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Wafik S. El-deiry - One of the best experts on this subject based on the ideXlab platform.
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BRCA1 Transcriptionally Regulates Damaged DNA Binding Protein (DDB2) In the DNA Repair Response Following UV-Irradiation
Cancer Biology & Therapy, 2002Co-Authors: Rishu Takimoto, Timothy K. Maclachlan, David T. Dicker, Yoshiro Niitsu, Toshio Mori, Wafik S. El-deiryAbstract:The p53 and BRCA1 tumor suppressors are involved in repair processes and may cooperate to transactivate certain genes, including p21WAF1/CIP1 and GADD45. We find that the Xeroderma Pigmentosum Complementation group E (XPE) mutated Damaged-DNA binding Protein p48 (DDB2) is upregulated by BRCA1 in a p53-dependent manner following UVC, Adriamycin, or Cisplatin exposure. BRCA1 enhances p53 binding to the DDB2 promoter in vivo as well as p53-dependent transactivation of DDB2 promoter-reporter constructs through a classical p53 DNA responsive element. Antisense abrogation of BRCA1 expression abrogates upregulation of DDB2 after UVC or cisplatin exposure. Using a host cell reactivation assay, DNA repair activity is more significantly restored by introduction of BRCA1 into wt as compared to DDB2-deficient cells. Furthermore disappearance of the photoproducts cyclobutane pyrimidine dimer (CPD) and 6-4 photoproduct (6-4PP) was delayed by antisense abrogation of BRCA1 expression in UV-exposed human cells. Thus the D...
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BRCA1 Transcriptionally Regulates Damaged DNA Binding Protein (DDB2) In the DNA Repair Response Following UV-Irradiation
Cancer Biology & Therapy, 2002Co-Authors: Rishu Takimoto, Timothy K. Maclachlan, David T. Dicker, Yoshiro Niitsu, Toshio Mori, Wafik S. El-deiryAbstract:The p53 and BRCA1 tumor suppressors are involved in repair processes and may cooperate to transactivate certain genes, including p21WAF1/CIP1 and GADD45. We find that the Xeroderma Pigmentosum Complementation group E (XPE) mutated Damaged-DNA binding Protein p48 (DDB2) is upregulated by BRCA1 in a p53-dependent manner following UVC, Adriamycin, or Cisplatin exposure. BRCA1 enhances p53 binding to the DDB2 promoter in vivo as well as p53-dependent transactivation of DDB2 promoter-reporter constructs through a classical p53 DNA responsive element. Antisense abrogation of BRCA1 expression abrogates upregulation of DDB2 after UVC or cisplatin exposure. Using a host cell reactivation assay, DNA repair activity is more significantly restored by introduction of BRCA1 into wt as compared to DDB2-deficient cells. Furthermore disappearance of the photoproducts cyclobutane pyrimidine dimer (CPD) and 6-4 photoproduct (6-4PP) was delayed by antisense abrogation of BRCA1 expression in UV-exposed human cells. Thus the D...
Rishu Takimoto - One of the best experts on this subject based on the ideXlab platform.
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BRCA1 Transcriptionally Regulates Damaged DNA Binding Protein (DDB2) In the DNA Repair Response Following UV-Irradiation
Cancer Biology & Therapy, 2002Co-Authors: Rishu Takimoto, Timothy K. Maclachlan, David T. Dicker, Yoshiro Niitsu, Toshio Mori, Wafik S. El-deiryAbstract:The p53 and BRCA1 tumor suppressors are involved in repair processes and may cooperate to transactivate certain genes, including p21WAF1/CIP1 and GADD45. We find that the Xeroderma Pigmentosum Complementation group E (XPE) mutated Damaged-DNA binding Protein p48 (DDB2) is upregulated by BRCA1 in a p53-dependent manner following UVC, Adriamycin, or Cisplatin exposure. BRCA1 enhances p53 binding to the DDB2 promoter in vivo as well as p53-dependent transactivation of DDB2 promoter-reporter constructs through a classical p53 DNA responsive element. Antisense abrogation of BRCA1 expression abrogates upregulation of DDB2 after UVC or cisplatin exposure. Using a host cell reactivation assay, DNA repair activity is more significantly restored by introduction of BRCA1 into wt as compared to DDB2-deficient cells. Furthermore disappearance of the photoproducts cyclobutane pyrimidine dimer (CPD) and 6-4 photoproduct (6-4PP) was delayed by antisense abrogation of BRCA1 expression in UV-exposed human cells. Thus the D...
