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26 results on '"Daigo, Kenji"'

5. Frequent Germline and Somatic Single Nucleotide Variants in the Promoter Region of the Ribosomal RNA Gene in Japanese Lung Adenocarcinoma Patients

Author

Ohashi, Riuko, primary, Umezu, Hajime, additional, Sato, Ayako, additional, Abé, Tatsuya, additional, Kondo, Shuhei, additional, Daigo, Kenji, additional, Sato, Seijiro, additional, Hara, Norikazu, additional, Miyashita, Akinori, additional, Ikeuchi, Takeshi, additional, Motoyama, Teiichi, additional, Kishi, Masashi, additional, Nagaoka, Tadahiro, additional, Horiuchi, Keiko, additional, Shiga, Atsushi, additional, Okuda, Shujiro, additional, Sekiya, Tomoki, additional, Ohtsubo, Aya, additional, Ichikawa, Kosuke, additional, Kagamu, Hiroshi, additional, Kikuchi, Toshiaki, additional, Watanabe, Satoshi, additional, Tanuma, Jun-Ichi, additional, Schraml, Peter, additional, Hamakubo, Takao, additional, Tsuchida, Masanori, additional, and Ajioka, Yoichi, additional

Published
2020
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7. Lineage-Specific Epigenomic and Genomic Activation of Oncogene HNF4A Promotes Gastrointestinal Adenocarcinomas

Author

Pan, Jian, primary, Silva, Tiago C., additional, Gull, Nicole, additional, Yang, Qian, additional, Plummer, Jasmine T., additional, Chen, Stephanie, additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Gery, Sigal, additional, Ding, Ling-Wen, additional, Jiang, Yan-Yi, additional, Hu, Shaoyan, additional, Xu, Li-Yan, additional, Li, En-Min, additional, Ding, Yanbing, additional, Klempner, Samuel J., additional, Gayther, Simon A., additional, Berman, Benjamin P., additional, Koeffler, H. Phillip, additional, and Lin, De-Chen, additional

Published
2020
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8. Lineage-Specific Epigenomic and Genomic Activation of the Oncogene HNF4A Promotes Gastrointestinal Adenocarcinomas

Author

Pan, Jian, primary, Silva, Tiago C., additional, Gull, Nicole, additional, Yang, Qian, additional, Plummer, Jasmine, additional, Chen, Stephanie, additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Gery, Sigal, additional, Ding, Ling-Wen, additional, Jiang, Yan-Yi, additional, Hu, Shao-Yan, additional, Xu, Li-Yan, additional, Li, En-Min, additional, Ding, Yanbing, additional, Klempner, Samuel J., additional, Berman, Benjamin P., additional, Phillip Koeffler, H., additional, and Lin, De-Chen, additional

Published
2019
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13. Factor H–Related Protein 5 Interacts with Pentraxin 3 and the Extracellular Matrix and Modulates Complement Activation

Author

Csincsi, Ádám I., primary, Kopp, Anne, additional, Zöldi, Miklós, additional, Bánlaki, Zsófia, additional, Uzonyi, Barbara, additional, Hebecker, Mario, additional, Caesar, Joseph J. E., additional, Pickering, Matthew C., additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Lea, Susan M., additional, Goicoechea de Jorge, Elena, additional, and Józsi, Mihály, additional

Published
2015
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14. Protective effect of the long pentraxin PTX3 against histone-mediated endothelial cell cytotoxicity in sepsis

Author

Daigo, Kenji, primary, Nakakido, Makoto, additional, Ohashi, Riuko, additional, Fukuda, Rie, additional, Matsubara, Koichi, additional, Minami, Takashi, additional, Yamaguchi, Naotaka, additional, Inoue, Kenji, additional, Jiang, Shuying, additional, Naito, Makoto, additional, Tsumoto, Kouhei, additional, and Hamakubo, Takao, additional

Published
2014
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16. Proteomic analysis of native hepatocyte nuclear factor-4α (HNF4α) isoforms, phosphorylation status, and interactive cofactors.

Author

Daigo, Kenji, primary, Kawamura, Takeshi, additional, Ohta, Yoshihiro, additional, Ohashi, Riuko, additional, Katayose, Satoshi, additional, Tanaka, Toshiya, additional, Aburatani, Hiroyuki, additional, Naito, Makoto, additional, Kodama, Tatsuhiko, additional, Ihara, Sigeo, additional, and Hamakubo, Takao, additional

Published
2013
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17. The Proteomic Profile of Circulating Pentraxin 3 (PTX3) Complex in Sepsis Demonstrates the Interaction with Azurocidin 1 and Other Components of Neutrophil Extracellular Traps

