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Tatsuya Moriyama has a total of 303 co-authors. Here are the top co-authors by number of shared publications:


Latest Publications

  • Open Access

    Identification of a Candidate IgE‐Binding Maize Protein in a Patient With Corn‐Dependent Exercise‐Induced Anaphylaxis: A Case Report

    by Ayako Goto, Nobue Takamatsu, Tatsuya Moriyama, Yasuto Kondo, Shinichiro Nagamitsu

    Corn‐dependent exercise‐induced anaphylaxis (food‐dependent exercise‐induced anaphylaxis [FDEIA]) is rare, and its causative allergens remain poorly defined. Here, we report a case of corn‐dependent FDEIA and investigate candidate IgE‐binding proteins using immunological and proteomic analyses. A 13‐year‐old boy with a history of buckwheat allergy developed recurrent anaphylaxis during exercise after ingesting corn‐containing foods. An exercise challenge after ingesting 272 g of sweet corn reproduced the symptoms and confirmed the diagnosis. Corn‐specific IgE was 3.72 UA/mL, and skin prick testing was positive. IgE immunoblotting revealed patient‐specific bands at ~45 and 60 kDa. Two‐dimensional immunoblotting and mass spectrometry identified globulin‐1S (GLB1) and other proteins as candidate IgE‐binding proteins in this patient. Sequence analysis revealed significant local sequence similarity between maize GLB1 and buckwheat Fag e 5 within the second cupin domain. These findings identify GLB1 as a candidate IgE‐binding protein in this patient with corn‐dependent FDEIA. Although sequence similarities were observed between maize GLB1 and buckwheat Fag e 5, their immunological and clinical significance remains unclear, and further studies are required to determine whether cross‐reactivity exists.

  • Open Access

    Soybean Allergen Detection for Hypoallergenicity Validation of Natto-A Fermented Soybean Food

    by Rikiya Shimada, Yohei Harada, Erika Yano, Nobuhiro Zaima, Tatsuya Moriyama


  • Commercial ELISA kits for soy protein determination: Characterization and compatibility

    by Rikiya Shimada, Erika Yano, Nobuhiro Zaima, Tatsuya Moriyama

    Soy protein has been approved in Japan as a Food for Specified Health Uses to lower serum cholesterol. A foreign-made soy protein ELISA kit has been proposed for quantifying soy protein levels. However, acquisition of this foreign-made product is time-consuming, making the product inconvenient for soy protein quantification in Japan. Therefore, as possible alternatives, we evaluated two commercial domestic ELISA kits, both of which quantify soy protein and specific allergens for food-allergen labeling. In this study, we compared antibody reactivity and soy protein levels in soy milk using these three types of ELISA kits (one foreign-made and two domestic ELISA kits). Per the results, we found that commercial domestic ELISA kit-derived soy protein levels could be converted to the soybean protein levels obtained from the foreign-made soy protein ELISA kit, through multiplication by specific factors.


  • Open Access

    Co-Application with Tannic Acid Prevents Transdermal Sensitization to Ovalbumin in Mice

    by Eri Izumi, Nana Tanahashi, Serina Kinugasa, Shota Hidaka, Nobuhiro Zaima, Tatsuya Moriyama

    Transdermal sensitization to allergens is of great concern as a sensitization route for food allergies. This skin-mediated invasion and sensitization to allergens is involved in skin barrier breakdown and inflammation, followed by the production of several kinds of cytokines. Cytokines such as thymic stromal lymphopoietin and thymus and activation-regulated chemokine are also involved. In this study, we investigated the suppressive effect of tannic acid (TA) on transdermal sensitization using ovalbumin (OVA), a major egg-white allergen. We also analyzed the mechanisms associated with the inhibitory effects of TA. The results showed that the co-application with TA prevents transdermal sensitization to OVA. As possible mechanisms, its anti-inflammatory and astringent effect on the skin and binding ability with the protein were considered. These results indicate that TA could be applied to cosmetics and lotions, which could suppress the transdermal sensitization to allergens.


