Akio TomodaShow email address
Tokyo Medical University, Tokyo 160-0022, Japan | Tokyo Medical University, Tokyo 160-8402, Japan | Department of Biochemistry, Tokyo Medical University, 6-1-1 Shinjuku, Tokyo ...
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Akio Tomoda:Expert Impact
Concepts for whichAkio Tomodahas direct influence:Urinary bicarbonate,Hemoglobin oxidation,Ascorbic acid,Human erythrocytes,Methemoglobin reduction,Blood cells,Organic phosphates,Phenoxazine derivatives.
Akio Tomoda:KOL impact
Concepts related to the work of other authors for whichfor which Akio Tomoda has influence:Multiple myeloma,Cytochrome b5,Human erythrocytes,Urinary bicarbonate,Methemoglobin reduction,Erythrocyte membrane,Blood cells.
KOL Resume for Akio Tomoda
Tokyo Medical University, Tokyo 160-0022, Japan
Department of Biochemistry, Tokyo Medical University, 6-1-1 Shinjuku, Tokyo 160-8402, Japan; E-Mail:,
Department of Biochemistry and Intractable Immune System Disease Research Center, Tokyo Medical University, Tokyo, Japan
Department of Biochemistry, Tokyo Medical University, Tokyo 160-8402, Japan
Department of Biochemistry, Tokyo Medical University, Tokyo, Japan,
Department of Biochemistry, Tokyo Medical University, Japan
Department of Biochemistry and Intractable, Tokyo Medical University
Department of Biochemistry and Intractable Immune System Disease Research Center, Tokyo Medical University
Department of Biochemistry, Tokyo Medical University, 6-1-1, Shinjuku, 160-8402, Tokyo, Japan
Department of Infectious Disease, Division of Microbiology1, First Department of Internal Medicine2, Laboratory of Electron Microscopy4 and Department of Anatomy5, Kyorin University School of Medicine,Tokyo 181-8611, Japan 3Division of Molecular Microbiology, Department of Basic Laboratory Sciences, Graduate School of Medicine, Osaka University, 1-7 Yamadaoka, Suita, Osaka 565-0871, Japan 6Department of Virology I, National Institute of Infectious Diseases, Tokyo 162-8642, Japan 7Department of Biochemistry, Tokyo Medical University, Tokyo 160-0022, Japan.
Department of Biochemistry, Tokyo Medical University, Tokyo 160‐0032, Japan
Department of Biochemistry, Tokyo Medical University, 6-1-1 Shinjuku, Shinjuku-ku, Tokyo 160-8402, Japan
Laboratory of Microbiology, Department of Public Health Pharmacy, Gifu Pharmaceutical University, Mitahora-higashi 5-6-1, Gifu 502-8585, Japan. Laboratory of Chemotherapy, Aichi Cancer Center Institute, Kanokoden 1-1, Chikusa-Ku, Nagoya 464-8681, Japan. Department of Obstetrics and Gynecology, Hachioji Medical Center of Tokyo Medical University, Tatemachi 1163, Hachioji, Tokyo 193-0944, Japan. Department of Biochemistry, Tokyo Medical University, Shinjuku 6-1-1, Shinjuku-ku, Tokyo 160-0022, Japan.
Department of Biochemistry, Tokyo Medical College
Department of Biochemistry, Tokyo Medical College, Shinjuku 6-1-1, Shinjuku, Tokyo 160, Japan.
Department of Biochemistry, Tokyo Medical College, Japan.
Department of Biochemistry, Tokyo Medical College, Tokyo 160, Japan
Department of Biochemistry, Tokyo Medical College, Shinjuki, Tokyo Japan
Department of Biochemistry, Kanazawa University School of Medicine, Kanazawa, Ishikawa 920 Japan
Departments of, Biochemistry and, Ophthalmology, Kanazawa University School of Medicine, Kanazawa, Ishikawa;, National Institute of Hygienic Sciences, Kamiyoga, Tokyo, Japan
Department of Biochemistry, Kanazawa University School of Medicine, Ishikawa, Japan.
