Kyushu University Academic Staff Educational and Research Activities Database
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Yoshinori Fujimura Last modified date:2021.06.11

Associate Professor / Division of Applied Biological Chemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture
Department of Bioscience and Biotechnology
Faculty of Agriculture

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Academic Degree
PhD, Agriculture
Country of degree conferring institution (Overseas)
Field of Specialization
Food Preventive Medicine, Food Chemical Biology, Nutrimetabolomics
ORCID(Open Researcher and Contributor ID)
Total Priod of education and research career in the foreign country
Research Interests
  • R&D of high-precision metabolic profiling system by multiple mass spectrometric analysis
    keyword : Metabolic profiling, Metabolomics, Mass spectrometry, Redox-related diseases, Biomarker, Pathological diagnosis
  • Chemical biology based food preventive medicine research
    keyword : Chemical biology, Target molecule, Preventive medicine, Nutrimetabolomics, Green tea catechin
Academic Activities
1. Fujimura Y, Tachibana H, Genomics, Proteomics and Metabolomics in Nutraceuticals and Functional Foods, 2nd Edition, Wiley-Blackwell, 397-406, 2015.09.
2. Fujimura, Y. and Tachibana, H., Handbook of Green Tea and Health Research, Nova Science Publishers Inc., 257-299, 2009.05.
1. 三浦 大典, 藤村 由紀, Unno Y, Yamaguchi R, Ogata K, Analysis of Lipids in a NAFLD Model Mouse, SHIMADZU Technical Reports, C146-E266, 1-4, 2014.04.
2. Fujimura, Y. and Tachibana, H., Molecular basis for anti-cancer activity of EGCG in vivo: Molecular-targeting prevention of cancer by green tea catechin, Handbook of Green Tea and Health Research, Nova Science Publishers Inc., 257-299, 2009.05.
1. Fujimura Y, Fujino K, Yoshimoto T, Nezu A, Marugame Y, Bae J, Kumazoe M, Tachibana H., Eriodictyol-amplified 67-kDa laminin receptor signaling potentiates the antiallergic effect of O-methylated catechin, J Nat Prod, in press, 2021.06.
2. Kumazoe M, Tanaka Y, Yoshitomi R, Marugame Y, Lee KW, Onda H, Fujimura Y, Yonekura M, Shimamoto Y, Tachibana H., Glucosyl-hesperidin enhances the cyclic guanosine monophosphate-inducing effect of a green tea polyphenol EGCG., J Nat Med, in press, 2021.06.
3. Kumazoe M, Kadomatsu M, Bae J, Otsuka Y, Fujimura Y, Tachibana H., Src Mediates Epigallocatechin-3-O-Gallate-Elicited Acid Sphingomyelinase Activation, Molecules, 10.3390/molecules25225481, 25, 22, 2020.11.
4. Yoshitomi R, Nakayama K, Yamashita S, Kumazoe M, Lin TA, Mei CY, Marugame Y, Fujimura Y, Maeda-Yamamoto M, Kuriyama S, *Tachibana H, Plasma Homocysteine Concentration is Associated with the Expression Level of Folate Receptor 3, Sci Rep, 10.1038/s41598-020-67288-9, 10, 1, 2020.06.
5. Murata M, Shimizu Y, Marugame Y, Nezu A, Fujino K, Yamada S, Kumazoe M, Fujimura Y, Tachibana H., EGCG down-regulates MuRF1 expression through 67-kDa laminin receptor and the receptor signaling is amplified by eriodictyol, J. Nat. Med.,, in press, 2020.05.
