11 results on '"FUkumoto, H."'
Search Results
2. Effects of oral glucose administration on preproinsulin mRNA in rats in vivo
- Author
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Fukumoto, H., primary, Seino, Y., additional, Koh, G., additional, Takeda, J., additional, Tsuji, K., additional, Kurose, T., additional, Kitano, N., additional, Tsuda, K., additional, Taminato, T., additional, and Imura, H., additional
- Published
- 1986
- Full Text
- View/download PDF
3. Fumagillin, a potent angiogenesis inhibitor, induces Kaposi sarcoma-associated herpesvirus replication in primary effusion lymphoma cells.
- Author
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Kanno T, Uehara T, Osawa M, Fukumoto H, Mine S, Ueda K, Hasegawa H, and Katano H
- Subjects
- Cell Division drug effects, Cell Line, Tumor, Herpesvirus 8, Human genetics, Humans, Lymphoma pathology, RNA, Messenger genetics, Sesquiterpenes pharmacology, Angiogenesis Inhibitors pharmacology, Cyclohexanes pharmacology, Fatty Acids, Unsaturated pharmacology, Herpesvirus 8, Human physiology, Lymphoma virology, Virus Replication drug effects
- Abstract
Kaposi sarcoma and primary effusion lymphoma cells are infected with Kaposi sarcoma-associated herpesvirus (KSHV), predominantly in the latent form, and KSHV replication is observed rarely. Angiogenesis plays a crucial role in the pathogenesis of both Kaposi sarcoma and primary effusion lymphoma. In this study, we found that fumagillin, a potent angiogenesis inhibitor, induced replication of KSHV in primary effusion lymphoma cell lines. The transcript and protein product of replication transcriptional activator (RTA) were induced by 1-10 μM fumagillin at 24 and 48 h, respectively. Western blot analysis demonstrated that 10 μM fumagillin induced not only RTA expression but also other KSHV-encoded lytic proteins. A real-time PCR array detecting KSHV gene expression demonstrated that the expression profiles of KSHV induced by fumagillin were similar to those induced by 12-O-tetradecanoylphorbol-13-acetate (TPA), but the amounts of each transcript were lower than those induced by TPA. Finally, real-time PCR demonstrated an increase in that viral DNA copy number per cell in fumagillin-stimulated primary effusion lymphoma cell lines, indicating replication of KSHV. In addition to TPA, 10 μM fumagillin resulted in growth inhibition of primary effusion lymphoma cell lines. These observations suggest that an angiogenesis inhibitor is an agent with potent effects on cell growth and KSHV reactivation in primary effusion lymphoma cells., (Copyright © 2015 Elsevier Inc. All rights reserved.)
- Published
- 2015
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4. PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone.
- Author
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Toyama H, Fukumoto H, Saeki M, Matsushita K, Adachi O, and Lidstrom ME
- Subjects
- Bacterial Proteins chemistry, Bacterial Proteins genetics, Dose-Response Relationship, Drug, Escherichia coli genetics, Kinetics, NADP pharmacology, PQQ Cofactor, Protein Structure, Tertiary, Sequence Deletion, Bacterial Proteins metabolism, Methylobacterium extorquens enzymology, Quinolones metabolism, Quinones metabolism
- Abstract
PqqC/D was purified from Escherichia coli transformant. The purified enzyme converted an intermediate that accumulated in a pqqC mutant of Methylobacterium extorquens AM1 to PQQ. The reaction did not show any dependence of NAD(P)H that was observed in the crude extract before purification. PqqC/D reacted with the intermediate stoichiometrically, but not catalytically. When partially purified proteins from the crude extract of E. coli were added to the reaction mixture, the rate of PQQ production increased dependent on the amount of NADPH added and the total amount of PQQ produced increased.
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- 2002
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5. Proximal 5'-flanking sequence of the human gamma-glutamylcysteine synthetase heavy subunit gene is involved in cisplatin-induced transcriptional up-regulation in a lung cancer cell line SBC-3.
