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  1. AU="Kurashige, Seiichiro"
  2. AU="Yoshiaki Yasumizu"
  3. AU=Arendt Lisa M.
  4. AU=BATTEN P J AU=BATTEN P J
  5. AU="Konieczny, S F"
  6. AU="Riches, Lucy"
  7. AU=Sozkes Sarkis AU=Sozkes Sarkis
  8. AU="Patrignelli, Robert"
  9. AU="Muzamil shah"
  10. AU="Bhat, Aishwarya"
  11. AU="Hossain, Md Zakir"
  12. AU=Jiang Xianhan
  13. AU="Mousavi, Seyyed Meysam"
  14. AU=Paulson J C
  15. AU="Saif, Tahir"
  16. AU=Alam Sabiha AU=Alam Sabiha
  17. AU="Braniff, Julia"
  18. AU="Kasim, Sazzli"
  19. AU=Brown Samuel M
  20. AU="Daubenberger, Claudia A."
  21. AU="Esteban, L"
  22. AU=Tyrka Audrey R.
  23. AU="Álvarez-Valenzuela, Francisco D"
  24. AU="Akrofi, M.M."
  25. AU="Torres, Daiana Rodrigues"
  26. AU="Bercovici, Nicholas"
  27. AU="Di Maio, Ginevra"
  28. AU="Indelicarto, Matthew"
  29. AU="Ma, Yan"
  30. AU="Ngan, CDR Kelly"
  31. AU="Arzamendi, Dabit"
  32. AU="Rezende, Carlos Eduardo Borges"
  33. AU="Brunvand, E."
  34. AU="Gateno, Jaime"

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  1. Artikel ; Online: Evaluation of circulating miR-216a and miR-217 as biomarkers of pancreatic damage in the L-arginine-induced acute pancreatitis mouse model.

    Kurashige, Seiichiro / Matsutani, Naomi / Aoki, Toyohiko / Kodama, Terutaka / Otagiri, Yasuteru / Togashi, Yuko

    The Journal of toxicological sciences

    2023  Band 48, Heft 10, Seite(n) 527–534

    Abstract: We investigated the usefulness of circulating miR-216a-5p and miR-217-5p that are pancreas-enriched micro RNAs (miRNAs) as biomarkers of acute pancreatic damage, and compared them with conventional pancreatic biomarkers in L-arginine-induced acute ... ...

    Abstract We investigated the usefulness of circulating miR-216a-5p and miR-217-5p that are pancreas-enriched micro RNAs (miRNAs) as biomarkers of acute pancreatic damage, and compared them with conventional pancreatic biomarkers in L-arginine-induced acute pancreatitis mouse model. As the results, amylase and lipase levels apparently increased and peaked on Day 3 when acute pancreatitis including acinar cell degeneration/necrosis and inflammatory cell infiltration reached its peak. In contrast, miR-216a-5p and miR-217-5p increased from Day 1 when histopathological findings in the acinar cells were limited to decreased zymogen granules, and the increases in ratios were much higher than those of amylase and lipase. The miRNAs remained at high levels until Day 5 when the pseudo-tubular complex and replacement of inflammatory cells and fibrotic cells were apparent instead of necrosis, whereas amylase and lipase levels decreased to the control levels. Furthermore, we examined the relationship between biomarker levels and histopathological degeneration/necrosis scores in the acinar cells. miR-216a-5p and miR-217-5p levels increased depending on the score of degeneration/necrosis, and all individual miRNAs exceeded the control levels from a score of 2 (focal necrosis), whereas all individual amylase and lipase levels exceeded the control levels at scores of 4 (lobular necrosis) and 3 (sublobular necrosis), respectively. In conclusion, we demonstrated that circulating miR-216a-5p and miR-217-5p could detect pancreatic damage earlier with greater magnitude, and the sensitivity to detect acinar cell degeneration/necrosis was superior to that of conventional biomarkers in the L-arginine-induced acute pancreatitis mouse model.
    Mesh-Begriff(e) Mice ; Animals ; Pancreatitis/chemically induced ; Pancreatitis/diagnosis ; Pancreatitis/pathology ; Acute Disease ; Pancreas/pathology ; MicroRNAs ; Necrosis/pathology ; Biomarkers ; Disease Models, Animal ; Arginine/toxicity ; Amylases/toxicity ; Lipase/genetics ; Lipase/toxicity
    Chemische Substanzen MicroRNAs ; Biomarkers ; Arginine (94ZLA3W45F) ; Amylases (EC 3.2.1.-) ; Lipase (EC 3.1.1.3)
    Sprache Englisch
    Erscheinungsdatum 2023-09-16
    Erscheinungsland Japan
    Dokumenttyp Journal Article
    ZDB-ID 770623-6
    ISSN 1880-3989 ; 0388-1350
    ISSN (online) 1880-3989
    ISSN 0388-1350
    DOI 10.2131/jts.48.527
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: SLX4-XPF mediates DNA damage responses to replication stress induced by DNA-protein interactions.

    Ishimoto, Riko / Tsuzuki, Yota / Matsumura, Tomoki / Kurashige, Seiichiro / Enokitani, Kouki / Narimatsu, Koki / Higa, Mitsunori / Sugimoto, Nozomi / Yoshida, Kazumasa / Fujita, Masatoshi

    The Journal of cell biology

    2020  Band 220, Heft 1

    Abstract: The DNA damage response (DDR) has a critical role in the maintenance of genomic integrity during chromosome replication. However, responses to replication stress evoked by tight DNA-protein complexes have not been fully elucidated. Here, we used ... ...