6. Kumazoe M, Hiroi S, Tanimoto Y, Miyakawa J, Yamanouchi M, Suemasu Y, Yoshitomi R, Murata M, Fujimura Y, Takahashi T, Tanaka H, Tachibana H., Cancer cell selective probe by mimicking EGCG, Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2020.03.021, 525, 4, 974-981, 2020.05, Targeting proteins that are overexpressed in cancer cells is the major strategy of molecular imaging and drug delivery systems. The 67-kDa laminin receptor (67LR), also known as oncofetal antigen, is overexpressed in several types of cancer, including melanoma, multiple myeloma, cervical cancer and bile duct carcinoma. 67LR is involved in tumour growth, tumour metastasis and drug resistance. Green tea polyphenol (−)-epigallocatechin-3-O-gallate (EGCG) directly binds to cell-surface 67LR and induces apoptosis through the protein kinase B (Akt)/endothelial nitric oxide synthase/nitric oxide/cyclic GMP (cGMP) axis. Here we report the optimum hydroxyl group for the utilization of EGCG as a novel fluorescent EGCG-mimic imaging probe based on 67LR agonist characters, including Akt activation and inhibitory effect on viable cell number in cancer cells. 67LR specific targeting is unambiguously confirmed with the use of a non-labelled EGCG competitive assay and 67LR knockdown. Importantly, this probe strongly binds to multiple myeloma cells compared with its binding to normal cells..
7. Bae J, Kumazoe M, Murata K, Fujimura Y, Tachibana H., Procyanidin C1 Inhibits Melanoma Cell Growth by Activating 67-kDa Laminin Receptor Signaling, Mol. Nutr. Food Res., 10.1002/mnfr.201900986, 64, 7, 2020.04, Scope: Procyanidin C1 (PC1) is an epicatechin trimer found mainly in grapes that is reported to provide several health benefits. However, little is known about the molecular mechanisms underlying these benefits. The aim of this study is to demonstrate the molecular mechanisms by which PC1 operates. Methods and results: A 67-kDa laminin receptor (67LR) is identified as a cell surface receptor of PC1, with a Kd value of 2.8 µm. PC1 induces an inhibitory effect on growth, accompanied by dephosphorylation of the C-kinase potentiated protein phosphatase-1 inhibitor protein of 17 kDa (CPI17) and myosin regulatory light chain (MRLC) proteins, followed by actin cytoskeleton remodeling in melanoma cells. These actions are mediated by protein kinase A (PKA) and protein phosphatase 2A (PP2A) activation once PC1 is bound to 67LR. Conclusion: It is demonstrated that PC1 elicits melanoma cell growth inhibition by activating the 67LR/PKA/PP2A/CPI17/MRLC pathway..
8. Bae J, Kumazoe M, Takeuchi C, Hidaka S, Fujimura Y, Tachibana H., Epigallocatechin-3-O-gallate induces acid sphingomyelinase activation through activation of phospholipase C, Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2019.09.102, 520, 1, 186-191, 2019.11, Epigallocatechin-3-O-gallate (EGCG)-induced cyclic guanosine monophosphate (cGMP) plays a crucial role in EGCG-induced cell death in various types of cancer cells. However, little is known regarding the early molecular events after cGMP induction. In this study, we showed that cGMP induction is sufficient to induce the phosphorylation of protein kinase C delta (PKCδ) at Ser664, the crucial kinase for EGCG-induced activation of acid sphingomyelinase (ASM). Using a chemical inhibitor library, we revealed that the inhibitors of the negative regulators of diacylglycerol strongly increase the effect of EGCG. We also showed that EGCG treatment increased phospholipase C (PLC) activity, and the same results were obtained with cGMP inducer treatment. EGCG-induced ASM activation was completely suppressed by pharmacological inhibition of PLC. Collectively, EGCG-induced cGMP activated the cGMP/PLC/PKCδ/ASM signaling axis in multiple myeloma cells..
9. Hayakawa E, Ohgidani M, Fujimura Y, Kanba S, Miura D, Kato TA, Cuprizone-treated mice, a possible model of schizophrenia, highlighting the simultaneous abnormalities of GABA, serine and glycine in hippocampus, Schizophr. Res., 10.1016/j.schres.2019.06.010, 210, 326-328, 2019.08.
10. Morikawa-Ichinose T, Fujimura Y, Murayama F, Yamazaki Y, Yamamoto T, Wariishi H, and Miura D., Improvement of sensitivity and reproducibility for imaging of endogenous metabolites by matrix-assisted laser desorption/ionization-mass spectrometry, J Am Soc Mass Spectrum, 10.1007/s13361-019-02221-7, 30, 1512-1520, 2019.05.
