Preparative High-Resolution Two-Dimensional Electrophoresis Enables the Identification of RNA Polymerase B Transcription Factor 3 as an Apoptosis-Associated Protein in the Human BL60–2 Burkitt Lymphoma Cell Line

Brockstedt, Ekkehard; Otto, Albrecht; Rickers, Anke; Bommert, Kurt; Wittmann‐Liebold, Brigitte

doi:10.1023/a:1020636308270

Cited by 50 publications

(23 citation statements)

References 33 publications

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“…SU11248 treatment also resulted in increased levels of TC-PTP and BTF3, genes involved in apoptosis (Brockstedt et al, 1999;Gupta et al, 2002). Regulation of these markers is also consistent with the previously observed dose-dependent induction of apoptosis in xenograft models by SU11248 Potapova et al, 2003).…”

Section: Discussionsupporting

confidence: 88%

Gene expression profiling of human colon xenograft tumors following treatment with SU11248, a multitargeted tyrosine kinase inhibitor

Morimoto¹,

Tan²,

West³

et al. 2004

Oncogene

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Section: Discussionsupporting

confidence: 88%

Gene expression profiling of human colon xenograft tumors following treatment with SU11248, a multitargeted tyrosine kinase inhibitor

Morimoto¹,

Tan²,

West³

et al. 2004

Oncogene

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“…Among these proteins, ␣ NAC, hnRNP A0, hnRNP A2/B1, hnRNP A3, hnRNP K, hnRNP R, KH-type splicing regulatory protein, NS1-associated protein 1, p54 nrb , poly(A)-binding protein 4, and splicing factors ASF-2 and SRp30c were not known to be modified during apoptosis. However, we also identified proteins that were previously found to be modified during apoptosis by a proteome approach using the Burkitt lymphoma B cell line HL-60 and IgM as an inducer of apoptosis (16,40,41). These proteins included hnRNP A1, hnRNP C1/C2, FUSEbinding protein, nucleolin, Rho GDI 2, and the transcription factor BTF3.…”

Section: Discussionmentioning

confidence: 95%

Predominant Identification of RNA-binding Proteins in Fas-induced Apoptosis by Proteome Analysis

Thiede

Dimmler

Siejak

et al. 2001

Journal of Biological Chemistry

122

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Proteome analysis of Jurkat T cells was performed in order to identify proteins that are modified during apoptosis. Subtractive analysis of two-dimensional gel patterns of apoptotic and nonapoptotic cells revealed differences in 45 protein spots. 37 protein spots of 21 different proteins were identified by peptide mass fingerprinting using matrix-assisted laser desorption/ionization mass spectrometry. The hnRNPs A0, A2/B1, A3, K, and R; the splicing factors p54 nrb , SRp30c, ASF-2, and KH-type splicing regulatory protein (FUSE-binding protein 2); and ␣ NAC, NS1-associated protein 1, and poly(A)-binding protein 4 were hitherto unknown to be involved in apoptosis. The putative cleavage sites of the majority of the proteins could be calculated by the molecular masses and isoelectric points in the two-dimensional electrophoresis gel, the peptide mass fingerprints, and after translation by treatment with recombinant caspase-3. Remarkably, 15 of the 21 identified proteins contained the RNP or KH motif, the best characterized RNA-binding motifs.

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“…TNFAIP3 and API2 are antiapoptotic factors whose genes are transcriptionally up-regulated by infection (14,15). Furthermore, transcription of BTF3, a transcription factor associated with apoptosis, is decreased (16). Given that monocytes and neutrophils have been described to undergo apoptosis in response to B. pertussis infection (17)…”

Section: The Transcriptional Profile Of Beas-2b Cells Infected With Bmentioning

confidence: 99%

The transcriptional responses of respiratory epithelial cells toBordetella pertussisreveal host defensive and pathogen counter-defensive strategies

Belcher

Drenkow

Kehoe

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

140

104

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Bordetella pertussis, the causative agent of whooping cough, has many well-studied virulence factors and a characteristic clinical presentation. Despite this information, it is not clear how B. pertussis interaction with host cells leads to disease. In this study, we examined the interaction of B. pertussis with a human bronchial epithelial cell line (BEAS-2B) and measured host transcriptional profiles by using high-density DNA microarrays. The early transcriptional response to this pathogen is dominated by altered expression of cytokines, DNA-binding proteins, and NFB-regulated genes. This previously unrecognized response to B. pertussis was modified in similar but nonidentical fashions by the antiinflammatory agents dexamethasone and sodium salicylate. Cytokine protein expression was confirmed, as was neutrophil chemoattraction. We show that B. pertussis induces mucin gene transcription by BEAS-2B cells then counters this defense by using mucin as a binding substrate. A set of genes is described for which the catalytic activity of pertussis toxin is both necessary and sufficient to regulate transcription. Host genomic transcriptional profiling, in combination with functional assays to evaluate subsequent biological events, provides insight into the complex interaction of host and pathogen. Bordetella pertussis is a Gram-negative coccobacillus and the causative agent of whooping cough in humans. It is a well-studied pathogen with a number of potent virulence factors. However, little is known about the responses elicited by this organism in human cells, especially at the level of gene transcription.Autopsy studies of pertussis victims performed in the early 20th century revealed a diffuse bronchopneumonia with increased secretion of mucus, associated with airway plugging and atelectasis (1). Bacteria were seen tightly packed between the cilia of epithelial cells, which desquamated during infection. Rodent models of Bordetella pertussis infection have revealed infiltrates of monocytes, neutrophils, and lymphocytes in the lung (2).B. pertussis expresses several virulence factors directed at the host epithelium. Filamentous hemagglutinin is the major adhesin of B. pertussis for bronchial epithelial cells (3). B. pertussis also produces several toxins, including pertussis toxin (PT). PT is associated with a panoply of biological effects, many of which are linked to its ADP-ribosyltransferase activity. ADP ribosylation of the G␣ family of host proteins prevents their usual regulatory response to G-protein-linked receptor engagement (4). B. pertussis also secretes an adenylate cyclase toxin that enters host cells and raises intracellular cAMP concentrations (5). Tracheal cytotoxin (TCT), a muramyl tetrapeptide bacterial cell wall fragment, in combination with lipopolysaccharide, paralyzes respiratory epithelial cilia and ultimately causes cell death and extrusion through pathways involving IL-1 and nitric oxide synthase (iNOS) (6). The molecular mechanisms through which B. pertussis exerts these effects and by which h...

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Preparative High-Resolution Two-Dimensional Electrophoresis Enables the Identification of RNA Polymerase B Transcription Factor 3 as an Apoptosis-Associated Protein in the Human BL60–2 Burkitt Lymphoma Cell Line

Cited by 50 publications

References 33 publications

Gene expression profiling of human colon xenograft tumors following treatment with SU11248, a multitargeted tyrosine kinase inhibitor

Gene expression profiling of human colon xenograft tumors following treatment with SU11248, a multitargeted tyrosine kinase inhibitor

Predominant Identification of RNA-binding Proteins in Fas-induced Apoptosis by Proteome Analysis

The transcriptional responses of respiratory epithelial cells toBordetella pertussisreveal host defensive and pathogen counter-defensive strategies

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