Author

Daigo, Kenji, primary, Yamaguchi, Naotaka, additional, Kawamura, Takeshi, additional, Matsubara, Koichi, additional, Jiang, Shuying, additional, Ohashi, Riuko, additional, Sudou, Yukio, additional, Kodama, Tatsuhiko, additional, Naito, Makoto, additional, Inoue, Kenji, additional, and Hamakubo, Takao, additional

Published
2012
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19. Proteomic Analysis of Native Hepatocyte Nuclear Factor-4α (HNF4α) Isoforms, Phosphorylation Status, and Interactive Cofactors

Author

Daigo, Kenji, primary, Kawamura, Takeshi, additional, Ohta, Yoshihiro, additional, Ohashi, Riuko, additional, Katayose, Satoshi, additional, Tanaka, Toshiya, additional, Aburatani, Hiroyuki, additional, Naito, Makoto, additional, Kodama, Tatsuhiko, additional, Ihara, Sigeo, additional, and Hamakubo, Takao, additional

Published
2011
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21. Hepatocyte Nuclear Factor 4α Contributes to Thyroid Hormone Homeostasis by Cooperatively Regulating the Type 1 Iodothyronine Deiodinase Gene with GATA4 and Krüppel-Like Transcription Factor 9

Author

Ohguchi, Hiroto, primary, Tanaka, Toshiya, additional, Uchida, Aoi, additional, Magoori, Kenta, additional, Kudo, Hiromi, additional, Kim, Insook, additional, Daigo, Kenji, additional, Sakakibara, Iori, additional, Okamura, Masashi, additional, Harigae, Hideo, additional, Sasaki, Takeshi, additional, Osborne, Timothy F., additional, Gonzalez, Frank J., additional, Hamakubo, Takao, additional, Kodama, Tatsuhiko, additional, and Sakai, Juro, additional

Published
2008
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22. Cooperative Interaction between Hepatocyte Nuclear Factor 4α and GATA Transcription Factors Regulates ATP-Binding Cassette Sterol Transporters ABCG5 and ABCG8

Author

Sumi, Koichi, primary, Tanaka, Toshiya, additional, Uchida, Aoi, additional, Magoori, Kenta, additional, Urashima, Yasuyo, additional, Ohashi, Riuko, additional, Ohguchi, Hiroto, additional, Okamura, Masashi, additional, Kudo, Hiromi, additional, Daigo, Kenji, additional, Maejima, Takashi, additional, Kojima, Noriaki, additional, Sakakibara, Iori, additional, Jiang, Shuying, additional, Hasegawa, Go, additional, Kim, Insook, additional, Osborne, Timothy F., additional, Naito, Makoto, additional, Gonzalez, Frank J., additional, Hamakubo, Takao, additional, Kodama, Tatsuhiko, additional, and Sakai, Juro, additional

Published
2007
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24. Activation of Leukemia-associated RhoGEF by Gα13 with Significant Conformational Rearrangements in the Interface.

Author

Suzuki, Nobuchika, Tsumot, Kouhei, Hajicek, Nicole, Daigo, Kenji, Tokita, Reiko, Minami, Shiro, Kodama, Tatsuhiko, Hamakubo, Takao, and Kozasa, Tohru

Subjects
*G proteins, *SURFACE plasmon resonance, *CELLULAR control mechanisms, *THERMODYNAMICS, *ENTROPY, *PROTEIN-protein interactions, *LEUKEMIA, *ALANINE
Abstract

The transient protein-protein interactions induced by guanine nucleotide-dependent conformational changes of G proteins play central roles in G protein-coupled receptor-mediated signaling systems. Leukemia-associated RhoGEF (LARG), a guanine nucleotide exchange factor for Rho, contains an RGS homology (RH) domain and Dbl homology! pleckstrin homology (DH/PH) domains and acts both as a GTPase-activating protein (GAP) and an effector for Ga[sub13]. However, the molecular mechanism of LARG activation upon Ga[sub13] binding is not yet well understood. In this study, we analyzed the Ga[sub13]-LARG interaction using cellular and biochemical methods, including a surface plasmon resonance (SPR) analysis. The results obtained using various LARG fragments demonstrated that active Ga[sub13] interacts with LARG through the RH domain, DH/PH domains, and C-terminal region. However, an alanine substitution at the RH domain contact position in Ga[sub13] resulted in a large decrease in affinity. Thermodynamic analysis revealed that binding of Ga[sub13] proceeds with a large negative heat capacity change (ΔCp°°), accompanied by a positive entropy change (ΔS°), These results likely indicate that the binding of Ga[sub13] with the RH domain triggers conformational rearrangements between Ga[sub13] and LARG burying an exposed hydrophobic surface to create a large complementary interface, which facilitates complex formation through both GAP and effector interfaces, and activates the RhoGEF. We propose that LARG activation is regulated by an induced-fit mechanism through the GAP interface of Ga[sub13]. [ABSTRACT FROM AUTHOR]

Published
2009
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25. Expression and Purification of Full-Length and Domain-Fragment Recombinant Pentraxin 3 (PTX3) Proteins from Mammalian and Bacterial Cells.