- Author
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Tomonari A, Nishio K, Kurokawa H, Fukumoto H, Fukuoka K, Iwamoto Y, Usuda J, Suzuki T, Itakura M, and Saijo N
- Subjects
- Base Sequence, DNA chemistry, Human Growth Hormone genetics, Humans, Molecular Sequence Data, Promoter Regions, Genetic, Thymidine Kinase genetics, Transcription, Genetic drug effects, Transfection, Tumor Cells, Cultured, Antineoplastic Agents pharmacology, Carcinoma, Small Cell metabolism, Cisplatin pharmacology, Gene Expression Regulation, Neoplastic drug effects, Glutamate-Cysteine Ligase genetics, Lung Neoplasms metabolism
- Abstract
The contribution of the 5'-flanking sequence of the human gamma-glutamylcysteine synthetase heavy subunit (gamma-GCSh) gene to cisplatin-induced transcriptional up-regulation was studied using various human growth hormone reporter constructs which were transfected to a human lung cancer cell line SBC-3. Cisplatin at the concentration of 3 microM increased the transcriptional activity of the longest sequence from -1,413 to +91 bp of the gamma-GCSh gene to 246% of that in non-exposed cells. The distal sequence from -1,413 to -193 bp was shown to negatively regulate transcriptional activity in both cisplatin-exposed and non-exposed cells using deletion and thymidine kinase (TK) promoter-linked constructs. Cisplatin increased the transcriptional activity of the proximal GC-rich sequence from -192 to +91 bp to 340%, of which magnitude was the maximum among deletion constructs. A deletion from -108 to -28 bp, or +34 to +91 bp significantly decreased cisplatin-induced increases in transcriptional activity from 258 to 105%, or 340 to 160%, respectively. When the sequence from -108 to -22 bp, or +26 to +91 bp was linked to the heterologous TK promoter, cisplatin increased the transcriptional activity to 171 or 181%, respectively, from that of 128 or 137%, respectively, in non-exposed cells. These findings indicate that the proximal sequence from -192 to +91 bp of the gamma-GCSh gene, especially from -108 to -28 bp, and +34 to +91 bp, is involved in cisplatin-induced transcriptional up-regulation in SBC-3 cells.
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- 1997
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6. Identification of cis-acting DNA elements of the human gamma-glutamylcysteine synthetase heavy subunit gene.
- Author
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Tomonari A, Nishio K, Kurokawa H, Arioka H, Ishida T, Fukumoto H, Fukuoka K, Nomoto T, Iwamoto Y, Heike Y, Itakura M, and Saijo N
- Subjects
- Base Composition, Base Sequence, Humans, Molecular Sequence Data, Sequence Analysis, DNA, Sequence Deletion, Transcription Factor AP-1 genetics, Transcription, Genetic, Genes, Glutamate-Cysteine Ligase genetics, Regulatory Sequences, Nucleic Acid
- Abstract
Transcriptional activity of the 5'-flanking sequence of the human gamma-glutamylcysteine synthetase heavy subunit (gamma-GCSh) gene was investigated in COS7 cells transfected with hGH reporter constructs having successively deleted 5'-flanking sequence of the gamma-GCSh gene. Transcriptional activity was determined by the amounts of hGH secreted from the reporter constructs. Deletion of the sequence from -1,413 to -664 or -315 base pairs (bp) increased transcriptional activity from 100 to 138 or 136%. Further deletion from -315 to -241 bp, which contained an AP1 site, decreased transcriptional activity to 87%. Mutations introduced into the AP1 decreased transcriptional activity from 136 to 105%. These findings suggested that the AP1 increased transcriptional activity. When the sequence from -241 to -192 bp was deleted, transcriptional activity was restored from 87 to 128%. When this sequence was linked to the thymidine kinase promoter, it also decreased transcriptional activity by 38%. Deletion from -192 to -149, -116, or -108 bp did not significantly alter transcriptional activity. Further deletion of the GC-rich sequences from -108 to -70 and -28 bp dramatically decreased transcriptional activity from 135 to 87 and 34%, respectively. These findings indicate that multiple DNA elements, especially those in the proximal GC-rich sequences, are involved in the regulation of transcriptional activity of the gamma-GCSh gene.
