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Multiplexed proteome dynamics profiling of HSP90 inhibitor 17-AAG in anti-CD3 and anti-CD28 stimulated T-cells

ABSTRACT: Investigation of proteostatic effects of HSP90 inhibition by 17-AAG and differentiation of maturation state dependent HSP90 requirements of proteins in activated T-cells.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell

SUBMITTER: Maria Faelth Savitski

LAB HEAD: Marcus Bantscheff

PROVIDER: PXD008634 | Pride | 2018-05-02

REPOSITORIES: Pride

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			Action	DRS
	02149_F1_R1_P0179684B02_HYPS2ME3.raw.gz	Raw
	02149_F1_R1_P0179684B03_HYPS2ME3.raw.gz	Raw
	02149_F1_R1_P0179684B04_HYPS2ME3.raw.gz	Raw
	02149_F1_R1_P0179684B05_HYPS2ME3.raw.gz	Raw
	02149_F1_R1_P0179684B06_HYPS2ME3.raw.gz	Raw

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Publications

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis.

Savitski Mikhail M MM Zinn Nico N Faelth-Savitski Maria M Poeckel Daniel D Gade Stephan S Becher Isabelle I Muelbaier Marcel M Wagner Anne J AJ Strohmer Katrin K Werner Thilo T Melchert Stephanie S Petretich Massimo M Rutkowska Anna A Vappiani Johanna J Franken Holger H Steidel Michael M Sweetman Gavain M GM Gilan Omer O Lam Enid Y N EYN Dawson Mark A MA Prinjha Rab K RK Grandi Paola P Bergamini Giovanna G Bantscheff Marcus M

Cell 20180315 1

Protein degradation plays important roles in biological processes and is tightly regulated. Further, targeted proteolysis is an emerging research tool and therapeutic strategy. However, proteome-wide technologies to investigate the causes and consequences of protein degradation in biological systems are lacking. We developed "multiplexed proteome dynamics profiling" (mPDP), a mass-spectrometry-based approach combining dynamic-SILAC labeling with isobaric mass tagging for multiplexed analysis of ...[more]

PMID: 29551266

Similar Datasets

Expression profiling of HSP90 inhibitor 17-AAG in anti-CD3 and anti-CD28 stimulated T-cells

Project description:Investigation of expression effects of HSP90 inhibition by 17-AAG of proteins in resting and activated T-cells.

2018-05-02 | PXD008627 | Pride

Multiplexed proteome dynamics profiling of HSP90 inhibitor 17-AAG

Project description:Investigation of proteostatic effects of HSP90 inhibition by 17-AAG and differentiation of maturation state dependent HSP90 requirements of proteins.

2018-04-05 | PXD008633 | Pride

Multiplexed proteome dynamics profiling of HSP90 inhibitor 17-AAG in T-cells

Project description:Investigation of proteostatic effects of HSP90 inhibition by 17-AAG and differentiation of maturation state dependent HSP90 requirements of proteins in resting T-cells.

2018-05-02 | PXD008635 | Pride

Expression data from human colonic cancer cell line SW480 and its acquired 17-AAG resistance cell line SW480-R

Project description:Heat shock protein 90 (HSP90) is a molecular chaperone required for the stability and function of many proteins. The chaperoning of oncoproteins by HSP90 enhances survival, growth and invasive potential of cancer cells. HSP90 inhibitors are promising new anticancer agents, in which the benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin (17-AAG) is currently in clinical evaluation. However, the implications of acquired resistance to this class of drug remain largely unexplored. In the present study, we have generated isogenic human colonic cancer cell line SW480 that is resistant to 17-AAG by continued culturing in the compound. We used microarrays to detail the global programme of gene expression underlying the acquired resistance to 17-AAG in SW480 and SW480-R cell lines.

2015-03-14 | GSE66867 | GEO

Wee1 Inhibition sensitizes prostate cancer cells to Hsp90 inhibitor to activate the intrinsic apoptotic pathway

