Temporal proteome profiling of taxol‐induced mitotic arrest and apoptosis

Bull, Vibeke Hervik; Fargestad, Ellen M.; Strozynski, Margarita; Thiede, Bernd

doi:10.1002/elps.200900780

Cited by 15 publications

(9 citation statements)

References 70 publications

(66 reference statements)

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“…Protein statistics (unpaired t-test, p<0.05) was performed in the Biological Variation Analysis module, excluding proteins present in less than 80% of the spotmaps. SyproRuby stained single gels spots were in-gel digested for 16 hours prior to peptide identification using the LTQ-Orbitrap XL (Thermo Scientific, Waltham, MA, USA) as described [28]. A minor adjustment was made increasing the starting solvent from 0 to 7% B.…”

Section: Methodsmentioning

confidence: 99%

Cross-Species Functional Genomic Analysis Identifies Resistance Genes of the Histone Deacetylase Inhibitor Valproic Acid

et al. 2012

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The mechanisms of successful epigenetic reprogramming in cancer are not well characterized as they involve coordinated removal of repressive marks and deposition of activating marks by a large number of histone and DNA modification enzymes. Here, we have used a cross-species functional genomic approach to identify conserved genetic interactions to improve therapeutic effect of the histone deacetylase inhibitor (HDACi) valproic acid, which increases survival in more than 20% of patients with advanced acute myeloid leukemia (AML). Using a bidirectional synthetic lethality screen revealing genes that increased or decreased VPA sensitivity in C. elegans, we identified novel conserved sensitizers and synthetic lethal interactors of VPA. One sensitizer identified as a conserved determinant of therapeutic success of HDACi was UTX (KDM6A), which demonstrates a functional relationship between protein acetylation and lysine-specific methylation. The synthetic lethal screen identified resistance programs that compensated for the HDACi-induced global hyper-acetylation, and confirmed MAPKAPK2, HSP90AA1, HSP90AB1 and ACTB as conserved hubs in a resistance program for HDACi that are drugable in human AML cell lines. Hence, these resistance hubs represent promising novel targets for refinement of combinatorial epigenetic anti-cancer therapy.

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Section: Methodsmentioning

confidence: 99%

Cross-Species Functional Genomic Analysis Identifies Resistance Genes of the Histone Deacetylase Inhibitor Valproic Acid

et al. 2012

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“…Of interest, increased expression of TCTP is revealed to have an interrelation with increased chemoresistance, of malignant melanoma to cytotoxic agents such as etoposide and its increased survival [16]. In addition, a temporal proteome profiling upon taxol exposure, revealed increased TCTP expression during apoptosis [17]. Studies of colon cancer cell response to oxaliplatin treatment revealed temporal upregulation of TCTP [18].…”

Section: Introductionmentioning

confidence: 99%

Interaction of translationally controlled tumor protein with Apaf-1 is involved in the development of chemoresistance in HeLa cells

et al. 2014

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BackgroundTranslationally controlled tumor protein (TCTP), alternatively called fortilin, is believed to be involved in the development of the chemoresistance of tumor cells against anticancer drugs such as etoposide, taxol, and oxaliplatin, the underlying mechanisms of which still remain elusive.MethodsCell death analysis of TCTP-overexpressing HeLa cells was performed following etoposide treatment to assess the mitochondria-dependent apoptosis. Apoptotic pathway was analyzed through measuring the cleavage of epidermal growth factor receptor (EGFR) and phospholipase C-γ (PLC-γ), caspase activation, mitochondrial membrane perturbation, and cytochrome c release by flow cytometry and western blotting. To clarify the role of TCTP in the inhibition of apoptosome, in vitro apoptosome reconstitution and immunoprecipitation was used. Pull-down assay and silver staining using the variants of Apaf-1 protein was applied to identify the domain that is responsible for its interaction with TCTP.ResultsIn the present study, we confirmed that adenoviral overexpression of TCTP protects HeLa cells from cell death induced by cytotoxic drugs such as taxol and etoposide. TCTP antagonized the mitochondria-dependent apoptotic pathway following etoposide treatment, including mitochondrial membrane damage and resultant cytochrome c release, activation of caspase-9, and -3, and eventually, the cleavage of EGFR and PLC-γ. More importantly, TCTP interacts with the caspase recruitment domain (CARD) of Apaf-1 and is incorporated into the heptameric Apaf-1 complex, and that C-terminal cleaved TCTP specifically associates with Apaf-1 of apoptosome in apoptosome-forming condition thereby inhibiting the amplification of caspase cascade.ConclusionsTCTP protects the cancer cells from etoposide-induced cell death by inhibiting the mitochondria-mediated apoptotic pathway. Interaction of TCTP with Apaf-1 in apoptosome is involved in the molecular mechanism of TCTP-induced chemoresistance. These findings suggest that TCTP may serve as a therapeutic target for chemoresistance in cancer treatment.

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“…Calumenin was also described in functional association with the cytoskeleton where it is translocated from the organelle-containing membrane fraction to the cytosol upon mitotic arrest and during late apoptosis in HeLa cells, treated with the tubulin-depolymerizing drug taxol (Bull et al, 2010). Additionally, extracellular calumenin appears to have an autocrine and/or paracrine modulating effect on organization of the actin cytoskeleton (Ostergaard et al, 2006).…”

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confidence: 99%

Spatio-temporal expression analysis of the calcium-binding protein calumenin in the rodent brain

Vasiljevic¹,

Heisler²,

Hausrat³

et al. 2012

Neuroscience

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Calumenin is a Ca2+-binding protein that belongs to the CREC superfamily. It contains six EF-hand domains that exhibit a low affinity for Ca2+ as well as an endoplasmic reticulum retention signal. Calumenin exhibits a broad and relatively high expression in various brain regions during development as demonstrated by in situ hybridization. Signal intensity of calumenin is highest during the early development and then declines over time to reach a relatively low expression in adult animals. Immunohistochemistry indicates that at the P0 stage, calumenin expression is most abundant in migrating neurons in the zones around the lateral ventricle. In the brain of adult animals, it is expressed in various glial and neuronal cell types, including immature neurons in subgranular zone of hippocampal dentate gyrus. At the subcellular level, calumenin is identified in punctuate and diffuse distribution mostly in somatic regions where it co-localizes with endoplasmic reticulum (ER) and partially Golgi apparatus. Upon subcellular fractionation, calumenin is enriched in fractions containing membranes and is only weakly present in soluble fractions. This study points to a possible important role of calumenin in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons.

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Temporal proteome profiling of taxol‐induced mitotic arrest and apoptosis

Cited by 15 publications

References 70 publications

Cross-Species Functional Genomic Analysis Identifies Resistance Genes of the Histone Deacetylase Inhibitor Valproic Acid

Cross-Species Functional Genomic Analysis Identifies Resistance Genes of the Histone Deacetylase Inhibitor Valproic Acid

Interaction of translationally controlled tumor protein with Apaf-1 is involved in the development of chemoresistance in HeLa cells

Spatio-temporal expression analysis of the calcium-binding protein calumenin in the rodent brain

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