Author

Daigo K and Hamakubo T

Subjects
Animals, Arginine chemistry, Buffers, C-Reactive Protein metabolism, CHO Cells, Cricetulus, Escherichia coli genetics, Humans, Protein Domains, Serum Amyloid P-Component metabolism, C-Reactive Protein genetics, Escherichia coli growth & development, Protein Engineering methods, Recombinant Proteins isolation & purification, Serum Amyloid P-Component genetics
Abstract

Although cell-based protein expression systems enable us a certain amount of protein suitable for subsequent biological experiments to be obtained, aggregates of the protein of interest are sometimes encountered during the purification procedure. Pentraxin 3 (PTX3), a member of the pentraxin family that is classified as a carbohydrate-binding protein based on its structure, comprises one of the humoral arms of the pattern recognition receptors that play an important role in the innate immune response. PTX3 comprises two domains; an N-terminal domain and a C-terminal domain. The C-terminal domain containing pentraxin signature has similar biological functions as other pentraxins such as C-reactive protein (CRP) and serum amyloid-P component (SAP). On the other side, the N-terminal domain is specific to PTX3. A supply of the PTX3 protein in full length or partial fragments is thus essential for the elucidation of its biological functions. Here we describe the expression and purification of recombinant PTX3. An arginine-containing buffer is essential for the elution of bacterially expressed PTX3 N-terminal domain to minimize aggregation. This method allows high-yield purification of full-length or domain-fragment recombinant PTX3 proteins for biological study.

Published
2020
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26. Cooperative interaction between hepatocyte nuclear factor 4 alpha and GATA transcription factors regulates ATP-binding cassette sterol transporters ABCG5 and ABCG8.

Author

Sumi K, Tanaka T, Uchida A, Magoori K, Urashima Y, Ohashi R, Ohguchi H, Okamura M, Kudo H, Daigo K, Maejima T, Kojima N, Sakakibara I, Jiang S, Hasegawa G, Kim I, Osborne TF, Naito M, Gonzalez FJ, Hamakubo T, Kodama T, and Sakai J

Subjects
ATP Binding Cassette Transporter, Subfamily G, Member 5, ATP Binding Cassette Transporter, Subfamily G, Member 8, ATP-Binding Cassette Transporters genetics, Adenoviridae genetics, Amino Acid Motifs, Amino Acid Sequence, Base Sequence, Binding Sites, Carcinoma, Hepatocellular metabolism, Carcinoma, Hepatocellular pathology, Cell Line, Cell Line, Tumor, Consensus Sequence, Conserved Sequence, GATA4 Transcription Factor genetics, GATA6 Transcription Factor genetics, Gene Deletion, Genes, Reporter, Hepatocyte Nuclear Factor 4 chemistry, Humans, Lipoproteins genetics, Liver Neoplasms metabolism, Liver Neoplasms pathology, Luciferases metabolism, Molecular Sequence Data, Oligonucleotide Array Sequence Analysis, Promoter Regions, Genetic, Protein Binding, Protein Structure, Tertiary, RNA Interference, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, ATP-Binding Cassette Transporters metabolism, GATA4 Transcription Factor metabolism, GATA6 Transcription Factor metabolism, Hepatocyte Nuclear Factor 4 metabolism, Lipoproteins metabolism
Abstract

Cholesterol homeostasis is maintained by coordinate regulation of cholesterol synthesis and its conversion to bile acids in the liver. The excretion of cholesterol from liver and intestine is regulated by ATP-binding cassette half-transporters ABCG5 and ABCG8. The genes for these two proteins are closely linked and divergently transcribed from a common intergenic promoter region. Here, we identified a binding site for hepatocyte nuclear factor 4alpha (HNF4alpha) in the ABCG5/ABCG8 intergenic promoter, through which HNF4alpha strongly activated the expression of a reporter gene in both directions. The HNF4alpha-responsive element is flanked by two conserved GATA boxes that were also required for stimulation by HNF4alpha. GATA4 and GATA6 bind to the GATA boxes, coexpression of GATA4 and HNF4alpha leads to a striking synergistic activation of both the ABCG5 and the ABCG8 promoters, and binding sites for HNF4alpha and GATA were essential for maximal synergism. We also show that HNF4alpha, GATA4, and GATA6 colocalize in the nuclei of HepG2 cells and that a physical interaction between HNF4alpha and GATA4 is critical for the synergistic response. This is the first demonstration that HNF4alpha acts synergistically with GATA factors to activate gene expression in a bidirectional fashion.

Published
2007
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