11. Bae J, Kumazoe M, Fujimura Y, Tachibana H, Diallyl disulfide potentiates anti-obesity effect of green tea in high-fat/high-sucrose diet-induced obesity, J Nutr Biochem, 10.1016/j.jnutbio.2018.10.014, 64, 152-161, 2019.02.
12. Wasai M, Fujimura Y, Nonaka H, Murata M, Kitamura R, Tachibana H, Postprandial glycaemia-lowering effect of a green tea cultivar Sunrouge and cultivar-specific metabolic profiling for determining bioactivity-related ingredients, Sci Rep, 10.1038/s41598-018-34316-8, 8, 16041, 2018.10.
13. Torata N, Kubo M, Miura D, Ohuchida K, Mizuuchi Y, Fujimura Y, Hayakawa E, Kai M, Oda Y, Mizumoto K, Hashizume M, Nakamura M, Visualizing Energy Charge in Breast Carcinoma Tissues by MALDI Mass-spectrometry Imaging Profiles of Low-molecular-weight Metabolites, Anticancer Res, 10.21873/anticanres.12723, 38, 4267-4272, 2018.07.
14. Irie M, Hayakawa E, Fujimura Y, Honda Y, Setoyama D, Wariishi H, Hyodo F, Miura D, Analysis of spatiotemporal metabolomic dynamics for sensitively monitoring biological alterations in cisplatin-induced acute kidney injury, Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2018.01.012., 496, 140-146, 2018.01.
15. Fujimura Y, Miura D, Tachibana H, A Phytochemical-Sensing Strategy Based on Mass Spectrometry Imaging and Metabolic Profiling for Understanding the Functionality of the Medicinal Herb Green Tea, Molecules, 10.3390/molecules22101621, 22, E1621, 2017.09.
16. Fujimura Y, Kawano C, Maeda-Murayama A, Nakamura A, Koike-Miki A, Yukihira D, Hayakawa E, Ishii T, Tachibana H, Wariishi H, Miura D, A Chemometrics-driven Strategy for the Bioactivity Evaluation of Complex Multicomponent Systems and the Effective Selection of Bioactivity-predictive Chemical Combinations, Sci. Rep., 7, 2257, 2017.05.
17. Huang Y, Sumida M, Kumazoe M, Sugihara K, Suemasu Y, Yamada S, Yamashita S, Miyakawa J, Takahashi T, Tanaka H, Fujimura Y, Tachibana H, Oligomer formation of a tea polyphenol, EGCG, on its sensing molecule 67 kDa laminin receptor, Chem. Commun., 53, 1941-1944, 2017.02.
18. Nakamura J, Morikawa-Ichinose T, Fujimura Y, Hayakawa E, Takahashi K, Ishii T, Miura D, Wariishi H, Spatially resolved metabolic distribution for unraveling the physiological change and responses in tomato fruit using matrix-assisted laser desorption/ionization-mass spectrometry imaging (MALDI-MSI), Anal. Bioanal. Chem., 409, 1697-1706, 2017.02.
19. Hayakawa E, Fujimura Y, Miura D, MSIdV: a versatile tool to visualize biological indices from mass spectrometry imaging data, Bioinfomatics, 10.1093/bioinformatics/btw548, 32, 3852-3854, 2016.08.
20. Tsukamoto S, Huang Y, Kumazoe M, Lesnick C, Yamada S, Ueda N, Suzuki T, Yamashita S, Kim YH, Fujimura Y, Miura D, Kay NE, Shanafelt TD, Tachibana H, Sphingosine Kinase-1 Protects Multiple Myeloma from Apoptosis Driven by Cancer-Specific Inhibition of RTKs, Mol Cancer Ther, 10.1158/1535-7163, 14, 2303-2312, 2015.10.
21. Yukihira D, Fujimura Y, Wariishi H, Miura D, Bacterial metabolism in immediate response to nutritional perturbation with temporal and network view of metabolites, Mol Biosyst, 10.1039/c5mb00182j, 11, 2473-2482, 2015.09.
22. Inoue T, Inoguchi T, Sonoda N, Hendarto H, Makimura H, Sasaki S, Yokomizo H, Fujimura Y, Miura D, Takayanagi R, GLP-1 analog liraglutide protects against cardiac steatosis, oxidative stress and apoptosis in streptozotocin-induced diabetic rats, Atherosclerosis, 10.1016/j.atherosclerosis.2015.03.026, 240, 250-259, 2015.05.