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- 1997
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7. Gamma-glutamylcysteine synthetase gene overexpression results in increased activity of the ATP-dependent glutathione S-conjugate export pump and cisplatin resistance.
- Author
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Kurokawa H, Ishida T, Nishio K, Arioka H, Sata M, Fukumoto H, Miura M, and Saijo N
- Subjects
- Adenosine Triphosphate metabolism, Base Sequence, Carcinoma, Small Cell, Carrier Proteins biosynthesis, Cell Division drug effects, Cell Line, Cell Membrane metabolism, Cisplatin metabolism, Gene Library, Humans, Kinetics, Leukotriene C4 metabolism, Lung Neoplasms, Membrane Transport Proteins, Molecular Sequence Data, Recombinant Proteins biosynthesis, Thymus Gland metabolism, Transfection, Tumor Cells, Cultured, Carrier Proteins metabolism, Cisplatin toxicity, Drug Resistance, Neoplasm, Gene Expression, Glutamate-Cysteine Ligase biosynthesis, Glutathione metabolism
- Abstract
The ATP-dependent glutathione S-conjugate export pump (GS-X pump) has been suggested to play a role in the mechanism of cisplatin resistance. The purpose of this study was to determine the relationship between intracellular glutathione (GSH) levels and GS-X pump activity and whether GS-X pump overexpression results in cisplatin resistance. We transfected the human gamma-glutamylcysteine synthetase (gamma-GCS) gene into a human small-cell lung cancer cell line, SBC-3, producing SBC-3/GCS. The intracellular GSH content of SBC-3/GCS was twice that of the parental line, its GS-X pump activity was significantly enhanced and cellular cisplatin accumulation decreased. SBC-3/GCS showed higher resistance (relative resistance value of 7.4) to cisplatin than the parental line SBC-3. These data indicate that gamma-GCS gene overexpression induces cellular cisplatin resistance associated with increases in both the GSH content and GS-X pump activity, resulting in reduced cisplatin accumulation. In conclusion, GS-X pump expression is related to cellular GSH metabolism and involved in cisplatin resistance.
- Published
- 1995
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8. Liver and muscle-fat type glucose transporter gene expression in obese and diabetic rats.
- Author
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Yamamoto T, Fukumoto H, Koh G, Yano H, Yasuda K, Masuda K, Ikeda H, Imura H, and Seino Y
- Subjects
- Animals, Blotting, Northern, Diabetes Mellitus, Experimental metabolism, Gene Expression, Insulin Resistance, Male, Obesity metabolism, RNA, Messenger analysis, RNA, Messenger genetics, RNA, Messenger metabolism, Rats, Rats, Inbred Strains, Rats, Mutant Strains, Rats, Zucker, Reference Values, Diabetes Mellitus, Experimental genetics, Liver metabolism, Monosaccharide Transport Proteins genetics, Muscles metabolism, Obesity genetics
- Abstract
In order to investigate the regulation of glucose transporter gene expression in the altered metabolic conditions of obesity and diabetes, we have measured mRNA levels encoding GLUT2 in the liver and GLUT4 in the gastrocnemius muscle from various insulin resistant animal models, including Zucker fatty, Wistar fatty, and streptozocin(STZ)-treated diabetic rats. Northern blot analysis revealed that GLUT2 mRNA levels were significantly (P less than 0.001) elevated in 14 wk Zucker fatty and Wistar fatty rats relative to lean littermates but were similar in these two groups at 5 wk of age. Furthermore, there was significant increase (P less than 0.01) in GLUT2 mRNA levels in STZ diabetic rats at 3 wk after treatment. GLUT4 mRNA levels were not significantly different between control and insulin resistant rats in all animal models. These results indicate that neither hyperinsulinemia nor hyperglycemia affects GLUT4 mRNA levels in the muscle. However, GLUT2 mRNA levels in the liver were elevated in obesity and diabetes, although this regulatory event occurred independently from circulating insulin or glucose concentrations.
