Transcriptome profiles of control and PIM1 over-expressing LNCaP cells in complete media
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ABSTRACT:
PROVIDER: PRJNA752387 | ENA |
REPOSITORIES: ENA
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Project description:We used control and PIM1 over-expressing LNCaP cells to analyze the effect of PIM1 on gene expression. We find that PIM1 over-expression results in up- and down-regulation of different classes of genes, including increasing gene expression involved in extracellular matrix organization, cell adhesion, and cytokine signaling.
2021-11-03 | GSE181225 | GEO
Project description:We used ChIP-seq to identify chromatin binding sites for AR, 14-3-3 ζ, and pS213 AR in the absence and presence of PIM1 over-expression. We find that, as expected, pS213 AR occupancy almost completely overlaps with total AR occupancy, and increases in the presence of PIM1 over-expression. Additionally, the majority of pS213 AR sites are co-occupied by 14-3-3 ζ. 14-3-3 ζ is a known AR co-activator, but this study definitively shows its co-occupancy on chromatin with AR and pS213 AR.
2021-11-03 | GSE181224 | GEO
Project description:14-3-3 ζ is an androgen receptor (AR) co-activator. To further understand how 14-3-3 ζ may be modulating AR activity, we performed rapid immunoprecipitation mass spectrometry of endogenous proteins for analysis of chromatin complexes (RIME) on AR and 14-3-3 ζ in LNCaP prostate cancer cells in the presence of PIM1. This enabled us to observe what other proteins associate with both 14-3-3 ζ and AR on chromatin. Notably, several of the proteins we identified as associated with both AR and 14-3-3 ζ are known AR co-regulators. We hypothesized that to co-regulate AR, 14-3-3 ζ may be recruiting or altering interactions between AR and AR co-regulators.
2021-11-25 | PXD023634 | Pride
Project description:Genome-wide maps of the androgen receptor, pS213 androgen receptor, and 14-3-3 ζ chromatin occupancy in control and PIM1 over-expressing LNCaP cells
| PRJNA751082 | ENA
Project description:To identify the downstream molecules that mediate PIM1 induced aggressive prostate cancer cells, p53 and Rb-deficient mouse prostate epithelial cells were transduced with PIM1 lentivirus and performed a gene expression profile microarray.
2018-08-21 | GSE118786 | GEO
Project description:Background: PIM1 is a constitutively active serine-threonine kinase regulating cell survival and proliferation. Increased PIM1 expression has been correlated with cancer metastasis by facilitating migration and anti-adhesion. Endothelial cells play a pivotal role in these processes by contributing a barrier to the blood stream. Here, we investigated whether PIM1 regulates mouse aortic endothelial cell (MAEC) monolayer integrity. Methods: Pim1-/-MAEC were isolated from Pim1 knockout mice and used in trypsinization-, wound closure assays, electrical cell-substrate sensing, immunostaining, cDNA transfection and as RNA source for microarray analysis. Results: Pim1-/-MAEC displayed decreased migration, slowed cell detachment and increased electrical resistance across the endothelial monolayer. Reintroduction of Pim1- cDNA into Pim1-/-MAEC significantly restored wildtype adhesive characteristics. Pim1-/--MAEC displayed enhanced focal adhesion and adherens junction structures containing vinculin and M-NM-2-catenin, respectively. Junctional molecules such as Cadherin 13 and matrix components such as Collagen 6a3 were highly upregulated in Pim1-/- cells. Intriguingly, extracellular matrix deposited by Pim1-/- cells alone was sufficient to induce the hyperadhesive phenotype in wildtype endothelial cells. Conclusion: Loss of Pim1 induces a strong adhesive phenotype by enhancing endothelial cell-cell and cell-matrix adhesion by the deposition of a specific extracellular matrix. Targeting PIM1 function therefore might be important to promote endothelial barrier integrity. Pim-1-/- mouse aortic endothelial cells were compared to wildtype cells
2012-10-29 | E-GEOD-32059 | biostudies-arrayexpress
Project description:PIM1 is an oncogenic serine/threonine kinase that promotes and maintains prostate
tumorigenesis. To more fully understand the mechanism by which PIM1 promotes oncogenesis,
we performed a chemical genetic screen to identify direct PIM1 substrates in prostate cancer
cells. To identify PIM1 substrates and their phosphorylation sites in LNCaP cells, we coupled a
chemical genetic screen with a peptide capture, mass spectrometry (MS)-based approach. We
mutated the PIM1 gatekeeper residue in the ATP binding site to accept a bulky ATP analog. By
using an ATP analog labeled with a thiol group on the gamma-phosphate, we were able specifically
label PIM1 substrates even in the presence of other cellular kinases.
