human prostate cancer tissue arrays  (Pantomics Inc)

Journal: PLoS ONE

Article Title: Beta-Catenin Phosphorylated at Threonine 120 Antagonizes Generation of Active Beta-Catenin by Spatial Localization in trans-Golgi Network

doi: 10.1371/journal.pone.0033830

Figure Lengend Snippet: Formalin fixed and paraffinized normal human prostate tissues were stained with either β-catenin H102 (A) or pT120 (B) antibodies with TGN marker p230 antibody. Nucleus was stained in blue. Inserts are higher magnification for details. Representative images from three assays were shown. (C) Immunohistochemical staining with the pT120 antibody on normal prostate tissue (left), in the presence of 20 nM antigenic phospho-peptide (middle) or 20 nM nonphospho-peptide (right).

Article Snippet: Human prostate tissue arrays were purchased from US Biomax.

Techniques: Staining, Marker, Immunohistochemical staining

Journal: Cell Death & Disease

Article Title: ROR2 suppresses metastasis of prostate cancer via regulation of miR-199a-5p–PIAS3–AKT2 signaling axis

doi: 10.1038/s41419-020-2587-9

Figure Lengend Snippet: ( a ) PC-3 human PCa cells (1 × 10 6 ) were directly injected into prostate organ of nude mice to form prostate tumors. There were five mice in control group and experimental group, respectively. Protein expression level of ROR2, PIAS3, E-cadherin, and vimentin was examined by IHC. Images were captured at ×40 magnification. Scale bar represented 50 μm. ( b ) Proteins level of ROR2, PIAS3, phospho-AKT S473, phospho-AKT T308, and total AKT in prostate xenografts were also determined by the western blotting assay. Expression of β-actin was used as loading control. ( c ) Hematoxylin and eosin staining of lung tissues in mice was examined for dissemination of PCa cells. Images were capture at ×20 (upper panel) and ×40 (bottom panel) magnification. Scale bar represented 50 μm. ( d ) A list of lung metastasis of PC-3 cells with or without ROR2 overexpression in the above orthotopic nude mice.

Article Snippet: Paraffin embedded tissue sections were derived from commercial human PCa tissue array (SUP-CA array from SuperBioChips, Seoul, Korea and PR956a array from US Biomax, Rockville, MD, USA) or tumor bearing mice.

Techniques: Injection, Expressing, Western Blot, Staining, Over Expression

Journal: Cancers

Article Title: Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

doi: 10.3390/cancers12051083

Figure Lengend Snippet: Promyelocytic leukemia zinc finger (PLZF) inhibits the activation of STAT3, which has an inverse correlation with PLZF. ( A ) IHC of PLZF, pY-STAT3 in tissue arrays of surrounding normal prostate tissues, and human prostate cancer specimens correlates with Gleason scores (GS). Quantification of PLZF-positive expression according to the GS in normal tissues adjacent to the benign tumors ( n = 9) and malignant tumors ( n = 40) (right). ( B ) Associations between expression of PLZF and pY-STAT3. Scatter plots showing the linear correlation determined by Pearson correlation coefficient calculation of those genes that were statistically significant. Pearson correlation coefficient r and p -values are given in each scatter plot. ( C ) PSA levels were measured according to the PLZF and pY-STAT3 protein levels, n = 40. ( D ) Kaplan–Meier recurrence-free survival analysis of prostate cancer patients according to PLZF (* p = 0.0344) and pY-STAT3 (* p < 0.0001) expression. ( E ) Quantification of PLZF mRNA expression according to the GS and metastasis in prostate cancer patients’ samples, *** p < 0.0001. ( F ) PLZF, pY-STAT3, STAT3, and GAPDH protein expression by Western blotting in the prostate cancer cell lines DU145 and LNCaP. GAPDH was used as a loading control. ( G ) Western blotting was performed in PLZF, CA-STAT3 plasmid, and siRNA-transfected cells. The uncropped blots and molecular weight markers of are shown in

Article Snippet: Human prostate cancer tissue arrays were purchase from SuperBioChips Lab (Seoul, Korea).

Techniques: Activation Assay, Expressing, Western Blot, Control, Plasmid Preparation, Transfection, Molecular Weight

Journal: Cancers

Article Title: Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

doi: 10.3390/cancers12051083

Figure Lengend Snippet: Tyrosine phosphatase SHP-1 is a direct target of PLZF and inhibits the tyrosine phosphorylation of JAKs–STAT3 signaling. ( A ) Western blotting was performed in PLZF-transfected DU145 cells. ( B ) Protein expression levels of the tyrosine phosphatase-related markers STAT3, JAK2, and TYK2 were detected by Western blotting. ( C ) mRNA expression levels of tyrosine phosphatases were examined by RT-PCR and qRT-PCR in DU145 and LNCaP cells. ( D ) Western blotting of SHP-1, STAT3, JAK2, and TYK2 in cells that were co-transfected with PLZF and si-SHP-1. ( E ) SHP-1 reporter assay in DU145 and LNCaP cells transfected with PLZF plasmid and siRNA. ( F ) IHC of SHP-1 in tissue arrays of surrounding normal prostate tissues and human prostate cancer specimens correlates with GS. Quantification of SHP-1-positive expression according to the GS scores in benign ( n = 9) and malignant tumors ( n = 40) (right). ( G ) Associations between SHP-1 and PLZF. Scatter plots showing the linear correlation determined by Pearson correlation coefficient calculation of those genes that were statistically significant. Pearson correlation coefficient r and p-values are given in each scatter plot. ( H ) PSA levels were measured according to the SHP-1 protein levels, n = 40. ( I ) Kaplan–Meier recurrence-free survival analysis of prostate cancer patients according to SHP-1 (* p < 0.0001) expression. In C, E, and F data are presented as the mean ± SD; * p < 0.05, *** p < 0.001. The uncropped blots and molecular weight markers of are shown in

