Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA327397 | ENA |
REPOSITORIES: ENA
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Project description:Gene expression analysis of BJhTERT RhoA-KO and PC3 mRFP was performed before and after six days confrontation in co-cultivation. Analyses of original and control fibroblasts was also performed. To identify molecules that may mediate the tumor promoting effect of RhoA knock out fibroblasts, we performed gene expression analysis of BJhTERT RhoA-KO and PC3 mRFP cells before the confrontation and then after six days after it, using Affymetrix Whole Transcript Assay platform.
2016-07-01 | GSE83913 | GEO
Project description:Gene expression analysis of BJhTERT RhoA-KO and PC3 mRFP was performed before and after six days confrontation in co-cultivation. Analyses of original and control fibroblasts was also performed. To identify molecules that may mediate the tumor promoting effect of RhoA knock out fibroblasts, we performed gene expression analysis of BJhTERT RhoA-KO and PC3 mRFP cells before the confrontation and then after six days after it, using Affymetrix Whole Transcript Assay platform. Four days old fibroblast monolayer was confronted with PC3 mRFP tumor cells, plated in ratio 1:30 to number of plated fibroblasts. After six days of confrontation cells were sorted by FACS (Fluorescence-activated cell sorting). Total RNA was isolated from each confronted and non-confronted cells with kit. Then 150 ng of total RNA were used for transcriptomic analysis.for RNA extraction and hybridization on Affymetrix microarrays
2016-07-01 | E-GEOD-83913 | biostudies-arrayexpress
Project description:Microarray analysis of PC3 prostate tumor-initiating cells (PC3 holoclones)
| PRJNA227068 | ENA
Project description:Tumor microenvironment or stroma has the potency to regulate the behavior of malignant cells. Fibroblast-like cells are abundant in tumor stroma and they are also responsible for the synthesis of many extracellular matrix components. Fibroblast–cancer cell interplay can modify the functions of both cell types. We applied mass spectrometry and proteomics to unveil the matrisome in 3D spheroids formed by DU145 prostate cancer cells, PC3 prostate cancer cells or prostate derived fibroblasts. Similarly DU145/fibroblast and PC3/fibroblast co-culture spheroids were also analyzed. Western Blotting and immunofluorescence were used to confirm the presence of specific proteins in spheroids. Cancer dissemination was studied by utilizing "out of spheroids" migration and invasion assays. In the spheroid model cancer cell–fibroblast interplay caused remarkable changes in extracellular matrix and accelerated the invasion of DU145 cells. Fibroblasts produced structural matrix proteins, growth factors and matrix metalloproteinases. In cancer cell/fibroblast co-cultures basement membrane components, including laminins (3, 5, 2, 3), heparan sulphate proteoglycan (HSPG2 gene product), and collagen XVIII accumulated in a prominent manner when compared to spheroids that contained fibroblasts or cancer cells only. Furthermore, collagen XVIII was intensively processed to different endostatin isoforms by cancer cell derived cathepsin L. To sum up, fibroblasts can promote carcinoma cell dissemination by several different mechanisms. Extracellular matrix and basement membrane proteins provide attachment sites for cell locomotion promoting adhesion receptors. Growth factors and metalloproteinases are known to accelerate cell invasion. Additionally, cancer cell–fibroblast interplay generates biologically active fragments of basement membrane proteins, such as endostatin.