2020-02-27 | MSV000085028 | MassIVE
Project description:It has been estimated that about 11% of cellular genes present a functional E box to which MYC can associate on the genome. MYC silencing demonstrated that MYC recruits PIM1 at specific MYC binding sites and confocal microscopy following growth factor treatment, showed an elevated degree of nuclear co-localization of PIM1 with nascent transcripts and with MYC suggesting that PIM1 is recruited by MYC to a large number of sites. To understand the actual extension of PIM1 and MYC co-operation in gene transcription we performed expression profile analysis of 293 cells silenced either for MYC or PIM1 at 120 minutes after serum treatment. MYC silencing affected the expression of 1026 genes of which 818 were up-regulated and 208 were down-regulated. Comparison of genes regulated by MYC with those regulated by PIM1, by RNAi silencing, showed that PIM1 contributes to the regulation of 207 genes out of the 1026 MYC-regulated genes. Thus, a subset of 20% of MYC-regulated genes, are also regulated by PIM1. The co-regulated includes genes involved in cell metabolism, protein synthesis, cycle progression, and oncogenesis. Interestingly, a large number of genes are transcriptional factors, which suggests that PIM1 participates in MYC-dependent regulatory networks. Keywords: expression profiles
2007-07-31 | GSE7960 | GEO
Project description:It has been estimated that about 11% of cellular genes present a functional E box to which MYC can associate on the genome. MYC silencing demonstrated that MYC recruits PIM1 at specific MYC binding sites and confocal microscopy following growth factor treatment, showed an elevated degree of nuclear co-localization of PIM1 with nascent transcripts and with MYC suggesting that PIM1 is recruited by MYC to a large number of sites. To understand the actual extension of PIM1 and MYC co-operation in gene transcription we performed expression profile analysis of 293 cells silenced either for MYC or PIM1 at 120 minutes after serum treatment. MYC silencing affected the expression of 1026 genes of which 818 were up-regulated and 208 were down-regulated. Comparison of genes regulated by MYC with those regulated by PIM1, by RNAi silencing, showed that PIM1 contributes to the regulation of 207 genes out of the 1026 MYC-regulated genes. Thus, a subset of 20% of MYC-regulated genes, are also regulated by PIM1. The co-regulated includes genes involved in cell metabolism, protein synthesis, cycle progression, and oncogenesis. Interestingly, a large number of genes are transcriptional factors, which suggests that PIM1 participates in MYC-dependent regulatory networks. Experiment Overall Design: The gene expression analysis was performed by hybridizing RNA samples to the Whole Human Genome Oligo Microarray from Agilent Technologies. Samples were obtained from 293 cells, treated with serum for 120 minutes, expressing either two independent MYC shRNA (shMYC#1 and shMYC#2) or their relative scrambled shRNA (shsM#1 and shsM#2) for MYC expression analysis; two independent PIM1 shRNA (shPIM1#1 and shPIM1#2) or their relative scrambled shRNA (shsP#1 and shsP#2) for PIM1 expression analysis.
2008-06-15 | E-GEOD-7960 | biostudies-arrayexpress
Project description:Background: PIM1 is a constitutively active serine-threonine kinase regulating cell survival and proliferation. Increased PIM1 expression has been correlated with cancer metastasis by facilitating migration and anti-adhesion. Endothelial cells play a pivotal role in these processes by contributing a barrier to the blood stream. Here, we investigated whether PIM1 regulates mouse aortic endothelial cell (MAEC) monolayer integrity. Methods: Pim1-/-MAEC were isolated from Pim1 knockout mice and used in trypsinization-, wound closure assays, electrical cell-substrate sensing, immunostaining, cDNA transfection and as RNA source for microarray analysis. Results: Pim1-/-MAEC displayed decreased migration, slowed cell detachment and increased electrical resistance across the endothelial monolayer. Reintroduction of Pim1- cDNA into Pim1-/-MAEC significantly restored wildtype adhesive characteristics. Pim1-/--MAEC displayed enhanced focal adhesion and adherens junction structures containing vinculin and β-catenin, respectively. Junctional molecules such as Cadherin 13 and matrix components such as Collagen 6a3 were highly upregulated in Pim1-/- cells. Intriguingly, extracellular matrix deposited by Pim1-/- cells alone was sufficient to induce the hyperadhesive phenotype in wildtype endothelial cells. Conclusion: Loss of Pim1 induces a strong adhesive phenotype by enhancing endothelial cell-cell and cell-matrix adhesion by the deposition of a specific extracellular matrix. Targeting PIM1 function therefore might be important to promote endothelial barrier integrity.
2012-10-29 | GSE32059 | GEO