Department of Biochemistry, Kanazawa University School of Medicine, Kanazawa, Ishikawa 920, Japan
Department of Biochemistry, Kanazawa University School of Medicine, Kanazawa, Japan
Department of Biochemistry, Kanazwa University School of Medicine, Kanazawa, Ishikawa 920, Japan
Department of Biochemistry, Faculty of Medicine, Kyushu University, 813, Fukuoka, (Japan)
Department of Biochemsitry, Kanazawa University School of Medicine, 920, Kanazawa, (Japan)
Department of Biochemistry, Kanazawa University School of Medicine Kanazawa 920, Japan
Department of Biochemistry, Kanazawa University School of Medicine, 920, Kanazawa, (Japan)
Department of Medical Technology, Kanazawa University, School of Paramedicine, 920, Kanazawa, (Japan)
Department of Biochemistry, Kyushu University School of MedicineHigashi-ku, Fukuoka, Fukuoka 812
Department of Biochemistry, Kyushu University School of Medicine, 812, Fukuoka, (Japan)
|methemoglobin aromatic compounds||#1|
|ferrous state cyanide||#1|
|publication adult atmosphere||#1|
|methemoglobin aromatic reductants||#1|
|immune complexes pma||#1|
|methemoglobin tryptophan metabolites||#1|
|ferrous ferric haemoglobin||#1|
|wga immune complexes||#1|
|kappa1 kappa4 addition||#1|
|purified human oxy||#1|
|methaemoglobin kappa3 alpha||#1|
|ferrous hemoglobin reduction||#1|
|3hour car trip||#1|
|methemoglobin 3hydroxyanthranilic acid||#1|
|nadphflavin reductase basis||#1|
|oxidation ferrous hemoglobin||#1|
|increase urinary bicarbonate||#1|
|urinary bicarbonate contents||#1|
|beta intermediate haemoglobins||#1|
|valency hybrids studies||#1|
|windows carbon dioxide||#1|
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Prominent publications by Akio Tomoda
Macrolide antibiotics block autophagy flux and sensitize to bortezomib via endoplasmic reticulum stress-mediated CHOP induction in myeloma cells
[ PUBLICATION ]
The specific 26S proteasome inhibitor bortezomib (BZ) potently induces autophagy, endoplasmic reticulum (ER) stress and apoptosis in multiple myeloma (MM) cell lines (U266, IM-9 and RPMI8226). The macrolide antibiotics including concanamycin A, erythromycin (EM), clarithromycin (CAM) and azithromycin (AZM) all blocked autophagy flux, as assessed by intracellular accumulation of LC3B-II and p62. Combined treatment of BZ and CAM or AZM enhanced cytotoxicity in MM cell lines, although ...
|Known for Myeloma Cells | Autophagy Flux | Macrolide Antibiotics | Endoplasmic Reticulum | Combination Bz|
The rate of methemoglobin reduction by ascorbic acid was accelerated in the presence of ATP,2,3-diphosphoglycerate (2,3-DPG), and inositol hexaphosphate (IHP). The acceleration was as much as three times, four times, and ten times in the presence of ATP, 2.3-DPG, and IHP at pH 7.0, respectively. The changes of the concentrations of methemoglobin and ascorbic acid during the methemoglobin reduction were determined, and the reaction was found to proceed stoichiometrically in the presence ...
|Known for Ascorbic Acid | Methemoglobin Reduction | Organic Phosphates | Presence Ihp | Inositol Hexaphosphate|
Clarithromycin enhances bortezomib-induced cytotoxicity via endoplasmic reticulum stress-mediated CHOP (GADD153) induction and autophagy in breast cancer cells
[ PUBLICATION ]
The specific 26S proteasome inhibitor, bortezomib (BZ) potently induces apoptosis as well as autophagy in metastatic breast cancer cell lines such as MDA-MB-231 and MDA-MB-468. The combined treatment of clarithromycin (CAM) and BZ significantly enhances cytotoxicity in these cell lines. Although treatment with up to 100 µg/ml CAM alone had little effect on cell growth inhibition, the accumulation of autophagosomes and p62 was ...
|Known for Cancer Cell | Combined Treatment | Mediated Chop | Reticulum Stress | Induced Cytotoxicity|
[ PUBLICATION ]
In this study, we sought to identify the transporters that mediate the uptake of L-carnitine and acetyl-L-carnitine in cultured rat cortical astrocytes. L-[(3)H]carnitine and acetyl-L-[(3)H]carnitine uptake were both saturable, and mediated by a single Na(+)-dependent transport system. Uptake of both was inhibited by L-carnitine, D-carnitine, acetyl-L-carnitine and various organic cations. Acylcarnitines (acetyl-, butyryl-, hexanoyl-, octanoyl- and palmitoyl-L-carnitine) also interacted ...
|Known for Organic Cation | Carnitine Transporter | Functional Expression | Rat Astrocytes | Transport Proteins|
Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency.