  • Open Access

    Detection and Characterization of the Soybean Allergen Gly m 7 in Soybeans and Processed Soybean Foods

    by Ayano Fukuzumi, Naoki Tokumasu, Ayato Matsuo, Erika Yano, Nobuhiro Zaima, Tatsuya Moriyama

    Gly m 7, a novel soybean allergen, was recently reported. In this study, we attempted to detect Gly m 7 in various soybeans and processed soybean foods using raised anti-Gly m 7 antibodies and enzyme-linked streptavidin, specifically binding to the biotin moiety of Gly m 7. There was a large difference in Gly m 7 levels in various soybean-processed foods. When Gly m 7 levels were determined, all cultivars contained this allergen almost completely, but the biotin moiety detected by streptavidin varied, suggesting that biotinylated levels of Gly m 7 might differ among cultivars. The thermal stability of Gly m 7 was determined by heating soybean extracts. During detection using anti-peptide antibodies, detectable intact Gly m 7 was gradually reduced by heating. Gly m 7 was not detected by peptide or biotin detection in worm-wounded soybeans. Soybeans were immersed in distilled water as a pretreatment step for germination, and Gly m 7 levels were compared by immersion time (4–96 h). Intact Gly m 7 was rapidly degraded in detection by both peptide and biotin moieties. This suggested that Gly m 7 was degraded by some protease(s) during germination. These results would be useful for understanding the properties or risk assessment of Gly m 7, a newly discovered soybean allergen.


  • Anaphylaxis to lipid transfer protein from butterbur scape

    by Shunsuke Miura, Tatsuya Moriyama, Junko Yoshimura, Kaichi Umehara, Haruko Hino, Takahiko Tsunoda, Shinji Kagami

  • Open Access

    Kiwifruit defense protein, kiwellin (Act d 5) percutaneously sensitizes mouse models through the epidermal application of crude kiwifruit extract

    by Serina Kinugasa, Shota Hidaka, Serina Tanaka, Eri Izumi, Nobuhiro Zaima, Tatsuya Moriyama

    Background: Kiwifruit is a popular fruit consumed worldwide and is also used as a cosmetic ingredient. However, it is known to cause allergic reactions in humans. Recent studies have suggested an association between food allergy and food allergens entering the body via the skin. However, percutaneously sensitizing kiwifruit allergens have not been identified in human studies or in animal models. Objective: This study aimed to identify kiwifruit proteins that percutaneously sensitized mice through the epidermal application of crude extracts from green and gold kiwifruit on the dorsal skin, and serum IgE and IgG1 levels were used as sensitization markers. Design: BALB/c mice were back-shaved and their skin was exposed to crude extracts from green and gold kiwifruit that contained sodium dodecyl sulfate. Specific IgE and IgG1 antibodies generated and secreted in response to antigens were measured using enzyme-linked immunosorbent assay or immunoblotting. Results: Skin exposure to kiwifruit extract induced an increase in the levels of kiwifruit-specific IgE and IgG1, which are helper T cell 2-related allergenic antibodies in mice. These antibodies reacted with 18, 23, and 24 kDa proteins found in both green and gold kiwifruits. Thus, three percutaneously sensitizing allergens were identified and purified. Their amino acid sequences partially matched with that of kiwellin (Act d 5). Discussion and conclusion: Kiwellin has been identified as a plant defense-related protein. Interestingly, many plant allergens are biodefense-related proteins belonging to the pathogenesis-related protein family. Kiwellin, which was discovered to be a transdermal sensitizing antigen, might also be categorized as a biodefense-related protein. This study is the first to identify kiwellin (Act d 5) as a percutaneously sensitizing kiwifruit allergen in a mouse model.