23. Iwasa K, Setoyama D, Shimizu H, Seta H, Fujimura Y, Miura D, Wariishi H, Nagai C, Nakahara K, Identification of 3-methylbutanoyl glycosides in green Coffea arabica beans as causative determinants for the quality of coffee flavors, J Agric Food Chem, 10.1021/jf5054047, 63, 3742-3751, 2015.04.
24. Kumazoe M, Fujimura Y, Hidaka S, Kim Y, Murayama K, Takai M, Huang Y, Yamashita S, Murata M, Miura D, Wariishi H, Maeda-Yamamoto M, Tachibana H, Metabolic profiling-based data-mining for an effective chemical combination to induce apoptosis of cancer cells, Sci Rep, 10.1038/srep09474, 5, 9474, 2015.03.
25. Fujimura Y, Small molecule-sensing strategy and techniques for understanding the functionality of green tea, Biosci Biotechnol Biochem, 10.1080/09168451.2014.996205, 79, 687-699, 2015.01.
26. Kim YH, NinomiyaY, Yamashita S, Kumazoe M, Huang Y, Nakahara K, Won YS, Murata M, Fujimura Y, Yamada K, Tachibana H, IL-4 receptor α in non-lipid rafts is the target molecule of strictinin in inhibiting STAT6 activation, Biochem Biophys Res Commun, 450, 824-830, 2014.09.
27. Kim YH, Fujimura Y, Sasaki M, Yang X, Yukihira D, Miura D, Unno Y, Ogata K, Wariishi H, Nakajima H, Yamashita S, Nakahara K, Murata M, Lin IC, Yamada K, Tachibana H., In situ label-free visualization of orally dosed strictinin within mouse kidney by MALDI-MS imaging., J Agric Food Chem, 62, 9279-9285, 2014.09.
28. Fujimura Y, Miura D, MALDI Mass Spectrometry Imaging for Visualizing In Situ Metabolism of Endogenous Metabolites and Dietary Phytochemicals, Metabolites, 4, 319-346, 2014.05.
29. Fujimura Y, Ikenaga N, Ohuchida K, Setoyama D, Irie M, Miura D, Wariishi H, Murata M, Mizumoto K, Hashizume M, Tanaka M, Mass spectrometry-based metabolic profiling of gemcitabine-sensitive and gemcitabine-resistant pancreatic cancer cells, Pancreas, 43, 311-318, 2014.03.
30. Irie M, Fujimura Y, Yamato M, Miura D, Wariishi H, Integrated MALDI-MS Imaging and LC-MS Techniques for Visualizing Spatiotemporal Metabolic Dynamics in a Rat Stroke Model, Metabolomics, 10, 473-483, 2014.03.
31. Nagao T, Yukihira D, Fujimura Y, Saito K, Miura D, Wariishi H, Power of isotopic fine structure for unambiguous determination of metabolite elemental compositions: in silico evaluation and metabolomic application, Anal Chim Acta, 813, 70-76, 2014.02.
32. Batchuluun B, Kobayashi K, Inoguchi T, Sonoda N, Fujii M, Maeda Y, Fujimura Y, Miura D, Hirano K, Takayanagi R, Metformin and liraglutide ameliorate high glucose-induced oxidative stress via inhibition of PKC-NAD(P)H oxidase pathway in human aortic endothelial cells, Atherosclerosis, 232, 156-164, 2014.01.
33. Yukihira D, Miura D, Fujimura Y, Umemura Y, Yamaguchi S, Funatsu S, Yamazaki M, Ohta T, Inoue H, Shindo M, Wariishi H, A QSPR Study on Structural Properties of Metabolites for Preferred Ionization in MALDI-MS Analysis, J. Am. Soc. Mass Spectrom., 25, 1-5, 2014.01.
34. Kim YH, Fujimura Y, Hagihara T, Sasaki M, Yukihira D, Nagao T, Miura D, Wariishi H, Saito K, Yamaguchi S, Tanaka H, Yamada K, Tachibana H, In situ label-free imaging for visualizing the biotransformation of a bioactive polyphenol, Sci. Rep., 3, 2805, 2013.10.
