Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells

Tenev, Tencho; Böhmer, Sylvia‐Annette; Kaufmann, Roland; Frese, Steffen; Bittorf, Thomas; Beckers, Thomas; Böhmer, Frank‐D.

doi:10.1078/s0171-9335(04)70029-1

Cited by 69 publications

(50 citation statements)

References 38 publications

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“…27 Fulllength human caspase -3 cDNA was generated by reverse transcriptase polymerase chain reaction ( PCR ) from OVCAR3 cells and cloned as an EcoRI fragment into pNRTIS -33. 25 Plasmid maps are presented in Figure 1a.…”

Section: Construction Of Plasmidsmentioning

confidence: 99%

Herpes simplex virus thymidine kinase/ganciclovir–induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells

et al. 2001

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There is a need to enhance the efficacy of genetic prodrug activation therapy using herpes simplex virus thymidine kinase ( tk ) and ganciclovir ( GCV ) following disappointing results in early clinical trials. tk / GCV has been shown to lead to the activation of caspase -3, a potent executor of apoptosis. We demonstrate that co -expression of pro -caspase -3 with tk / GCV leads to enhanced cell death in ovarian carcinoma cells in vitro. Following transfection with recombinant adenoviral vectors encoding tk, GCV treatment leads to greater cell death in pro -caspase -3 ± expressing clones of SKOV3 and IGROV1 than control cells, as well as more rapid activation of caspase -3 and more rapid cleavage of PARP. Flow cytometry suggests that there is a greater degree of S -phase block in the pro -caspase -3 ± expressing clones than in control cells following treatment with tk / GCV. None of these effects is seen following transfection with a control adenovirus that does not encode tk. The increased cell death, early caspase -3 activation and PARP cleavage, and flow cytometric changes seen in pro -caspase -3 ± expressing cells can be partially inhibited by treatment with benzyloxycarbonyl ± val ± ala ± asp fluoromethylketone, a synthetic caspase inhibitor. Our data suggest that co -expression of procaspase -3 may lead to a significant enhancement of the efficacy of tk / GCV therapy. Cancer Gene Therapy ( 2001 ) 8, 308 ± 319

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Section: Construction Of Plasmidsmentioning

confidence: 99%

Herpes simplex virus thymidine kinase/ganciclovir–induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells

et al. 2001

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“…pmEGFP-b was prepared by inserting the EGFP-coding sequence from pEGFP-c1 into the pNRTIS-21 vector. 28 The pmEGFP-b construct contains a premature stop codon at Lys 41 (AAG) to stop 41 (TAG) that renders the EGFP protein nonfluorescent and the following silent point mutations: Gly 31 (GGC to GGA), Gly 33 (GGC to GGA), Gly 35 (GGC to GGA) and Gly 40 (GGC to GGA). The pmEGFP-a and pmEGFP-b constructs were stably transfected into CHO cells and individual clones were isolated after G418 selection (0.8 mg/ml).…”

mentioning

confidence: 99%

Implications of cell cycle progression on functional sequence correction by short single-stranded DNA oligonucleotides

