Quantitative analysis of 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels

Sarioglu, Hakan; Brandner, Sebastian; Jacobsen, Carola; Meindl, T; Schmidt, Alexander; Kellermann, Josef; Lottspeich, Friedrich; Andrae, U.

doi:10.1002/pmic.200500680

Cited by 49 publications

(62 citation statements)

References 103 publications

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“…Out of these 168 nonredundant proteins, a mutant/control (H/L) protein ratio was calculated for 130 of them (all 130 proteins are listed in supplementary Table 3, and all peptide sequences for the identified proteins are listed in supplementary Table 4); for the remaining 38, this was not possible because of the absence of detected labeled peptides from either the control or the mutant sample. The minimum variation of H/L ratios associated to significant variation of protein expression was determined similarly to (34). The average of the CV (coefficient of variation) obtained for H/L ratios of all proteins for which at least two peptides were quantified was 11.1%.…”

Section: Sc-expressed Mirnas Affect Testicular Transcription-wementioning

confidence: 99%

Loss of Dicer in Sertoli Cells Has a Major Impact on the Testicular Proteome of Mice

Papaioannou

Lagarrigue

Vejnar

et al. 2011

Molecular & Cellular Proteomics

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Sertoli cells (SCs) are the central, essential coordinators of spermatogenesis, without which germ cell development cannot occur. We previously showed that Dicer, an RNaseIII endonuclease required for microRNA (miRNA) biogenesis, is absolutely essential for Sertoli cells to mature, survive, and ultimately sustain germ cell development. Here, using isotope-coded protein labeling, a technique for protein relative quantification by mass spectrometry, we investigated the impact of Sertoli cell-Dicer and subsequent miRNA loss on the testicular proteome. We found that, a large proportion of proteins (50 out of 130) are up-regulated by more that 1.3-fold in testes lacking Sertoli cell-Dicer, yet that this protein up-regulation is mild, never exceeding a 2-fold change, and is not preceeded by alterations of the corresponding mRNAs. Of note, the expression levels of six proteins of interest were further validated using the Absolute Quantification (AQUA) peptide technology. Furthermore, through 3UTR luciferase assays we identified one up-regulated protein, SOD-1, a Cu/Zn superoxide dismutase whose overexpression has been linked to enhanced cell death through apoptosis, as a likely direct target of three Sertoli cell-expressed miRNAs, miR-125a-3p, miR-872 and miR-24. Altogether, our study, which is one of the few in vivo analyses of miRNA effects on protein output, suggests that, at least in our system, miRNAs play a significant role in translation control.

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Section: Sc-expressed Mirnas Affect Testicular Transcription-wementioning

confidence: 99%

Loss of Dicer in Sertoli Cells Has a Major Impact on the Testicular Proteome of Mice

Papaioannou

Lagarrigue

Vejnar

et al. 2011

Molecular & Cellular Proteomics

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“…Moreover they have been successfully used in projects aiming at the identification of novel target genes of the AhR (14,35). We recently reported results of a proteomics study in which the effects of TCDD on 5L cells were investigated using an LC-based mass spectrometric approach, the so-called isotope-coded protein label (ICPL) method (36,37). In this study, we identified 89 protein species of various functional categories as up-or down-regulated by TCDD.…”

Section: Molecular and Cellular Proteomics 7:394 -410 2008mentioning

confidence: 99%

Analysis of 2,3,7,8-Tetrachlorodibenzo-p-dioxin-induced Proteome Changes in 5L Rat Hepatoma Cells Reveals Novel Targets of Dioxin Action Including the Mitochondrial Apoptosis Regulator VDAC2

Sarioglu

Brandner

Haberger

et al. 2008

Molecular & Cellular Proteomics

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As part of a comprehensive survey of the impact of the environmental pollutant and hepatocarcinogen 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on the proteome of hepatic cells, we have performed a high resolution twodimensional gel electrophoresis study on the rat hepatoma cell line 5L. 78 protein species corresponding to 73 different proteins were identified as up-or down-regulated following exposure of the cells to 1 nM TCDD for 8 h. There was an overlap of only nine proteins with those detected as altered by TCDD in our recent study using the non-gel-based isotope-coded protein label method (Sarioglu, H., Brandner, S., Jacobsen, C., Meindl, T., Schmidt, A., Kellermann, J., Lottspeich, F., and Andrae, U. The environmental contaminant 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) 1 is the prototype of a class of compounds known as halogenated aromatic hydrocarbons that includes dibenzo-p-dioxins, dibenzofurans, and polychlorinated biphenyls. TCDD has been shown to cause a wide variety of toxic effects and is regarded as the most potent hepatocarcinogen in experimental animals (1). Epidemiological evidence suggests that TCDD is also a human carcinogen (2, 3). The molecular mechanisms underlying the tumorigenic activity of the compound are still largely unknown, which strongly hampers the estimation of the risk to humans associated with dioxin exposure and necessitates further studies aimed at the clarification of these mechanisms. Moreover the multifaceted toxicity of TCDD makes it a very attractive model compound for studies addressing the identification of basic principles associated with the disturbance of cellular homeostasis.

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“…7,8 The separation of peptides by onedimensional nano reverse-phase liquid chromatography and their identification by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF/TOF), including the use of the GPS Explorer software for protein identification, were performed as described. 16 …”

Section: Reporter Gene Assaysmentioning

confidence: 99%

Proteomic identification of the MYST domain histone acetyltransferase TIP60 (HTATIP) as a co-activator of the myeloid transcription factor C/EBPα

et al. 2008

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The transcription factor C/EBPa (CEBPA) is a key player in granulopoiesis and leukemogenesis. We have previously reported the interaction of C/EBPa with other proteins (utilizing mass spectrometry) in transcriptional regulation. In the present study, we characterized the association of the MYST domain histone acetyltransferase Tat-interactive protein (TIP) 60 (HTA-TIP) with C/EBPa. We show in pull-down and co-precipitation experiments that C/EBPa and HTATIP interact. A chromatin immunoprecipitation (ChIP) and a confirmatory Re-ChIP assay revealed in vivo occupancy of the C/EBPa and GCSF-R promoter by HTATIP. Reporter gene assays showed that HTATIP is a coactivator of C/EBPa. The co-activator function of HTATIP is dependent on its intact histone acetyltransferase (HAT) domain and on the C/EBPa DNA-binding domain. The resulting balance between histone acetylation and deacetylation at the C/EBPa promoter might represent an important mechanism of C/EBPa action. We observed a lower expression of HTATIP mRNA in undifferentiated U937 cells compared to retinoic acid-induced differentiated U937 cells, and correlated expression of CEBPA and HTATIP mRNA levels were observed in leukemia samples. These findings point to a functional synergism between C/EBPa and HTATIP in myeloid differentiation and suggest that HTATIP might be an important player in leukemogenesis.

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Quantitative analysis of 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels

Cited by 49 publications

References 103 publications

Loss of Dicer in Sertoli Cells Has a Major Impact on the Testicular Proteome of Mice

Loss of Dicer in Sertoli Cells Has a Major Impact on the Testicular Proteome of Mice

Analysis of 2,3,7,8-Tetrachlorodibenzo-p-dioxin-induced Proteome Changes in 5L Rat Hepatoma Cells Reveals Novel Targets of Dioxin Action Including the Mitochondrial Apoptosis Regulator VDAC2

Proteomic identification of the MYST domain histone acetyltransferase TIP60 (HTATIP) as a co-activator of the myeloid transcription factor C/EBPα

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