35. Setoyama D, Fujimura Y, Miura D, Metabolomics reveals that carnitine-palmitoyltransferase-1 is a novel target for oxidative inactivation in human cells, Genes Cells, 18, 311-318, 2013.09.
36. Kim YH, Yoshimoto M, Nakayama K, Tanino S, Fujimura Y, Yamada K, Tachibana H, Tannic acid, a higher galloylated pentagalloylglucose, suppresses antigen-specific IgE production by inhibiting ε germline transcription induced by STAT6 activation, FEBS Open Bio, 3, 341-345, 2013.08.
37. Inoue T, Kobayashi K, Inoguchi T, Sonoda N, Maeda Y, Hirata E, Fujimura Y, Miura D, Hirano KI, Takayanagi R, Downregulation of adipose triglyceride lipase in the heart aggravates diabetic cardiomyopathy in db/db mice, Biochem. Biophys. Res. Commun., 438, 224-229, 2013.08.
38. Fujimura Y, Sumida M, Ogawa N, Tsuruda S, Sugihara K, Tsukamoto S, Yamada K, Tachibana H, Green Tea Polyphenol EGCG Sensing Motif on the 67-kDa Laminin Receptor, PLoS One, 7, e37942, 2012.05, Background: We previously identified the 67-kDa laminin receptor (67LR) as the cell-surface receptor conferring the major green tea polyphenol (–)-epigallocatechin-3-O-gallate (EGCG) responsiveness to cancer cells. However, the underlying mechanism for interaction between EGCG and 67LR remains unclear. In this study, we investigated the possible role of EGCG-67LR interaction responsible for its bioactivities.
Methodology/Principal Findings: We synthesized various peptides deduced from the extracellular domain corresponding to the 102-295 region of human 67LR encoding a 295-amino acid. The neutralizing activity of these peptides toward EGCG cell-surface binding and inhibition of cancer cell growth were assayed. Both activities were inhibited by a peptide containing the 10-amino acid residues, IPCNNKGAHS, corresponding to residues 161-170. Furthermore, mass spectrometric analysis revealed the formation of a EGCG-LR161-170 peptide complex. A study of the amino acid deletion/replacement of the peptide LR161-170 indicated that the 10-amino acid length and two basic amino acids, K166 and H169, have a critical role in neutralizing EGCG’s activities. Moreover, neutralizing activity against the anti-proliferation action of EGCG was observed in a recombinant protein of the extracellular domain of 67LR, and this effect was abrogated by a deletion of residues 161-170. These findings support that the 10 amino-acid sequence, IPCNNKGAHS, might be the functional domain responsible for the anti-cancer activity of EGCG.
Conclusions/Significance: Overall, our results highlight the nature of the EGCG-67LR interaction and provide novel structural insights into the understanding of 67LR-mediated functions of EGCG, and could aid in the development of potential anti-cancer compounds for chemopreventive or therapeutic uses that can mimic EGCG-67LR interactions.
39. Miura D, Fujimura Y, Wariishi H., In situ Metabolomic Mass Spectrometry Imaging: Recent Advances and Difficulties, J Proteomics, 75, 5052-5060, 2012.02, MS imaging (MSI) is a remarkable new technology that enables us to determine the distribution of biological molecules present in tissue sections by direct ionization and detection. This technique is now widely used for in situ imaging of endogenous or exogenous molecules such as proteins, lipids, drugs and their metabolites, and it is a potential tool for pathological analysis and the investigation of disease mechanisms. MSI is also thought to be a technique that could be used for biomarker discovery with spatial information. The application of MSI to the study of endogenous metabolites has received considerable attention because metabolites are the result of the interactions of a system's genome with its environment and a total set of these metabolites more closely represents the phenotype of an organism under a given set of conditions. Recent studies have suggested the importance of in situ metabolite imaging in biological discovery and biomedical applications, but several issues regarding the technical application limits of MSI still remained to be resolved. In this review, we describe the capabilities of the latest MSI techniques for the imaging of endogenous metabolites in biological samples, and also discuss the technical problems and new challenges that need to be addressed for effective and widespread application of MSI in both preclinical and clinical settings. This article is part of a Special Issue entitled: Mass spectrometric interrogation and imaging of tissues Mass spectrometric interrogation and imaging of tissues..