Olsen¹,

Randøl²,

Krauß³

2005

Gene Ther

106

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Oligonucleotide-based sequence alteration in living cells is a substantial methodological challenge in gene therapy. Here, we demonstrate that using corrective single-stranded oligonucleotides (ssODN), high and reproducible sequence correction rates can be obtained. CHO cell lines with chromosomally integrated multiple copy EGFP reporter genes routinely show rates of 4.5% targeted sequence correction after transfection with ssODN. We demonstrate that the cell cycle influences the rates of targeted sequence correction in vivo, with a peak in the early S phase during ssODN exposure. After cell division, the altered genomic sequence is predominantly passed to one daughter cell, indicating that targeted sequence alteration occurs after the replication fork has passed over the targeted site. Although high initial correction rates can be obtained by this method, we show that a majority of the corrected cells arrest in the G2/M cell cycle phase, although 1-2% of the corrected cells form viable colonies. The G2/M arrest observed after targeted sequence correction can be partially released by caffeine, pentoxifylline or Gö 6976 exposure. Despite substantial remaining challenges, targeted sequence alteration based on ssODN increasingly promises to become a powerful tool for functional gene alterations. Gene Therapy (2005) Various strategies have been developed to achieve therapeutic targeted gene repair, including small fragment homologous sequence 1,2 ssODN, 3-6 triple helixforming oligonucleotides containing a reactive group, 7-9 bifunctional oligonucleotides based on a triple helixforming DNA recognition domain 10,11 and branched oligonucleotides. 12 Although a general proof of principle for oligonucleotide-based sequence alteration appears to be established, the paradigm for oligonucleotide-based genome alteration remain largely unknown. 6 The central problem in studying this phenomenon are low rates of in vivo sequence correction rates in cell culture. Generally, observed sequence alteration rates on in vivo chromosomal templates in selected cell lines are in the range of 0.1%, 6 while correction rates in untransformed primary cells are substantially lower. [13][14][15] In the absence of a suitable selection system, such low rates allow only limited functional analysis, although Yoon and co-workers have recently suggested a selection system based on simultaneous targeting of two loci. 16 A further problem is the variety of model systems and assays that were used to measure targeted sequence correction which lead to confusing and often conflicting results. 6 Despite these obstacles, several consistent observations have been made: targeted sequence correction depends centrally on transcription, and ssODN that are complementary to the nontranscribed strand show in most cases substantially higher correction rates than ssODN complementary to the transcribed strand in both episomal and chromosomal assays. 17,18 The involvement of transcription-coupled repair has therefore been suggested. Furthermore, the absence of MSH2, ...

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“…24 Constitutively active caspase-3 (reverse caspase-3) was kindly provided from Dr ES Alnemri. 46 HEK 293 cells were transiently transfected with plasmids using a Calcium Phosphate Transfection kit (Invitrogen).…”

Section: Plasmids and Transient Transfectionmentioning

confidence: 99%

“…24 Stable derivatives of the OVCAR3 and SKOV3 cell lines were generated after transfection with control or procaspase-3 expression vectors. Several clones inducibly expressing pro-caspase 3 were isolated.…”

Section: Generation Of Skov3 and Ovcar3 Stable Cell Lines Expressing mentioning

confidence: 99%

Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors

et al. 2001

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The ubiquitin-proteasome pathway plays a critical role in the degradation of several proteins involved in the cell cycle. Dysregulation of this pathway leads to inhibition of cellular proliferation and the induction of apoptosis. Ubiquitination and its downstream consequences have been investigated intensively as targets for the development of drugs for tumour therapy. Here we have investigated the mechanism of apoptosis induced by the proteasome inhibitors MG-132, lactacystin and calpain inhibitor I (ALLN), in the HEK 293 cell line and the ovarian cancer cell lines SKOV3 and OVCAR3. We have found strong caspase-3-like and caspase-6-like activation upon treatment of HEK 293 cells with MG-132. Using a tricistronic expression vector based on a tetracyclineresponsive system we generated stable SKOV3 nd OVCAR3 cell lines with inducible expression of pro-caspase-3. Induction of pro-caspase-3 expression in normally growing cells does not induce apoptosis. However, in the presence of the proteasome inhibitors MG-132, lactacystin or ALLN we found that cells overexpressing pro-caspase-3 are rapidly targeted for apoptosis. Our results demonstrate that procaspase-3 can sensitise ovarian cancer cells to proteasome inhibitor-induced apoptosis, and a combination of these approaches might be exploited for therapy of ovarian and other cancers.Cell Death and Differentiation (2001) 8, 256 ± 264.

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Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells

Cited by 69 publications

References 38 publications

Herpes simplex virus thymidine kinase/ganciclovir–induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells

Herpes simplex virus thymidine kinase/ganciclovir–induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells

Implications of cell cycle progression on functional sequence correction by short single-stranded DNA oligonucleotides

Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors

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