Observation of B+ → χc0K+

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Immunohistochemical analysis of RANKL in C4-2 tumored tibiae of control, prevention, and treatment groups

<p><b>Copyright information:</b></p><p>Taken from "Host-derived RANKL is responsible for osteolysis in a C4-2 human prostate cancer xenograft model of experimental bone metastases"</p><p>http://www.biomedcentral.com/1471-2407/7/148</p><p>BMC Cancer 2007;7():148-148.</p><p>Published online 3 Aug 2007</p><p>PMCID:PMC2034387.</p><p></p> Paraffin-embedded C4-2 tumored tibiae of the SCID mice were sectioned and stained for RANKL (negative control staining is shown in inset box). The tumor cells stained positively for RANKL. : Blood was collected to determine serum PSA levels by IMx Total PSA assay. Serum PSA levels were not significantly different between the C4-2 control with PBS injections (control), C4-2 with a concomitant subcutaneous injection of huRANKL MAb (5 mg/kg once a week) at implantation (prevention group), or C4-2 with a subcutaneous injection of huRANKL MAb (5 mg/kg biweekly, starting 3 weeks after implantation of C4-2 cells) (treatment group). Results are presented as mean ± SE

車輌運動データを利用した冬期路面状態の予測に関する研究

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Figure S1 from Novel Regulation of Integrin Trafficking by Rab11-FIP5 in Aggressive Prostate Cancer

Supplementary Figure 1. PC3N cells are negative for β4 integrin expression. DU145 and PC3N cells were labelled with an antibody against β4 integrin and cell surface levels of β4 integrin were measured using flow cytometry. Flow histograms of β4 integrin surface levels (top panel) in unlabeled PC3N cells (solid line), PC3N cells labelled with a non-specific fluorophore conjugated secondary antibody (2{degree sign} Ab only, dotted line) and DU145 (shaded solid line) and PC3N (dashed line) cells labeled with antibody against β4 integrin. The mean peak fluorescence values are reported for each condition (bottom panel).</p

Figure S3 from Novel Regulation of Integrin Trafficking by Rab11-FIP5 in Aggressive Prostate Cancer

Supplementary Figure 3. Recycling kinetics and cell membrane expression of β4 integrin in Rab11-FIP5 depleted cells. DU145 cells were transfected with non-targeting siRNA (siCon), and siRNA against Rab11-FIP5 (siFIP5) or α6 integrin (siα6). (A) Recycling kinetic curve for β4 integrin in untreated and siFIP5 DU145 cells. Percent label recycled to the cell surface at 25{degree sign}C (calculated as percent mean peak fluorescence of recycled label at a given timepoint vs total label internalized) is plotted for different time intervals. First order kinetic curve is fitted (R2>0.98). (B) Maximum label recycled (%) and recycling rate constants (observed, kobs and actual, kactual) calculated as per first order rate kinetics. Results represent 5 independent experiments. Statistical significance calculated for changes in label recycled at each timepoint and maximum label recycled as per student's t-test, unpaired, **p<0.01, n=5. (C) Flow histogram (top) and relative mean peak fluorescence of cell surface expression of β4 integrin assessed by immunolabelling in fixed, non-permeabilized untreated (shaded solid line), siCon (solid line), siFIP5 (dashed line) and siα6 (dotted line) cells (**p<0.01, n=5).</p

Supplementary Figure from Therapeutic Implications for Intrinsic Phenotype Classification of Metastatic Castration-Resistant Prostate Cancer

Supplementary Figure from Therapeutic Implications for Intrinsic Phenotype Classification of Metastatic Castration-Resistant Prostate Cance

Figure S4 from Novel Regulation of Integrin Trafficking by Rab11-FIP5 in Aggressive Prostate Cancer

Supplementary Figure 4. α3 integrin recycled to lamellipodia. Surface α3 integrin was labelled with P1B5 rabbit antibody in adherent DU145 cell monolayer and allowed to internalize for 40 minutes at 37{degree sign}C. Uninternalized label remaining at the cell membrane is detected and blocked from internalization using Alexa 568 conjugated anti-rabbit secondary antibody. P1B5 antibody bound integrin protected inside the cells was allowed to recycle back and subsequently reacted with Alexa 488 conjugated anti-rabbit secondary antibody. (A) Total membrane and internalized intracellular α3 integrin in permeabilized cells shown as control (red). (B) Uninternalized α3 integrin (red) and recycled α3 integrin (green) at 0min, 10min and 40 minutes of recycling and 40min recycling with primaquine (PQ, recycling inhibitor) are shown in merged images with DAPI (blue) stained nucleus (left panel). Middle panel shows only the recycled α3 integrin label in grey. Right panel is magnified images of boxed sections marked for recycled integrin localized at lamellipodia at cell front (white arrows) or at cell- cell locations (closed white triangles) and uninternalized integrin at cell front (open white triangles). Images acquired by deconvolution microscopy and single Z-plane is shown. Bars, 20µm. Images are representative fields of view obtained in 3 independent experiments.</p

AR variant mRNA was sensitive to androgen concentration in vitro.

<p>(<b>A</b>) AR^FL mRNA was suppressed by DHT, MDV-3100 and MDV-3100+DHT but not to the level seen by DHT alone. (<b>B</b>) AR^v567es mRNA was suppressed in the presence of DHT, further increased by addition of MDV-3100 and suppressed to the level of CSS when DHT was added along with MDV-3100. (<b>C</b>) AR-V7 mRNA responded in a similar manner as AR^FL.</p

Methylation profiling identified novel differentially methylated markers including <i>OPCML</i> and <i>FLRT2</i> in prostate cancer

<p>To develop new methods to distinguish indolent from aggressive prostate cancers (PCa), we utilized comprehensive high-throughput array-based relative methylation (CHARM) assay to identify differentially methylated regions (DMRs) throughout the genome, including both CpG island (CGI) and non-CGI regions in PCa patients based on Gleason grade. Initially, 26 samples, including 8 each of low [Gleason score (GS) 6] and high (GS ≥7) grade PCa samples and 10 matched normal prostate tissues, were analyzed as a discovery cohort. We identified 3,567 DMRs between normal and cancer tissues, and 913 DMRs distinguishing low from high-grade cancers. Most of these DMRs were located at CGI shores. The top 5 candidate DMRs from the low vs. high Gleason comparison, including <i>OPCML, ELAVL2, EXT1, IRX5</i>, and <i>FLRT2</i>, were validated by pyrosequencing using the discovery cohort. <i>OPCML</i> and <i>FLRT2</i> were further validated in an independent cohort consisting of 20 low-Gleason and 33 high-Gleason tissues. We then compared patients with biochemical recurrence (n=70) vs. those without (n=86) in a third cohort, and they showed no difference in methylation at these DMR loci. When GS 3+4 cases and GS 4+3 cases were compared, <i>OPCML</i>-DMR methylation showed a trend of lower methylation in the recurrence group (n=30) than in the no-recurrence (n=52) group. We conclude that whole-genome methylation profiling with CHARM revealed distinct patterns of differential DNA methylation between normal prostate and PCa tissues, as well as between different risk groups of PCa as defined by Gleason scores. A panel of selected DMRs may serve as novel surrogate biomarkers for Gleason score in PCa.</p

Quantitative RT-PCR of genes associated with AR C-terminal truncated variants.

<p>(<b>A</b>) Profile of seven AR variant associated genes expression in human metastatic tissues. (<b>B</b>) The same genes were measured in LuCaP 86.2 and LuCaP 35 xenografts. The housekeeping gene RPL13A was used as an endogenous control.</p