Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-5

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>u region, 3R tau fragment and 3RC tau fragment, with 3-APS. Inset shows the polymers found after incubation of tau peptide (residues 317–335) with 3-APS. Bars indicate 0.2 μ

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-0

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p> protein (Tau-5) and phalloidin to identifiy actin polymers. The results obtained for untransfected (left) and tau-transfected (right) cells are shown. In the presence of Tau, tubulin bundles were observed (see arrows). Inset shows a microtubule bundle inside HEK 293 tau expressing cells. B) RNA was isolated from previously mentioned cell lines as described in Materials and methods and a quantitative RT/PCR analysis using actin RNA, as internal control, was done. The size of the amplified DNA was determined by gel electrophoresis; Tau DNA, lanes 2 and 4 and actin DNA (lanes 3 and 5) are shown. In lane 1, are Hind III fragments of φ29 DNA used as electrophoretic markers. The quantitation of the ratio Tau/actin in arbitrary units is shown. C) Total protein extract from HEK 293 and HEK 293 expressing tau was obtained and Western blot analysis using an antibody against β-actin and an antibody (ab 7.51) against Tau, was done

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-6

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>dide as described in "methods" and photographed at a fluorescence microscope. Percentages of specific cell survival were determined as described in "methods"

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-1

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>ab T14) (A) or with 0.01 % thioflavin S (Th-S) (B). Quantitation of both T14 (C) and Thioflavin S (D) fluorescence observed by fluorescence microscopy is shown. The fluorescence intensity of each sample was obtained by background subtraction. A significant fluorescence intesity increase (P < 0.05 as compared with untreated cells) is shown for both T14 and Thioflavin S staining. The average of at least three separate determinations is indicated. DAPI was used for nuclei staining

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-10

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>rgent insoluble material (see methods) was analyzed by western blot using an antibody against Tau (ab 7.51). Reaction of the unfractionated cell extract with β-actin antibody, was used as loading control. The average of at least three separate determinations is indicated. *, P < 0.05, **, P < 0.01 compared with control (Student's t test)

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-8

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p> protein (Tau-5) and phalloidin to identifiy actin polymers. The results obtained for untransfected (left) and tau-transfected (right) cells are shown. In the presence of Tau, tubulin bundles were observed (see arrows). Inset shows a microtubule bundle inside HEK 293 tau expressing cells. B) RNA was isolated from previously mentioned cell lines as described in Materials and methods and a quantitative RT/PCR analysis using actin RNA, as internal control, was done. The size of the amplified DNA was determined by gel electrophoresis; Tau DNA, lanes 2 and 4 and actin DNA (lanes 3 and 5) are shown. In lane 1, are Hind III fragments of φ29 DNA used as electrophoretic markers. The quantitation of the ratio Tau/actin in arbitrary units is shown. C) Total protein extract from HEK 293 and HEK 293 expressing tau was obtained and Western blot analysis using an antibody against β-actin and an antibody (ab 7.51) against Tau, was done

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-9

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>ab T14) (A) or with 0.01 % thioflavin S (Th-S) (B). Quantitation of both T14 (C) and Thioflavin S (D) fluorescence observed by fluorescence microscopy is shown. The fluorescence intensity of each sample was obtained by background subtraction. A significant fluorescence intesity increase (P < 0.05 as compared with untreated cells) is shown for both T14 and Thioflavin S staining. The average of at least three separate determinations is indicated. DAPI was used for nuclei staining

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-4

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>ated actin) and tau antibodies. The merged picture is also indicated. DAPI was used for nuclei staining (A). In the presence of 200 μM 3-APS, the phalloidin and Tau staining clearly decreases (B)

Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau-2

<p><b>Copyright information:</b></p><p>Taken from "Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau"</p><p>http://www.molecularneurodegeneration.com/content/2/1/17</p><p>Molecular Neurodegeneration 2007;2():17-17.</p><p>Published online 6 Sep 2007</p><p>PMCID:PMC2048960.</p><p></p>ergent insoluble material (see methods) was analyzed by western blot using an antibody against Tau (ab 7.51). Reaction of the unfractionated cell extract with β-actin antibody, was used as loading control. The average of at least three separate determinations is indicated. *, P < 0.05, **, P < 0.01 compared with control (Student's t test)

Examination of Target Genes in Late-Onset AD Brains.

<p><i>A–B</i>. qPCR of NLRP2 (<i>A</i>) and <i>ASB9</i> (<i>B</i>) from mRNA from Brodmann's area (BA38) from control and AD brains. Black bars (1–5) are controls and red bars represent AD patients (6–16), which are described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0084547#pone.0084547.s005" target="_blank">Fig S5</a>. qPCR data was normalized internally to <i>GAPDH</i> expression and also to the average of 5 control lines. Statistical significance was determined by Student's t-Test and error bars reflect SEM. For control vs. AD, n = 5 for control, n = 11 for AD, p = 0.005. <i>C</i>. List of <i>PSEN1</i> NPC target genes (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0084547#pone.0084547.s008" target="_blank">Table S2</a>) that have differential expression in independent microarray data of laser captured microdissected (LCM) cortical neurons from one of three brain areas (details in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0084547#pone.0084547.s005" target="_blank">Fig S5</a>). All comparisons are either non-demented AD pathology (NDAD) or AD versus control samples. HIP refers to hippocampus, EC for entorhinal cortex, and MTG for middle temporal gyrus. Fold change and significance (FDR: false discover rate) reflect values for LCM neuron arrays. See also <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0084547#pone.0084547.s004" target="_blank">Figure S4</a>.</p