40. Inoue T, Kobayashi K, Inoguchi T, Sonoda N, Fujii M, Maeda Y, Fujimura Y, Miura D, Hirano K, Takayanagi R., Reduced expression of adipose triglyceride lipase enhances tumor necrosis factor α-induced intercellular adhesion molecule-1 expression in human aortic endothelial cells via protein kinase c-dependent activation of nuclear factor-kB., J. Biol. Chem., 286, 32045-32053, 2011.08.
41. Fujimura Y, Kurihara K, Ida M, Kosaka R, Miura D, Wariishi H, Maeda-Yamamoto M, Nesumi A, Saito T, Kanda T, Yamada K, Tachibana H, Metabolomics-driven Nutraceutical Evaluation of Diverse Green Tea Cultivars , PLoS One, 6, e23426, 2011.08.
42. Miura D, Fujimura Y, Yamato M, Hyodo F, Utsumi H, Tachibana H, and Wariishi H, Ultrahighly Sensitive in Situ Metabolomic Imaging for Visualizing Spatiotemporal Metabolic Behaviors, Anal. Chem., 82, 9789-9796, 2010.02.
43. Byun, E.H., Fujimura, Y., Yamada, K., and Tachibana, H., TLR 4 Signaling Inhibitory Pathway Induced by Green Tea Polyphenol Epigallocatechin-3-Gallate through 67-kDa Laminin Receptor, J. Immunol., 185, 33-45, 2010.06.
44. Kanouchi, H., Shibuya, M., Tsukamoto, S., Fujimura, Y., Tachibana, H., Yamada, K., and Oka, T., Comparisons of uptake and cell surface binding among pyridoxal, pyridoxine, and pyridoxamine in RAW264.7 cells, Nutrition, 26, 648-652, 2010.05.
45. Miura, D., Fujimura, Y., Tachibana, H., and Wariishi, H. , Functional evaluation of anticancer drugs in human leukemia cells based on metabolic profiling technique, Animal Cell Technology, 2010.05.
46. Miura, D., Fujimura, Y., Tachibana, H., and Wariishi, H., Highly Sensitive MALDI-Mass Spectrometry for High-throughput Metabolic Profiling, Anal. Chem., 82, 498-504, 2010.01.
47. Fujimura, Y., Miura, D., Hyodo, F., Yasukawa, K., Tachibana, H., Utsumi, H., and Wariishi, H, Evaluation of cisplatin-induced nephrotoxicity by Overhauser MRI and mass spectrometry imaging, Free Radic. Biol. Med., 47, 141-142, 2009.11.
48. Miura, D., Yamato, M., Fujimura, Y., Hyodo, F., Tachibana, H., Utsumi, H., and Wariishi, H., In situ metabolomics imaging of a rat brain section of transient middle cerebral artery occlusion model, Free Radic. Biol. Med., 47, 146-147, 2009.11.
49. Hyodo, F., Miura, D., Fujimura, Y., Yasukawa, K., Sakai, K., Ichikawa, K., Wariishi, H., and Utsumi, H., Visualization of nitroxyl probes for molecular redox imaging by Overhauser MRI and mass spectrometry imaging, Free Radic. Biol. Med., 47, 144, 2009.11.
50. Ohta, S., Fujimura, Y., Yamada, K., and Tachibana, H., Involvement of 67 kDa laminin receptor on cellular uptake of green tea polyphenol, epigallocatechin-3-O-gallate, in Caco2 cells, Animal Cell Technology, 15, 211-215, 2009.11.
51. Lee, J.H., Tachibana, H., Morinaga, Y., Fujimura, Y., and Yamada, K., Modulation of proliferation and differentiation of C2C12 skeletal muscle cells by fatty acids, Life Sci., 84, 415-420, 2009.05.
52. Fujimura, Y., Umeda, D., Yamada, K., and Tachibana, H., The impact of the 67 kDa laminin receptor on both cell-surface binding and anti-allergic action of tea catechins, Arch. Biochem. Biophys., 476, 133-138, 2008.11.
