Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters











Database
Type of study
Language
Publication year range
1.
FEBS Open Bio ; 13(4): 655-669, 2023 04.
Article in English | MEDLINE | ID: mdl-36734593

ABSTRACT

Ovarian cancer is characterized by a high degree of genetic heterogeneity. Platinum-based chemotherapy and some gene-targeted therapies have shown limited treatment efficacy due to toxicity and recurrence, and thus, it is essential to identify additional therapeutic targets based on an understanding of the pathological mechanism. Here, we report that endonuclease G, which exhibits altered expression in ovarian cancer, does not function as a cell death effector that digests chromosomal DNA in ovarian cancer. Endonuclease G is modulated by intracellular reactive oxygen species dynamics and plays a role in cell proliferation in ovarian cancer, suggesting that targeting endonuclease G alone or in combination with other antitumor agents may have the potential for development into a treatment for endonuclease G-overexpressing cancers, including ovarian cancer.


Subject(s)
Antineoplastic Agents , Ovarian Neoplasms , Humans , Female , Ovarian Neoplasms/drug therapy , Ovarian Neoplasms/genetics , Ovarian Neoplasms/pathology , Antineoplastic Agents/pharmacology , Antineoplastic Agents/therapeutic use , Endodeoxyribonucleases , Cell Proliferation/genetics
2.
Biochem Biophys Res Commun ; 530(2): 440-447, 2020 09 17.
Article in English | MEDLINE | ID: mdl-32553630

ABSTRACT

C-terminal binding protein 2 (CtBP2) is a transcriptional co-repressor that regulates many genes involved in normal cellular events. Because CtBP2 overexpression has been implicated in various human cancers, its protein levels must be precisely regulated. Previously, we reported that CtBP1 and CtBP1-mediated transcriptional repression are regulated by X-linked inhibitor of apoptosis protein (XIAP). In the present study, we sought to investigate whether CtBP2 is also regulated by XIAP or any other human IAP. We found that cIAP1 interacts with CtBP2 via through BIR domains to regulates the steady-state levels of CtBP2 protein in the nucleus. The levels of CtBP2 were gradually increased upon cIAP1 overexpression and downregulated upon cIAP1 depletion. Interestingly, the RING domain of cIAP1 responsible for E3 ligase activity was not required for this regulation. Finally, the levels of CtBP2 modulated by cIAP1 affected the transcription of CtBP2 target genes and subsequent cell migration. Taken together, our data demonstrate a novel function of cIAP1 which involves protecting CtBP2 from degradation to stabilize its steady-state level. These results suggest that cIAP1 might be a useful target in strategies aiming to downregulate the steady-state level of CtBP2 protein in treating human cancers.


Subject(s)
Alcohol Oxidoreductases/metabolism , Co-Repressor Proteins/metabolism , Inhibitor of Apoptosis Proteins/metabolism , Alcohol Oxidoreductases/chemistry , Cell Line, Tumor , Co-Repressor Proteins/chemistry , HeLa Cells , Humans , Inhibitor of Apoptosis Proteins/chemistry , Neoplasms/metabolism , Protein Interaction Domains and Motifs , Protein Interaction Maps , Ubiquitin-Protein Ligases/chemistry , Ubiquitin-Protein Ligases/metabolism
3.
Virology ; 534: 25-35, 2019 08.
Article in English | MEDLINE | ID: mdl-31170545

ABSTRACT

Three ourmia-like viruses, designated Pyricularia oryzae ourmia-like virus (PoOLV) 1 to 3, were identified in a wheat-infecting isolate of P. oryzae. The sizes of the full-length PoOLV1-3 genomes were determined to be 2,528, 1,671, and 2,557 nt. Interestingly, we also found two abundant single-stranded RNAs sharing their 5' terminal 25 and 255 nt with PoOLV1 RNA and PoOLV3 RNA, respectively. The PoOLV1- and PoOLV3-associated RNAs (ARNA1 and ARNA3) were 639 and 514 nt in length, and possessed one and two small ORFs, respectively. In the field isolates of P. oryzae, PoOLVs and ARNAs were detectable at varying levels, and the levels of PoOLV1 and ARNA1 as well as those of PoOLV3 and ARNA3, were tightly correlated. In addition, gene silencing of PoOLV1 and PoOLV3 resulted in a reduction of ARNA1 and ARNA3, respectively. There results indicated that replication of ARNA1 and ARNA3 was associated with PoOLV1 and PoOLV3, respectively.


Subject(s)
Ascomycota/virology , Fungal Viruses/isolation & purification , Plant Diseases/microbiology , RNA, Viral/metabolism , Fungal Viruses/classification , Fungal Viruses/genetics , Genome, Viral , Open Reading Frames , Phylogeny , RNA, Viral/genetics , Triticum/microbiology , Viral Proteins/genetics , Viral Proteins/metabolism
4.
Appl Opt ; 57(12): 3180-3185, 2018 Apr 20.
Article in English | MEDLINE | ID: mdl-29714303

ABSTRACT

This study demonstrates the optical manipulation of colloids dispersed in azo-dye-doped liquid crystals (DDLCs) where the accumulation occurs at the interfaces of the phase domains. We explain the mechanism related to the formation of the domains and the movement of the colloids in DDLCs with respect to the isomerization of azo-dye molecules via the illumination of laser beams. The colloids are dragged to the interfaces of the isotropic/nematic domain and the air bubble/isotropic domain by molecular interaction and Marangoni flows.

5.
Chem Commun (Camb) ; (38): 3924-6, 2007 Oct 14.
Article in English | MEDLINE | ID: mdl-17896034

ABSTRACT

The reaction of the triosmium cluster anion, [Os(3)(micro-H)(CO)(11)][PPN] (PPN = [N(PPh(3))2]+), with [AgPF(6)] in the presence of [Ir(PPh(3))2(CO)Cl] in THF at room temperature affords two new high-nuclearity osmium-silver clusters, [Os(13)Ag(9)(CO)48][PPN] (1) and [Os(9)Ag(9)(micro3-O)2(CO)30][PPN] (2), and an iridium complex, [Ir(PPh(3))2(CO)Cl(O(2))] (3).

SELECTION OF CITATIONS
SEARCH DETAIL