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BRCA1 Transcriptionally Regulates Damaged DNA Binding Protein (DDB2) In the DNA Repair Response Following UV-Irradiation
Cancer Biology & Therapy, 2002Co-Authors: Rishu Takimoto, Timothy K. Maclachlan, David T. Dicker, Yoshiro Niitsu, Toshio Mori, Wafik S. El-deiryAbstract:The p53 and BRCA1 tumor suppressors are involved in repair processes and may cooperate to transactivate certain genes, including p21WAF1/CIP1 and GADD45. We find that the Xeroderma Pigmentosum Complementation group E (XPE) mutated Damaged-DNA binding Protein p48 (DDB2) is upregulated by BRCA1 in a p53-dependent manner following UVC, Adriamycin, or Cisplatin exposure. BRCA1 enhances p53 binding to the DDB2 promoter in vivo as well as p53-dependent transactivation of DDB2 promoter-reporter constructs through a classical p53 DNA responsive element. Antisense abrogation of BRCA1 expression abrogates upregulation of DDB2 after UVC or cisplatin exposure. Using a host cell reactivation assay, DNA repair activity is more significantly restored by introduction of BRCA1 into wt as compared to DDB2-deficient cells. Furthermore disappearance of the photoproducts cyclobutane pyrimidine dimer (CPD) and 6-4 photoproduct (6-4PP) was delayed by antisense abrogation of BRCA1 expression in UV-exposed human cells. Thus the D...
Robert P. Perry - One of the best experts on this subject based on the ideXlab platform.
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A mammalian DNA-binding Protein that contains a chromodomain and an SNF2/SWI2-like helicase domain.
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: Véronique Delmas, David G. Stokes, Robert P. PerryAbstract:Abstract Two overlapping cDNAs that encode a 197-kDa sequence-selective DNA-binding Protein were isolated from libraries derived from mouse lymphoid cell mRNA. In addition to a DNA-binding domain, the Protein contains both a chromodomain, which occurs in Proteins that are implicated in chromatin compaction, and an SNF2/SWI2-like helicase domain, which occurs in Proteins that are believed to activate transcription by counteracting the repressive effects of chromatin structure. A Southern blot analysis indicated that this Protein, which we have named CHD-1, for chromodomain-helicase-DNA-binding Protein, is present in most, if not all, mammalian species. A Northern blot analysis revealed multiple CHD mRNA components that differed both qualitatively and quantitatively among various cell types. The various mRNAs, which are probably produced by alternative RNA processing, could conceivably encode tissue-specific and developmental stage-specific isoforms of the Protein. Based on its interesting combination of features, we suspect that CHD-1 plays an important role in gene regulation.
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a mammalian dna binding Protein that contains a chromodomain and an snf2 swi2 like helicase domain
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: Véronique Delmas, David G. Stokes, Robert P. PerryAbstract:Abstract Two overlapping cDNAs that encode a 197-kDa sequence-selective DNA-binding Protein were isolated from libraries derived from mouse lymphoid cell mRNA. In addition to a DNA-binding domain, the Protein contains both a chromodomain, which occurs in Proteins that are implicated in chromatin compaction, and an SNF2/SWI2-like helicase domain, which occurs in Proteins that are believed to activate transcription by counteracting the repressive effects of chromatin structure. A Southern blot analysis indicated that this Protein, which we have named CHD-1, for chromodomain-helicase-DNA-binding Protein, is present in most, if not all, mammalian species. A Northern blot analysis revealed multiple CHD mRNA components that differed both qualitatively and quantitatively among various cell types. The various mRNAs, which are probably produced by alternative RNA processing, could conceivably encode tissue-specific and developmental stage-specific isoforms of the Protein. Based on its interesting combination of features, we suspect that CHD-1 plays an important role in gene regulation.
Paul E. Boehmer - One of the best experts on this subject based on the ideXlab platform.
