown. The graphs show the mean (± SD) density of individual bands from three independent experiments.

Yashodhar P. Bhandary, et al. Am J Respir Crit Care Med. 2009 February 15;179(4):288-298.

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