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The proteome of localized prostate cancer, part 7

ABSTRACT: Proteome characterization of gland confined prostate tumors and non-malignant prostate tissue. Whole cell protein extracts were purified from FFPE radical prostatectomy specimens for a total of 28 tumor samples and 8 adjacent non-malignant prostate tissues. Associated ProteomeXchange identifiers: PXD003430, PXD003452, PXD003515, PXD004132, PXD003615, PXD003636.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Prostate Adenocarcinoma

SUBMITTER: Diego Iglesias-Gato

LAB HEAD: Amilcar Flores Morales

PROVIDER: PXD004159 | Pride | 2016-06-01

REPOSITORIES: pride

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			Action	DRS
	20110819_EXQ4_TaGe_SA_PC12_1_110820100421.raw	Raw
	20110819_EXQ4_TaGe_SA_PC12_2.raw	Raw
	20110819_EXQ4_TaGe_SA_PC12_3.raw	Raw
	20110819_EXQ4_TaGe_SA_PC12_4.raw	Raw
	20110819_EXQ4_TaGe_SA_PC12_5.raw	Raw

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Publications

The Proteome of Primary Prostate Cancer.

Iglesias-Gato Diego D Wikström Pernilla P Tyanova Stefka S Lavallee Charlotte C Thysell Elin E Carlsson Jessica J Hägglöf Christina C Cox Jürgen J Andrén Ove O Stattin Pär P Egevad Lars L Widmark Anders A Bjartell Anders A Collins Colin C CC Bergh Anders A Geiger Tamar T Mann Matthias M Flores-Morales Amilcar A

European urology 20151202 5

<h4>Background</h4>Clinical management of the prostate needs improved prognostic tests and treatment strategies. Because proteins are the ultimate effectors of most cellular reactions, are targets for drug actions and constitute potential biomarkers; a quantitative systemic overview of the proteome changes occurring during prostate cancer (PCa) initiation and progression can result in clinically relevant discoveries.<h4>Objectives</h4>To study cellular processes altered in PCa using system-wide ...[more]

PMID: 26651926

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The proteome of localized prostate cancer, part 5

2016-06-01 | PXD003615 | Pride

The proteome of localized prostate cancer, part 2

2016-06-01 | PXD003452 | Pride

The proteome of localized prostate cancer, part 1

2016-06-01 | PXD003430 | Pride

The proteome of localized prostate cancer, part 4

2016-06-01 | PXD004132 | Pride

The proteome of localized prostate cancer, part 6

2016-06-01 | PXD003636 | Pride

The proteome of localized prostate cancer, part 3

2016-06-01 | PXD003515 | Pride

Prostate cancer progression: From non-malignant to bone metastasisProstate cancer progression: From non-malignant to bone metastasis

Project description:Proteome characterization of gland confined prostate tumors and non-malignant prostate tissue. Whole cell protein extracts were purified from FFPE radical prostatectomy specimens for a total of 28 tumor samples and 8 adjacent non-malignant prostate tissues. Associated ProteomeXchange identifiers: PXD003430, PXD003452, PXD003515, PXD004132, PXD003615, PXD003636. Quantitative proteomic analysis of adjacent non-malignant prostate tissue (n=8) and gland confined prostate tumors (n=28) obtained from radical prostatectomy procedures; and bone metastatic prostate tumors (n=22) obtained from patients operated to relief spinal cord compression. At the time of surgery, most metastatic patients had relapsed after androgen-deprivation therapy, while 5 were previously untreated.

2018-08-21 | PXD009868 | Pride

Proteomics of prostate cancer patient derived xenografts

Project description:A set of 17 prostate cancer patient-derived xenografts (PDX, Lin et al 2014, Cancer research) was analyzed by mass spectrometry-based proteomics to characterize the effects of castration in vivo, and the proteome differences between NEPC and prostate adenocarcinomas.

2019-09-11 | PXD009636 | Pride

eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression

Project description:Translational regulation plays a critical role in cell growth and proliferation, and its dysregulation results in cancer. Aberrant expression of the mRNA 5’cap-binding protein, eIF4E, has been implicated in cancer development and progression. eIF4E activity is promoted by phosphorylation. Here we show that “knock-in” mice in which eIF4E cannot be phosphorylated are resistant to tumorigenesis in a prostate cancer model. We identify multiple candidate genes involved in the resistance to oncogenic transformation. Importantly, phosphorylation of eIF4E is increased in hormone-refractory prostate cancer, the deadliest stage of the disease. Our results highlight eIF4E phosphorylation as a critical event in tumorigenesis. Comaparison of total RNA and polysomal RNA from mouse embryo fibroblasts derived from WT and eIF4E-KI (non phosphorylatable eIF4E) mice

2010-08-17 | E-GEOD-17451 | biostudies-arrayexpress

Identification of MEF2B, EBF1, and IL6R as chromosome bound targets of EBNA1 essential for EBV infected B-lymphocyte survival

Project description:EBNA1 is the EBV-encoded nuclear antigen required for viral episome maintenance during latency. EBNA1 is a sequence specific DNA binding protein with high affinity binding sites for the viral genome, especially OriP. EBNA1 can also bind sequence specifically to a large number of sites in the host cellular genome, but the function of these binding sites has remained elusive. EBNA1 is also known to provide a host cell survival function, but the molecular mechanisms accounting for this function are not completely understood. Here, we show by integrating ChIP-Seq and RNA-Seq with experimental validation that MEF2B, IL6R, and EBF1 are high confidence target genes of EBNA1 that are essential for viability of B-lymphocytes latently infected with EBV. We show that EBNA1 binds to ~1000 sites with many, but not all, universally bound in different cell types, including Burkitt lymphoma (BL) and nasopharyngeal carcinoma (NPC). We find that a large subset of EBNA1 binding sites are located proximal to transcription start sites and correlate genome-wide with transcription activity. EBNA1 bound to genes of high significance for B-cell growth and function, including MEF2B, IL6R, EBF1, RNF145, POU2F1, KDM4C, FGR, EGFR, LAIR, CDC7, CD44, and IL17A. EBNA1 depletion from latently infected LCLs results in the loss of cell proliferation, and the loss of gene expression for some EBNA1-bound genes, including MEF2B, EBF1, and IL6R. Depletion of MEF2B, EBF1, or IL6R partially phenocopies EBNA1-depletion by decreasing EBV-positive cell growth and viability. These findings indicate that EBNA1 binds to a large cohort of cellular genes important for cell viability, and implicates EBNA1 as a master coordinator of host cell gene expression important for enhanced survival of latently infected cells. Examination of EBNA1 binding in Raji, MutuI, LCL and C666-1 cells and EBNA1 knockdown effect on mRNA gene expression in LCL

2015-12-16 | E-GEOD-73887 | biostudies-arrayexpress

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