Article Snippet: Human prostate cancer tissue arrays were purchase from SuperBioChips Lab (Seoul, Korea).

Techniques: Phospho-proteomics, Western Blot, Transfection, Expressing, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR, Reporter Assay, Plasmid Preparation, Molecular Weight

Journal: Cancers

Article Title: Crosstalk between Prostate Cancer Cells and Tumor-Associated Fibroblasts Enhances the Malignancy by Inhibiting the Tumor Suppressor PLZF

doi: 10.3390/cancers12051083

Figure Lengend Snippet: Loss of CCL3 inhibits the fibroblast-induced prostate cancer cells migration and invasion. ( A ) Each CM was applied to the cytokine arrays (top). The cytokines in boxes are more enriched in co-cultured CM than in fibroblast CM. Mean intensities of cytokines are plotted (bottom). ( B ) PNT2, LNCaP, and DU145 cells were co-cultured with fibroblast in a cell culture chamber for 24 h. Cells in a lower chamber were lysed for qRT-PCR. ( C ) LNCaP cells were treated with the indicated conditioned media with the addition of an anti-CCL3 antibody or anti-uPAR antibody and then subjected to Western blotting. ( D ) Concentrations of CCL3 in the indicated conditioned media were analyzed using an ELISA kit. Summarized results from three independent experiments were quantified as the mean ± SD. ( E ) Cells, which had been transfected with the luciferase plasmid, were pre-treated with recombinant protein CCL3 for 4 h, incubated under FCM or Co-CM for 24 h. ( F ) LNCaP cells, which had been pre-treated with anti-CCL3 antibody for 4 h, were incubated in the indicated CMs for 24 h. The relative cell numbers are shown (right). In B, D, E, and F, representative images from three independent experiments were quantified as the mean ± SD; * p < 0.05, ** p < 0.01, *** p < 0.001. The uncropped blots and molecular weight markers of are shown in

Article Snippet: Human prostate cancer tissue arrays were purchase from SuperBioChips Lab (Seoul, Korea).

Techniques: Migration, Cell Culture, Quantitative RT-PCR, Western Blot, Enzyme-linked Immunosorbent Assay, Transfection, Luciferase, Plasmid Preparation, Recombinant, Incubation, Molecular Weight

Journal: International Journal of Cancer

Article Title: Olfactomedin 4 downregulation is associated with tumor initiation, growth and progression in human prostate cancer

doi: 10.1002/ijc.32535

Figure Lengend Snippet: Reduced OLFM4 expression is associated with higher Gleason scores and lower recurrence‐free survival in human primary prostate adenocarcinoma. ( a ) Representative images of HE staining and immunohistochemistry (IHC) analysis of OLFM4 protein expression in adjacent normal and tumor regions of whole‐mount section human prostate cancer tissue specimens (obtained from the Laboratory of Pathology, National Cancer Institute). All micrographs shown are for tissues obtained from the same case. LT, lower grade tumor (Gleason grade 3, GL. 3); HT, higher grade tumor Gleason grade 4, GL. 4). Scale bars: 50 μm. ( b ) Quantitation of OLFM4 protein expression from immunohistochemical analyses using human prostate cancer tissue slides obtained from CHTN and US Biomax. Data represent the mean ± standard deviation (SD) of 3,3′‐diaminobenzidine (DAB) intensity normalized to the number of nuclei. Adjacent Nor., normal tissue adjacent to primary tumor; Gleason score ≤4 + 3; Gleason score ≥4 + 4. We excluded CHTN and US Biomax cases with quality issues for which we could not obtain immunohistochemistry data. *** p ≤ 0.001 (ANOVA). ( c ) OLFM4 mRNA expression in prostate cancer specimens in data downloaded from the GSE21032 dataset. Data represent the mean ± SD. Normal, normal tissue adjacent to primary tumor; P‐tumor, primary tumor; M‐PCs; prostate tumor with distant metastasis. ** p ≤ 0.01; *** p ≤ 0.001 (ANOVA). ( d ) Kaplan–Meier plot of recurrence‐free survival for OLFM4 mRNA higher‐expressing (red line) and lower‐expressing (blue line) prostate adenocarcinoma patient cohorts in the GSE21032 dataset at 25% thresholds ( p = 0.0000154; log‐rank test).

Article Snippet: Human prostate cancer tissue array slides (for 70 prostate cancer cases and 10 normal tissues) were purchased from US Biomax (PR803, Rockville, MD).

Techniques: Expressing, Staining, Immunohistochemistry, Quantitation Assay, Immunohistochemical staining, Standard Deviation