[ PUBLICATION ]
We analyzed the NADH-cytochrome b5 reductase gene of hereditary methemoglobinemia type I and type III, by using PCR-related techniques. The mutation in type I is a guanine-to-adenine substitution in codon 57 of exon 3 of the NADH-cytochrome b5 reductase gene, and the sense of this codon is changed from arginine to glutamine. In type III the mutation is a thymine-to-cytosine transition in codon 148 of exon 5, causing leucine-to-proline replacement in type III. The former mutation ...
|Known for Hereditary Methemoglobinemia | Cytochrome B5 | Reductase Gene | Codon Exon | Recognition Site|
Chlamydia pneumoniae growth inhibition in human monocytic THP-1 cells and human epithelial HEp-2 cells by a novel phenoxazine derivative
[ PUBLICATION ]
In this study the effects of 2-amino-phenoxazine-3-one (phenoxazine derivate, Phx-3) on Chlamydia (Chlamydophila) pneumoniae growth in human monocytic THP-1 cells as well as human epithelial HEp-2 cells were examined. Cells were infected with bacteria at an m.o.i. of 10 by centrifugation. After washing to remove any remaining bacteria, the cells were incubated with or without Phx-3 in the presence or absence of tryptophan for 72 h. The bacteria in cells were assessed by staining of ...
|Known for Bacterial Rna | Human Epithelial | Chlamydia Pneumoniae | Growth Cells | Treatment Phx3|
Circadian Changes in Urinary Bicarbonate, Nitric Oxide Metabolites and pH in Female Player during Handball Camp Involved in an Exercise, Rest and Sleep Cycle
[ PUBLICATION ]
Bicarbonate and nitric oxide levels are important humoral factors in the blood and are affected by the human body's physical condition. There are few reports, however, on changes in blood bicarbonate and nitric oxide levels during exercise and rest. Since urinary bicarbonate and nitric oxide metabolites reflect the levels of bicarbonate and nitric oxide in the blood, we studied circadian changes in 6 female athletes by monitoring their urinary pH and their levels of urinary bicarbonate ...
|Known for Urinary Bicarbonate | Nitric Oxide | Exercise Female | Training Camp | Humans Hydrogen|
The time course of methemoglobin reduction by ascorbic acid under anaerobic conditions was analyzed by using isoelectric focusing on Ampholine plate gel in order to compare results obtained by studies of the changes in absorption during the reaction. The intermediate hemoglobin which appeared all through the reaction was single and identified as the alpha3+beta2+ valency hybrid. In the presence of inositol hexaphosphate, reduction of methemoglobin was considerably accelerated and this ...
|Known for Ascorbic Acid | Methemoglobin Reduction | Valency Hybrid | Anaerobic Conditions | Inositol Hexaphosphate|
Involvement of oxidoreductive reactions of intracellular haemoglobin in the metabolism of 3-hydroxyanthranilic acid in human erythrocytes
[ PUBLICATION ]
3-Hydroxyanthranilic acid, a metabolite of tryptophan, was rapidly metabolized by human erythrocytes. The final product was determined to be cinnabarinic acid as detected by spectrophotometry, paper chromatography and t.l.c. The formation of cinnabarinic acid from 3-hydroxyanthranilic acid in the cells was markedly inhibited by CO when intracellular haemoglobin was in a ferrous state, and by cyanide when it was in a ferric state. Ferrous haemoglobin in erythrocytes was oxidized to (alpha ...
|Known for Hydroxyanthranilic Acid | Human Erythrocytes | Oxidoreductive Reactions | Ferrous State | Oxidation Reduction|
Effect of transmethylation‐reaction and increased levels of cAMP on superoxide generation of guinea‐pig macrophages induced with wheat germ agglutinin and phorbor myristate
[ PUBLICATION ]
Superoxide (O2-) generation of guinea-pig macrophages induced by wheat germ agglutinin (WGA) was suppressed to a great extent by the inhibition of transmethylation with 3'-deazaadenosine. When macrophages were stimulated with phorbor myristate (PMA) instead of WGA, the suppression of O2- generation of macrophages was observed to be slight despite the presence of 3'-deazaadenosine. These results were confirmed under various conditions. Thus the WGA-stimulated O2- generation of macrophages ...
|Known for O2 Generation | Wheat Germ | Pma Wga | Pig Macrophages | Tetradecanoylphorbol Acetate|