Papers - IDA Takanori
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Searching for peptide hormones
Ida T
Abstracts for Annual Meeting of Japanese Proteomics Society 2019 ( 0 ) 148 - 148 2019
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Japanese Proteomics Society (Japan Human Proteome Organisation)
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Fujiwara Y., Hermann-Luibl C., Katsura M., Sekiguchi M., Ida T., Helfrich-Förster C., Yoshii T.
Frontiers in Physiology 9 ( SEP ) 1276 2018.9
Language：English Publishing type：Research paper (scientific journal) Publisher：Frontiers in Physiology
© 2018 Fujiwara, Hermann-Luibl, Katsura, Sekiguchi, Ida, Helfrich-Förster and Yoshii. The fruit fly Drosophila melanogaster possesses approximately 150 brain clock neurons that control circadian behavioral rhythms. Even though individual clock neurons have self-sustaining oscillators, they interact and synchronize with each other through a network. However, little is known regarding the factors responsible for these network interactions. In this study, we investigated the role of CCHamide1 (CCHa1), a neuropeptide expressed in the anterior dorsal neuron 1 (DN1a), in intercellular communication of the clock neurons. We observed that CCHa1 connects the DN1a clock neurons to the ventral lateral clock neurons (LNv) via the CCHa1 receptor, which is a homolog of the gastrin-releasing peptide receptor playing a role in circadian intercellular communications in mammals. CCHa1 knockout or knockdown flies have a generally low activity level with a special reduction of morning activity. In addition, they exhibit advanced morning activity under light-dark cycles and delayed activity under constant dark conditions, which correlates with an advance/delay of PAR domain Protein 1 (PDP1) oscillations in the small-LNv (s-LNv) neurons that control morning activity. The terminals of the s-LNv neurons show rather high levels of Pigment-dispersing factor (PDF) in the evening, when PDF is low in control flies, suggesting that the knockdown of CCHa1 leads to increased PDF release; PDF signals the other clock neurons and evidently increases the amplitude of their PDP1 cycling. A previous study showed that high-amplitude PDP1 cycling increases the siesta of the flies, and indeed, CCHa1 knockout or knockdown flies exhibit a longer siesta than control flies. The DN1a neurons are known to be receptive to PDF signaling from the s-LNv neurons; thus, our results suggest that the DN1a and s-LNv clock neurons are reciprocally coupled via the neuropeptides CCHa1 and PDF, and this interaction fine-tunes the timing of activity and sleep.
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Interleukin-15 derived from Guanylin-GC-C-expressing macrophages inhibits fatty acid synthase in adipocytes. Reviewed
Akieda-Asai S, Ida T, Miyazato M, Kangawa K, Date Y
Peptides 99 14 - 19 2017.10
Language：English Publishing type：Research paper (scientific journal)
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Role of neuromedin U in accelerating of non-alcoholic steatohepatitis in mice. Reviewed
Teranishi H, Hayashi M, Higa R, Mori K, Miyazawa T, Hino J, Amano Y, Tozawa R, Ida T, Hanada T, Miyazato M, Hanada R, Kangawa K, Nakao K
Peptides 2017.10
Language：English Publishing type：Research paper (scientific journal)
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Identification of neuromedin U precursor-related peptide and its possible role in the regulation of prolactin release. Reviewed
Mori K, Ida T, Fudetani M, Mori M, Kaiya H, Hino J, Nakahara K, Murakami N, Miyazato M, Kangawa K
Scientific reports 7 ( 1 ) 10468 2017.9
Language：English Publishing type：Research paper (scientific journal)
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Luqin-like RYamide peptides regulate food-evoked responses in C. elegans. Reviewed
Ohno H, Yoshida M, Sato T, Kato J, Miyazato M, Kojima M, Ida T, Iino Y
eLife 6 2017.8
Language：English Publishing type：Research paper (scientific journal)
DOI： 10.7554/eLife.28877
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Kono T., Ida T., Kawahara N., Watanabe F., Biswas G., Sato T., Mori K., Miyazato M.
Developmental and Comparative Immunology 73 246 - 256 2017.8
Language：English Publishing type：Research paper (scientific journal) Publisher：Developmental and Comparative Immunology
© 2017 Elsevier Ltd In this study, immunoregulatory function of neuromedin U (Nmu) in the teleost fish Fugu (Takifugu rubripes) was characterized. Three splicing variants of nmu mRNA encoding preproNMUs consisting of 164 (Nmu1), 139 (Nmu2), and 129 (Nmu3) amino acid residues were found in Fugu.The biologically active C-terminal region of Fugu Nmu showed high homology among fish and other vertebrate NMUs. The genomic organization of Fugu nmu differed from those of zebrafish and mammals. However, in phylogenetic analysis, Fugu Nmu formed a cluster with NMUs of other vertebrates, in addition to neuromedin S. The splicing variants of mRNA were identified in various tissues. Nmu-21 and Nmu-9 were purified as endogenous peptides from Fugu intestine. The synthetic Nmu-21 peptide activated phagocytic cells, and elevated the expression of cytokine mRNA in peripheral blood leukocytes.
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Mekata T., Kono T., Satoh J., Yoshida M., Mori K., Sato T., Miyazato M., Ida T.