Project description:Heat shock protein 90 (Hsp90) is an essential evolutionarily conserved molecular chaperone in eukaryotes. Cancer cells rely on Hsp90 to chaperone activated oncoproteins, and its involvement in numerous signaling pathways makes it an attractive target for drug development. Surprisingly, however, the impact of Hsp90 inhibitors on cancer cells is most commonly cytostatic, and efforts to enhance the anti-tumor activity of Hsp90 inhibitors in the clinic remain a significant challenge. In this study, we show that dual inhibition of Wee1 tyrosine kinase and Hsp90 causes prostate cancer cells to undergo apoptosis. Gene-expression profiling revealed that induction of the intrinsic apoptotic pathway by this drug combination coincided with transcriptional down-regulation of Survivin and Wee1, an outcome not seen in cells treated separately with either agent. At the translational level, expression of these two proteins as well as activated Akt was completely abrogated. Similar results were obtained in prostate cancer xenografts. These data establish a novel therapeutic strategy to enhance the efficacy of Hsp90 inhibitors in prostate cancer, and they provide a mechanistic rationale for stimulating the pro-apoptotic activity of Hsp90 inhibitors. In order to explore the mechanism underlying the enhanced cell death caused by Wee1 inhibitorII and 17-AAG combination, we performed microarray analysis using PC3 cells treated with Wee1 inhibitorII alone, 17-AAG alone, or the two drugs in combination. There are 12 samples in total. There are three experimental replicate. Samples 1, 5 and 9 are control (C) (untreated PC3- prostate cancer cells). Samples 2, 6, and 10 are cells treated with Wee1 inhibitor II (W). Samples 3, 7, and 11 are treated with 17-AAG (A), (an Hsp90 inhibitor). Samples 4, 8, and 12 are treated with both Wee1 inhibitorII and 17-AAG (WA). Samples 5 was removed from our analysis due to weak signal.

2013-01-10 | E-GEOD-38972 | biostudies-arrayexpress

Native SEC-MS of the human HT29 colon adenocarcinoma cell line treated with the HSP90 inhibitor tanespimycin (17-AAG)

Project description:The molecular chaperone heat shock protein 90 (HSP90) works in concert with its co-chaperones to stabilize its client proteins, which include several drivers of oncogenesis and malignant progression. Pharmacologic inhibitors of HSP90 are proposed to trigger widespread remodeling of cellular protein complexes, including dissociation of co-chaperones from HSP90, disruption of client protein signaling networks, and recruitment of the protein ubiquitination and degradation machinery. However, proteomic studies to date have focused on inhibitor-induced changes in total protein levels, often overlooking protein complex alterations. Here, we use size-exclusion chromatography in combination with mass spectrometry (SEC-MS) to characterize the changes in native protein complexes following treatment with the HSP90 inhibitor 17-AAG in the human HT29 colon adenocarcinoma cell line.

2022-12-20 | PXD033459 | Pride

Drug combination of 17-AAG and Belinostat on MDA-MB-231 breast cancer cells

Project description:Breast cancer is the most common cancer that threatens women's health. While the strategy of drug combination can help to reduce adverse effects and to overcome the resistance of clinical treatment of single drug. In this work, we report the synergetic effect between a HSP90 inhibitor 17-AAG and a HDAC inhibitor Belinostat, on the triple-negative breast cancer MDA-MB-231 cells. The RNA-Seq data analysis showed that the most over-represented KEGG pathways in the combination group came from migration or invasion related genes, which were not observed in the differentially expressed genes after the treatment of 17-AAG or Belinostat alone.

2019-05-17 | GSE129944 | GEO

Molecular Signature of response and potential pathways related to resistance to the HSP90 inhibitor, 17-AAG, in breast cancer.

Project description:We have done transcriptional profiling of 17-AAG treated (24h, 48H) breast cancer cell lines to understand the mechanisms of the drug action and indicate novel set of pharmacodynamic biomarkers of the drug response as well as of resistance Two-condition experiment, Untreated vs. Treated sensitive cells. Phenotype replicates: 8 untreated replicates, 14 treated replicates.

2010-10-11 | E-GEOD-23209 | biostudies-arrayexpress

Expression data from 17-AAG resistance cell line

Project description:Develop the 17-AAG resistance human lung cancer cell line and used microarrays to observe the gene alternnation

2017-01-11 | GSE93384 | GEO

Aedes aegypti Aag-2 cells proteome modulation in response to Chikungunya virus infection

Project description:Chikungunya virus (CHIKV) is a single-stranded positive RNA virus that belongs to the genus Alphavirus and is transmitted to humans by infected Aedes aegypti and Aedes albopictus bites. In humans, CHIKV can cause painful symptoms during acute and chronic stages of infection. However, the virus-vector interaction has characteristics that allow a persistent infection, not disturbing the mosquito’s fitness. Here, we aimed to clarify aspects of CHIKV infection in Ae. aegypti Aag-2 cells through label-free quantitative proteomic analysis and transmission electron microscopy (TEM). We used MOI 0.1 to infect Aag-2 cells in biological triplicates over 48 h. TEM images show a high load of intracellular viral cargo at 48 hpi, as well as an elongated unusual mitochondria morphology that might indicate a mitochondrial imbalance. Moreover, a total of 196 Ae. aegypti protein groups were up or downregulated upon infection, related to protein synthesis, energy metabolism, signaling pathways and apoptosis. These regulated Aag-2 proteins might have roles in antiviral and/or in pro-viral mechanisms during CHIKV infection, to support the balance between viral propagation and the survival of host cell, leading to the persistent infection.

2022-06-02 | PXD033231 | Pride

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