53. Yano, S., Fujimura, Y., Umeda, D., Miyase, T., Yamada, K., and Tachibana, H., Relationsip between the biological activities of methylated derivatives of EGCG and their cell surface binding activities, J. Clin Biochem. Nutr., 43, 473-476, 2008.11.
54. Fujimura, Y., Umeda, D., Maeda-Yamamoto, M., Yamada, K., and Tachibana, H., The 67 kDa laminin receptor mediates anti-allergic effects of (-)-epigallocatechin-3-O-(3-O-methyl) gallate, J. Clin Biochem. Nutr., 43, 477-480, 2008.10.
55. Fujimura, Y., Umeda, D., Yano, S., Maeda-Yamamoto, M., Yamada, K., and Tachibana, H., The 67 kDa laminin receptor as a primary determinant of anti-allergic effects of O-methylated EGCG, Biochem. Biophys. Res. Commun., 364, 79-85, 2007.12.
56. Tachibana, H., Fujimura, Y., Ogawa, N., Sumida, M., Tsuruda, S., and Yamada, K., Identification of the binding site of the green tea polyphenol EGCG receptor, J. Clin Biochem. Nutr., 41, S145, 2007.05.
57. Yano, S., Fujimura, Y., Umeda, D., Miyase, T., Yamada, K., and Tachibana, H., Relationship between the biological activities of methylated derivatives of EGCG and their cell surface binding activities, J. Agric. Food Chem., 55, 7144-7148, 2007.05.
58. Yano, S., Umeda, D., Yamashita, T., Ninomiya, Y., Sumida, M., Fujimura, Y., Yamada, K., and Tachibana, H., Dietary flavones suppress IgE and Th2 cytokines in OVA-immunized BALB/c mice, Eur. J. Nutr., 46, 257-263, 2007.05.
59. Ikeda, Y., Murakami, A., Fujimura, Y., Tachibana, H., Yamada, K., Hirano, K., and Ohigashi, H. , Aggregated ursolic acid, a natural triterpenoid, induces interleukin-1 release in murine peritoneal macrophages: Role of CD36, J. Immunol., 178, 4854-4864, 2007.05.
60. Tachibana, H., Daisuke, U., Fujimura, Y., and Yamada, K., Green tea polyphenol EGCG signaling through 67 kDa laminin receptor, J. Clin Biochem. Nutr., 41, S27, 2007.05.
61. Fujimura, Y., Umeda, D., Maeda-Yamamoto, M., Yamada, K., and Tachibana, H., The 67 kDa laminin receptor mediates anti-allergic effects of (-)-epigallocatechin-3-O-(3-O-methyl) gallate, J. Clin Biochem. Nutr., 41, S145, 2007.05.
62. Ikeda, Y., Murakami, A., Fujimura, Y., Tachibana, H., Yamada, K., Masuda, D., Hirano, K., Yamashita, S., and Ohigashi, H., Aggregated ursolic acid, a natural triterpenoid, binds to CD36 for inducing interleukin-1 release from murine peritoneal macrophages, J. Clin Biochem. Nutr., 41, 99, 2007.05.
63. Fujimura, Y., Umeda, D., Kiyohara, Y., Sunada, Y., Yamada, K., and Tachibana, H., The involvement of the 67 kDa laminin receptor-mediated modulation of cytoskeleton in the degranulation inhibition induced by epigallocatechin-3-O-gallate, Biochem. Biophys. Res. Commun., 348, 524-531, 2006.05.
64. Yano, S., Umeda, D., Maeda, N., Fujimura, Y., Yamada, K., Tachibana, H., Dietary Apigenin Suppresses IgE and Inflammatory Cytokines Production in C57BL/6N Mice., J. Agric. Food Chem., 54, 5203-5207, 2006.05.
65. Kobayashi, S., Ogawa, N., Fujimura, Y., Tachibana, H., and Yamada, K., Water-soluble Component in Dried Chrysanthemum Flower Stimulates Tumor Necrosis Factor-alpha Production by Mouse Macrophage-like Cell Line RAW264.7, Food Sci. Tech. Res., 12, 2, 144-147, 2006.05.