    Abstract The DNA damage response (DDR) has a critical role in the maintenance of genomic integrity during chromosome replication. However, responses to replication stress evoked by tight DNA-protein complexes have not been fully elucidated. Here, we used bacterial LacI protein binding to lacO arrays to make site-specific replication fork barriers on the human chromosome. These barriers induced the accumulation of single-stranded DNA (ssDNA) and various DDR proteins at the lacO site. SLX4-XPF functioned as an upstream factor for the accumulation of DDR proteins, and consequently, ATR and FANCD2 were interdependently recruited. Moreover, LacI binding in S phase caused underreplication and abnormal mitotic segregation of the lacO arrays. Finally, we show that the SLX4-ATR axis represses the anaphase abnormality induced by LacI binding. Our results outline a long-term process by which human cells manage nucleoprotein obstacles ahead of the replication fork to prevent chromosomal instability.
    Mesh-Begriff(e) Anaphase ; Ataxia Telangiectasia Mutated Proteins/metabolism ; Cell Line, Tumor ; Chromosome Segregation ; Chromosomes, Human/metabolism ; DNA/metabolism ; DNA Damage ; DNA Replication ; DNA-Binding Proteins/metabolism ; Fanconi Anemia Complementation Group D2 Protein/metabolism ; Humans ; Models, Biological ; Protein Binding ; Recombinases/metabolism ; S Phase ; Stress, Physiological
    Chemische Substanzen DNA-Binding Proteins ; Fanconi Anemia Complementation Group D2 Protein ; Recombinases ; xeroderma pigmentosum group F protein ; DNA (9007-49-2) ; ATR protein, human (EC 2.7.11.1) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; SLX4 protein, human (EC 3.1.-)
    Sprache Englisch
    Erscheinungsdatum 2020-12-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202003148
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: TRF2 recruits ORC through TRFH domain dimerization.

    Higa, Mitsunori / Kushiyama, Tatsunori / Kurashige, Seiichiro / Kohmon, Daisuke / Enokitani, Kouki / Iwahori, Satoko / Sugimoto, Nozomi / Yoshida, Kazumasa / Fujita, Masatoshi

    Biochimica et biophysica acta. Molecular cell research

    2016  Band 1864, Heft 1, Seite(n) 191–201

    Abstract: Telomeres are specialized chromatin structures that prevent the degradation and instability of the ends of linear chromosomes. While telomerase maintains long stretches of the telomeric repeat, the majority of telomeric DNA is duplicated by conventional ... ...

    Abstract Telomeres are specialized chromatin structures that prevent the degradation and instability of the ends of linear chromosomes. While telomerase maintains long stretches of the telomeric repeat, the majority of telomeric DNA is duplicated by conventional DNA replication. A fundamental step in eukaryotic DNA replication involves chromatin binding of the origin recognition complex (ORC). In human cells, telomeric repeat binding factor 2 (TRF2) is thought to play a role in the recruitment of ORC onto telomeres. To better understand the mechanism of TRF2-mediated ORC recruitment, we utilized a lacO-LacI protein tethering system in U2OS cells and found that ectopically targeted TRF2, but not TRF1, can recruit ORC onto the lacO array. We further found that the TRF homology (TRFH) dimerization domain of TRF2, but not its mutant defective in dimerization, is sufficient for ORC and minichromosome maintenance (MCM) recruitment. Mutations impairing the dimerization also compromised ORC recruitment by full-length TRF2. Similar results were obtained using immunoprecipitation and GST pull-down assays. Together, these results suggest that dimerized TRF2 recruits ORC and stimulates pre-replication complex (pre-RC) formation at telomeres through the TRFH domain.
    Mesh-Begriff(e) Cell Line, Tumor ; Chromatin/chemistry ; Chromatin/metabolism ; DNA Replication ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Expression ; HEK293 Cells ; HeLa Cells ; Humans ; Lac Repressors/genetics ; Lac Repressors/metabolism ; Minichromosome Maintenance Proteins/genetics ; Minichromosome Maintenance Proteins/metabolism ; Mutation ; Origin Recognition Complex/genetics ; Origin Recognition Complex/metabolism ; Osteoblasts/cytology ; Osteoblasts/metabolism ; Protein Domains ; Protein Multimerization ; Signal Transduction ; Telomere/metabolism ; Telomere/ultrastructure ; Telomeric Repeat Binding Protein 1/genetics ; Telomeric Repeat Binding Protein 1/metabolism ; Telomeric Repeat Binding Protein 2/chemistry ; Telomeric Repeat Binding Protein 2/genetics ; Telomeric Repeat Binding Protein 2/metabolism
    Chemische Substanzen Chromatin ; Escherichia coli Proteins ; Lac Repressors ; LacI protein, E coli ; Origin Recognition Complex ; TERF2 protein, human ; Telomeric Repeat Binding Protein 1 ; Telomeric Repeat Binding Protein 2 ; Minichromosome Maintenance Proteins (EC 3.6.4.12)
    Sprache Englisch
    Erscheinungsdatum 2016-11-09
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2016.11.004
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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