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The UL8 Subunit of the Herpes Simplex Virus Type-1 DNA Helicase-Primase Optimizes Utilization of DNA Templates Covered by the Homologous Single-strand DNA-binding Protein ICP8
The Journal of biological chemistry, 1996Co-Authors: Nicolas Gac, Giuseppe Villani, Jean Sébastien Hoffmann, Paul E. BoehmerAbstract:Abstract The herpes simplex virus type-1 DNA helicase-primase is a heterotrimer encoded by the UL5, UL8, and UL52 genes. The core enzyme, specified by the UL5 and UL52 genes, retains DNA helicase, DNA-dependent nucleoside triphosphatase, and primase activities. The UL8 subunit has previously been implicated in increasing primer stability and in stimulating primer synthesis by the core enzyme. To further characterize the function of the UL8 subunit, we have examined its effect on the activities of the UL5/52 core enzyme using DNA templates covered by the herpes simplex virus type-1 single-strand DNA-binding Protein ICP8. We found that while ICP8 stimulated the DNA helicase activity of the UL5/52 Proteins up to 3-fold, maximum stimulation by ICP8 required the presence of UL8 Protein. Moreover, UL8 Protein was required to reverse the inhibitory effect of ICP8 on the DNA-dependent ATPase and primase activities of the UL5/52 Proteins. These observations were specific for ICP8 since the heterologous Escherichia coli single-strand DNA-binding Protein could not substitute for ICP8. These data suggest that UL8 Protein mediates an interaction between the UL5/52 core enzyme and ICP8 that optimizes the utilization of ICP8-covered DNA templates during DNA replication.
John Q. Trojanowski - One of the best experts on this subject based on the ideXlab platform.
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tar dna binding Protein 43 in neurodegenerative disease
Nature Reviews Neurology, 2010Co-Authors: Alice Chenplotkin, John Q. TrojanowskiAbstract:In 2006, TAR DNA-binding Protein 43 (TDP-43), a highly conserved nuclear Protein, was identified as the major disease Protein in amyotrophic lateral sclerosis (ALS) and in the most common variant of frontotemporal lobar degeneration (FTLD), FTLD-U, which is characterized by cytoplasmic inclusions that stain positive for ubiquitin but negative for tau and α-synuclein. Since then, rapid advances have been made in our understanding of the physiological function of TDP-43 and the role of this Protein in neurodegeneration. These advances link ALS and FTLD-U (now designated FTLD-TDP) to a shared mechanism of disease. In this Review, we summarize the current evidence regarding the normal function of TDP-43 and the TDP-43 pathology observed in FTLD-TDP, ALS, and other neurodegenerative diseases wherein TDP-43 pathology co-occurs with other disease-specific lesions (for example, with amyloid plaques and neurofibrillary tangles in Alzheimer disease). Moreover, we discuss the accumulating data that support our view that FTLD-TDP and ALS represent two ends of a spectrum of primary TDP-43 Proteinopathies. Finally, we comment on the importance of recent advances in TDP-43-related research to neurological practice, including the new opportunities to develop better diagnostics and disease-modifying therapies for ALS, FTLD-TDP, and related disorders exhibiting TDP-43 pathology.
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concomitant tar dna binding Protein 43 pathology is present in alzheimer disease and corticobasal degeneration but not in other tauopathies
Journal of Neuropathology and Experimental Neurology, 2008Co-Authors: Kunihiro Uryu, Hanae Nakashimayasuda, Mark Forman, Linda K Kwong, Christopher M Clark, Murray Grossman, Hans A Kretzschmar, John Q. Trojanowski, Bruce L Miller, Manuela NeumannAbstract:Pathologic TAR-DNA-binding Protein 43 (TDP-43) is a disease Protein in frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U) and amyotrophic lateral sclerosis. We studied the presence, frequency, and distribution of TDP-43 pathology by immunohistochemistry and biochemistry in a series of clinically well-characterized tauopathy patient brains, including 182 Alzheimer disease (AD), 39 corticobasal degeneration, 77 progressive supranuclear palsy, and 12 Pick disease cases and investigated the clinical impact of concomitant TDP-43 pathology in these cases. TAR-DNA-binding Protein 43 pathology was found in 25.8% of AD cases. It was restricted to the dentate gyrus and entorhinal cortex in approximately 75% of cases; approximately 25% showed more widespread TDP-43 pathology in frontal and temporal cortices, resembling the FTLD-U subtype associated with progranulin mutations. TAR-DNA-binding Protein 43 pathology in AD was associated with significantly longer disease duration, but there was no association with the clinical presentation (148 cases diagnosed as AD and 34 cases diagnosed as frontotemporal lobar degeneration). Progressive supranuclear palsy and Pick disease cases showed no TDP-43 inclusions and no biochemical alterations of TDP-43. There was, however, a unique, predominantly glial TDP-43 pathology with staining of astrocytic plaque-like structures and coiled bodies in 15.4% of corticobasal degeneration cases; this was associated with biochemical TDP-43 changes similar to those in FTLD-U. These findings provide further insight into the burden and clinical significance of TDP-43 pathology in disorders other than FTLD-U and amyotrophic lateral sclerosis.