  • Inhibitory Activities of Sulfur Compounds in Garlic Essential Oil against Alzheimer’s Disease-Related Enzymes and Their Distribution in the Mouse Brain

    by Yuri Yoshioka, Shinichi Matsumura, Masanori Morimoto, Yuki Takemoto, Chihiro Kishi, Tatsuya Moriyama, Nobuhiro Zaima

    Alzheimer’s disease (AD) is the most common neurodegenerative disease. Garlic reportedly has various physiological effects, including a role in protecting against dementia. However, the action mechanisms of garlic on AD are not entirely clear. In this study, we investigated the inhibitory activity of garlic essential oil (GEO) against AD-related enzymes and evaluated the distribution of active substances in GEO to the brain. We found that several sulfur compounds in GEO significantly inhibited AD-related enzymes. Sulfur compounds were detected in the serum and brain 6 h post administration. The ratios of allyl mercaptan (24.0 ± 3.9%) and allyl methyl sulfide (49.8 ± 15.6%) in the brain were significantly higher than those in GEO, while those of dimethyl trisulfide (0.89 ± 34.8%), allyl methyl trisulfide (0.41 ± 19.0%), and diallyl trisulfide (0.43 ± 72.8%) in the brain were significantly lower than those in GEO. Similar results were observed in the serum, suggesting that the organosulfur compounds were converted to allyl mercaptan or allyl methyl sulfide in the body. Although allyl mercaptan and allyl methyl sulfide are not the main components of GEO, they might be key molecules to understand the bioactivities of GEO in the body.


  • Open Access

    Ellagic Acid Suppresses ApoB Secretion and Enhances ApoA-1 Secretion from Human Hepatoma Cells, HepG2

    by Ayana Ieda, Maki Wada, Yuuki Moriyasu, Yuuko Okuno, Nobuhiro Zaima, Tatsuya Moriyama

    The effect of ellagic acid (EA), a naturally occurring polyphenolic compound, on the secretion of apolipoproteins from human hepatocytes, HepG2, was investigated. The levels of apoB and apoA-1 secreted in the cell culture medium were determined by sandwich ELISA. EA did not affect cell viability at the tested concentrations (up to 50 µM). EA suppressed the secretion of apoB and enhanced that of apoA-1 from HepG2 cells. However, cellular apoB levels were increased, suggesting that EA inhibited the trafficking of apoB during the process of secretion. In contrast, the increase in the cellular levels of apoA-1 was consistent with its secreted levels. These results indicate that EA inhibits the secretion of apoB from hepatocytes and increases the secretion of apoA-1. Both of these effects are beneficial for lipoprotein metabolism in the prevention of lifestyle-related diseases. The detailed mechanism underlying these effects of EA on lipoprotein metabolism should be elucidated in the future, but this naturally occurring polyphenolic compound might be antihyperlipidemic. Based on these results, EA is suggested as a candidate food-derived compound for the prevention of hyperlipidemia.


  • Open Access

    Validation of Antiobesity Effects of Black Soybean Seed Coat Powder Suitable as a Food Material: Comparisons with Conventional Yellow Soybean Seed Coat Powder

    by Yuuki Moriyasu, Chiho Fukumoto, Maki Wada, Erika Yano, Hiroshi Murase, Masatoshi Mizuno, Nobuhiro Zaima, Tatsuya Moriyama

    In this study, we fed obese model mice black soybean seed coat powder (BSCP) and evaluated the antiobesity effects. As a control, normal yellow soybean seed coat powder (YSCP) was used. C57BL/6J, a high-fat diet-induced obesity model mouse, was fed a high-fat diet containing BSCP or YSCP (20% fat) to induce obesity. The results showed that in the BSCP group, it caused significant suppression of body weight gain and suppression of white adipose tissue weight compared with the YSCP group. Moreover, it significantly decreased serum leptin levels, which correlated with visceral fat mass, and increased antidiabetic adipocytokine and adiponectin levels. Therefore, this suggests the pigmented components contained in BSCP have an antiobesity effect in obese model mice. It is suggested that this material, which can be prepared without extraction with an organic solvent and is suitable for use as a food material, could be a functional food material with a practicable antiobesity effect.