- Published
- 1991
- Full Text
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9. Over-expression of facilitative glucose transporter genes in human cancer.
- Author
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Yamamoto T, Seino Y, Fukumoto H, Koh G, Yano H, Inagaki N, Yamada Y, Inoue K, Manabe T, and Imura H
- Subjects
- Digestive System Neoplasms metabolism, Humans, Monosaccharide Transport Proteins genetics, Neoplasms metabolism, Digestive System Neoplasms genetics, Gene Expression Regulation, Neoplastic, Monosaccharide Transport Proteins biosynthesis, Neoplasms genetics, RNA, Messenger analysis, RNA, Neoplasm analysis
- Abstract
The expression of five facilitative glucose transporter genes, GLUT1 (erythrocyte type), GLUT2 (liver type), GLUT3 (brain type), GLUT4 (muscle/fat type), and GLUT5 (small intestine type), was examined in human cancer tissues of the digestive system by RNA blotting analysis. The amounts of the GLUT1, GLUT2, and GLUT3 transcripts were elevated in most cancer tissues studied, although the expression of the GLUT2 gene is primarily restricted to the liver. On the other hand, mRNA levels of GLUT4 and GLUT5 were below sensitivity in all cancer tissues examined. These results suggest that over-expression of GLUT1 and GLUT3 might be closely related with tissue development and that the acceleration of glucose uptake by transformed cells may result, at least in part, from the increase in the expression of these two glucose transporters.
- Published
- 1990
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10. Increase in liver glucose transporter mRNA levels during rat liver regeneration.
- Author
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Yamada Y, Seino Y, Takeda J, Fukumoto H, Yano H, Inagaki N, Fukuda Y, Seino S, and Imura H
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- Animals, Blood Glucose metabolism, Cycloheximide pharmacology, Gene Expression, Male, Monosaccharide Transport Proteins genetics, Nucleic Acid Probes, RNA, Messenger biosynthesis, Rats, Rats, Inbred Strains, Liver Regeneration drug effects, Monosaccharide Transport Proteins metabolism
- Abstract
Gene expression of liver facilitated glucose transporter was rapidly induced during the liver regenerating process in rats. It reached maximum of 2.7 times at 8 hr of the regenerating course and returned to normal by 48 hr. The protein synthesis inhibitor, cycloheximide, did not interfere with the increased gene expression of liver facilitated glucose transporter. By contrast, erythrocyte/brain-type glucose transporter mRNA could not be detected in the livers of partially hepatectomized rats and sham-operated rats. The plasma glucose levels were transiently increased within 2 hr of the regenerative course and then decreased to a nadir at 4 hr. These results suggest that the increased gene expression of liver facilitated glucose transporter contributes to the decrease in plasma glucose levels.
- Published
- 1990
- Full Text
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11. Intracellular localization of ATP:AMP phosphotransferase in Escherichia coli.
- Author
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Watanabe K, Fukumoto H, and Isoi K
- Subjects
- Adenosine Monophosphate metabolism, Adenosine Triphosphate metabolism, Cell Compartmentation, Cytoplasm enzymology, Escherichia coli enzymology, Adenylate Kinase metabolism, Escherichia coli ultrastructure, Phosphotransferases metabolism
- Abstract
ATP and AMP were immediately converted into ADP by intact cells of Escherichia coli in the presence of Mg2+, while ADP was also rapidly converted into ATP and AMP under the same conditions. Adenylate kinase was released when E. coli cells were converted to spheroplasts by treatment with lysozyme-EDTA or osmotic shock. Adenylate kinase activities detected in the cytoplasm, periplasm and membrane fractions were approximately 58%, 36% and 6% of the total cellular activity, respectively. These results indicate that adenylate kinase in E. coli occurs in the periplasm as well as the cytoplasm.
- Published
- 1986
- Full Text
- View/download PDF
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