66. Fujimura, Y., Yamada, K., and Tachibana, H., A lipid raft-associated 67kDa laminin receptor mediates suppressive effect of epigallocatechin-3-O-gallate on FcepsilonRI expression., Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2005.08.146, 336, 2, 674-681, 2005.05.
67. Fujimura, Y., Tachibana, H., and Yamada, K., A difference between Epigallocatechin-3-gallate and Epicatechin-3-gallate on anti-allergic effect is dependent on their distinct distribution to lipid rafts, Biofactors, 21, 1-4, 133-135, 2004.05.
68. Tachibana, H., Fujimura, Y., and Yamada, K. , Epigallocatechin gallate associated with cell surface lipid rafts downregulates high affinity IgE receptor through the inhibition of extracellular signal-regulated kinase1/2 phosphorylation, Biofactors, 21, 1-4, 383-385, 2004.05.
69. Fujimura, Y., Tachibana, H., and Yamada, K., Negative regulation of the basophil activation by natural ligands for Peroxisome proliferator-activated receptors, Animal Cell Technology, 13, 369-374, 2004.05.
70. Tachibana, H., Koga, K., Fujimura, Y., and Yamada, K., A receptor for a tea polyphenol EGCG, Nature Struct. Mol. Biol., 11, 380-381, 2004.03.
71. Fujimura, Y., Tachibana, H., and Yamada, K., Lipid raft-associated catechin suppresses the FcepsilonRI expression by inhibiting phosphorylation of the extracellular signal-regulated kinase1/2, FEBS Lett., 10.1016/S0014-5793(03)01432-7, 556, 1-3, 204-210, 2004.01.
72. Fujimura, Y., Tachibana, H., and Yamada, K., Peroxisome proliferator-activated receptor (PPAR) ligands negatively regulate the expression of the high-affinity IgE receptor FcepsilonRI in human basophilic KU812 cells, Biochem. Biophys. Res. Commun., 10.1016/S0006-291X(02)02139-3, 297, 2, 193-201, 2002.05.
73. Fujimura, Y., Tachibana, H., Maeda-Yamamoto, M., Miyase, T., Sano, M., and Yamada, K., Antiallergic tea catechin, (-)-epigallocatechin-3-O-(3-O-methyl)-gallate, suppresses FcepsilonRI expression in human basophilic KU812 cells., J. Agric. Food Chem., 10.1021/jf025680z, 50, 20, 5729-5734, 2002.05.
74. Fujimura, Y., Tachibana, H., and Yamada, K., Downregulation of high affinity IgE receptor FcepsilonRI expression in the human basophilic KU812 cells by a tea catechin, Animal Cell Technology, 12, 365-370, 2002.05.
75. Fujimura, Y., Tachibana, H., and Yamada, K., A tea catechin suppresses the expression of the high-affinity IgE receptor FcepsilonRI in human basophilic KU812 cells, J. Agric. Food Chem., 10.1021/jf001392w, 49, 5, 2527-2531, 2001.05.
76. Fujimura, Y., Tachibana, H., Eto, N., and Yamada, K., Antigen binding of an ovomucoid specific antibody is affected by a carbohydrate chain located on the light chain variable region, Biosci. Biotechnol. Biochem., 10.1271/bbb.64.2298, 64, 11, 2298-2305, 2000.05.
1. Fujimura Y, Miura D, Tachibana H, Metabolic Profiling Strategy for the Bioactivity Evaluation of Green Tea and the Selection of Bioactivity-related Chemical Combinations, The 3rd Symposium of Kyoto Biomolecular Mass Spectrometry Society, 2019.02.
2. Yoshinori Fujimura, Hirofumi Tachibana, The biological function of tea via EGCG receptor, The 2014 Annual Meeting and Symposium of Health Food Science of Taiwan, 2014.03.
3. Yoshinori Fujimura, Metabolomics-driven chemical sensing strategy for better understanding of functions of green tea, 2014 Water-Algae-Tea Consortium for Health (WATCH), 2014.03.
Membership in Academic Society
  • Japanese Society of Catechinology
  • Japanese Society for Food Factors