2020-05-04 | PXD016882 | Pride
Project description:Differential protein expression between RhoA ko and wt bone marrow-derived dendritic cells
2015-10-01 | PXD001636 | Pride
Project description:Expression data from xenograft in BALB/c 6-wk-old nude mice with PC3 prostate cancer cells stably expressing PML or a vector control after treatment of the mice with palbociclib (100mg/kg/day diluted in sodium lactate 50mM pH4 given by gavage) during 5 consecutive days PML plays a role in the senescence tumor suppressor response of normal cells to oncogenic stress. PML also mediates therapy-induced senescence in acute promyelocytic leukemia cells after treatment with retinoic acid. However, many tumor cell lines fail to engage a complete senescence response to PML activation. Interestingly, in vivo and in vitro combination of PML overexpression with CDK inhibition induce senescence in PC3 prostate cancer cells. We used microarray to characterize the gene expression profile of PC3 stably expressing PML or a control vector after subcutaneous injection in BALB/c 6-wk-old nude mice and treatment of the mice with palbociclib (100mg/kg/day) during 5 consecutive days.. PC3 cells were infected with a retroviral vector that express PML or an empty vector before subcutaneous injection of 10^6 cells in both flanks of BALB/c 6-wk-old nude mice. Then, mice were treated for 5 consecutive days with palbociclib (100mg/kg/day diluted in sodium lactate 50mM pH4 given by gavage)
2016-07-03 | E-GEOD-70923 | biostudies-arrayexpress
Project description:We found that PC3 cells secrete proteases that cleavae and activate PAR1 and PAR2. In order to understand gene regulation by this autocrine signaling loop, PAR1 and PAR2 knockout cell gene expression was compared to WT PC3 cell gene expression. Proteinase activated receptors (PARs) are G protein-coupled receptors (GPCRs) activated by limited N-terminal proteolysis. A variety of proteolytic enzymes derived from the coagulation cascade and inflammatory milieu activate PARs, however specific activators in different physiological and pathophysiological contexts remain poorly defined. PARs are highly expressed in many cancer cells and regulate various aspects of tumor growth and metastasis. Endogenous proteinases that regulate PARs in the setting of various tumors however remains unresolved. Prostate cancer (PCa) remains a major cause of mortality in men despite advances in early detection and clinical intervention. PAR expression has been reported in PCa, however, their role here remains poorly defined. In androgen independent PC3 cells, we find functional expression of PAR1 and PAR2 but not PAR4. Using genetically encoded PAR cleavage biosensors, we find that PCa cells secrete proteolytic enzymes that cleave PARs and trigger autocrine signaling. Deletion of PAR1 and PAR2 using CRISPR/Cas9 combined with microarray analysis revealed genes that are differentially regulated by this autocrine signalling mechanism. Interestingly, several genes that are known PCa prognostic factors or biomarker were differentially expressed in PAR1-KO and PAR2-KO PC3 cells. We also examined PAR1 and PAR2 regulation of PCa cell proliferation and migration using PAR1 and PAR2-KO PC3 cells, as well as PAR1 and PAR2 specific agonists and antagonists. We find that PAR1 and PAR2 have opposite effects on PC3 cell proliferation and migration. In summary, we have identified an autocrine signaling mechanism through PARs as a regulator of PCa cell function.
2022-08-24 | GSE211813 | GEO
Project description:Expression data from control and WHSC1 siRNA treated PC3 cells
| PRJNA335397 | ENA
Project description:Due to the urgent need of new targeting strategies in PCa, AR interacting proteins should be considered. In this study we aimed to test the effect of a long-term knockdown of NCOA1, an AR coactivator, in PCa progression and metastatogenesis and whether NCOA1 could be used as a possible therapeutic target. To test the consequences of NCOA1 knockdown on proliferation, we performed by 3H thymidine incorporation assays revealing a strong reduction in castration resistant MDA PCa 2b and androgen-dependent LNCaP cells, without affecting AR negative PC3 cells. Furthermore, Boyden chamber assays revealed a strong decrease in migration and invasion upon NCOA1 knockdown. Using a cDNA microarray, we identified protein kinase D1 (PRKD1) as one prominent upregulated gene in MDA PCa 2b, which was not seen in PC3 cells. Knockdown of PRKD1 clearly reverted the reduced migratory potential. Moreover, we found phospholipase A2, group7 (PLA2G7) and eukaryotic translation initiation factor 5A2 (EIF5A2), which might be involved in migration of PC3 cells. Further, we can clearly demonstrate that PRKD1 is negatively regulated by the AR/NCOA1 complex. In addition, immunhistochemical staining revealed a strong increase in NCOA1 expression in matched and unmatched patientsâ samples, respectively between normal prostate and primary tumor. Regarding the PRKD1 staining, no final conclusion can be drawn in terms of a tumor suppressor function. Thus, our findings directly associate NCOA1/AR complex with PRKD1 regulation and further suggest NCOA1 as a potential therapeutic target also due to the effect on PC3 cell migration. Cell lines with a stable knockdown of NCOA1 were generated by lentiviral-based transduction of shRNA vectors. For each of the two cell lines MDA and PC3, gene expression profiles were generated for KO and CTRL samples with 3 biological replicates for each. Differential expression analysis was performed by comparing the gene expression estimates between KO and CTRL samples for each cell line.
2016-06-22 | E-GEOD-75531 | biostudies-arrayexpress
Project description:Prostate cancer cells (PC3) were treated with purified human recombinant CRISP3 protein or vehicle control for 4 hours before whole cell protein extraction
2020-07-15 | PXD009609 | JPOST Repository