General and Comparative Endocrinology 246 321 - 330 2017.5
Language：English Publishing type：Research paper (scientific journal) Publisher：General and Comparative Endocrinology
© 2017 To understand the regulation systems of appetite, bioactive peptides from the kuruma shrimp Marsupenaeus japonicus (Mj) were isolated and purified by reverse pharmacological assays using CHO cel ls expressing the Drosophila melanogaster G-protein-coupled receptors (GPCRs) CG5811 (a RYamide receptor) or CG14593 (a CCHamide-2 receptor). Four peptides having binding activity to GPCRs were obtained and named Mj RYamide-1, Mj RYamide-2, Mj RYamide-3, and Mj CCHamide. Genes encoding the prepropeptides of these peptides were identified using kuruma shrimp transcriptome databases. The Mj prepro-RYamide gene encodes a 130-amino acid polypeptide containing Mj RYamide-1, Mj RYamide-2, and Mj RYamide-3, whereas the Mj prepro-CCHamide gene encodes a 119-amino acid polypeptide containing a single Mj CCHamide peptide. The expression of these genes was confirmed in various neuronal organs including the brain and ventral nerve cord. In addition, prepro-RYamide gene expression is significantly reduced in the brain after starvation. RYamides may thus be associated with regulation of feeding or digestion. Changes in kayak (the c-fos ortholog in invertebrates) gene expression after administration of synthetic peptides were also investigated. Mj kayak expression levels are upregulated in hepatopancreas after treatment with Mj RYamide-3 or CCHamide. Thus, the peptides isolated in this study may have some regulatory effect on cellular metabolism in aquacultured invertebrates.
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Role of biological rhythms in the performance of physical activity Reviewed
Sato Takahiro, Ida Takanori, Kojima Masayasu
The Journal of Physical Fitness and Sports Medicine 6 ( 3 ) 125 - 134 2017
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：一般社団法人日本体力医学会
Most organisms display various periodicities. Periodicity has been observed in humans in association with sleep, body temperature and hormone secretion. The molecular mechanisms involved are being elucidated by the investigation of clock genes in mammals. The relationship between biological rhythms and disease is also being studied. For example, myocardial infarction occurs more frequently in the morning, and disruption of biological rhythm is associated with obesity and diabetes. Some drugs have different medicinal effects depending on the time of dosing. Drug therapy known as chronotherapy, that takes into account the diurnal rhythm found in a given target disease, is being administered in some cases. Moreover, physiological responses and metabolism differ with time. Therefore, understanding the mechanisms underlying biological rhythms could enable the safe and effective performance of physical activity, in addition to potential medical applications. This review article outlines current understandings of biological rhythmicity and explores the relationship between biological rhythms and exercise, training, and sports.
DOI： 10.7600/jpfsm.6.125
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Suppressive effects of dRYamides on feeding behavior of the blowfly, Phormia regina Reviewed
Maeda T, Nakamura Y, Shiotani H, Hojo M, Yoshii T, Ida T, Sato T, Yoshida M, Miyazato M, Kojima M, Ozaki M
Zoological Letters 2015.9
Language：English Publishing type：Research paper (scientific journal)
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Physiological functions and pathology of ghrelin Reviewed
Sato T, Oishi K, Ida T, Kojima M
American Journal of Life Sciences 2015.5
Language：English Publishing type：Research paper (scientific journal)
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Sano H., Nakamura A., Texada M., Truman J., Ishimoto H., Kamikouchi A., Nibu Y., Kume K., Ida T., Kojima M.
PLoS Genetics 11 ( 5 ) e1005209 2015.5
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：PLoS Genetics
© 2015 Sano et al. The coordination of growth with nutritional status is essential for proper development and physiology. Nutritional information is mostly perceived by peripheral organs before being relayed to the brain, which modulates physiological responses. Hormonal signaling ensures this organ-to-organ communication, and the failure of endocrine regulation in humans can cause diseases including obesity and diabetes. In Drosophila melanogaster, the fat body (adipose tissue) has been suggested to play an important role in coupling growth with nutritional status. Here, we show that the peripheral tissue-derived peptide hormone CCHamide-2 (CCHa2) acts as a nutrient-dependent regulator of Drosophila insulin-like peptides (Dilps). A BAC-based transgenic reporter revealed strong expression of CCHa2 receptor (CCHa2-R) in insulin-producing cells (IPCs) in the brain. Calcium imaging of brain explants and IPC-specific CCHa2-R knockdown demonstrated that peripheral-tissue derived CCHa2 directly activates IPCs. Interestingly, genetic disruption of either CCHa2 or CCHa2-R caused almost identical defects in larval growth and developmental timing. Consistent with these phenotypes, the expression of dilp5, and the release of both Dilp2 and Dilp5, were severely reduced. Furthermore, transcription of CCHa2 is altered in response to nutritional levels, particularly of glucose. These findings demonstrate that CCHa2 and CCHa2-R form a direct link between peripheral tissues and the brain, and that this pathway is essential for the coordination of systemic growth with nutritional availability. A mammalian homologue of CCHa2-R, Bombesin receptor subtype-3 (Brs3), is an orphan receptor that is expressed in the islet β-cells; however, the role of Brs3 in insulin regulation remains elusive. Our genetic approach in Drosophila melanogaster provides the first evidence, to our knowledge, that bombesin receptor signaling with its endogenous ligand promotes insulin production.
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Identification and application of Drosophila novel bioactive peptides dRYamides Reviewed
Ida T, Iwamoto E, Sato T, Kojima M
American Journal of Life Sciences 2015.4
Language：English Publishing type：Research paper (scientific journal)
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Suppressive effects of dRYamides on feeding behavior of the blowfly, Phormia regina. Reviewed
Maeda T, Nakamura Y, Shiotani H, Hojo MK, Yoshii T, Ida T, Sato T, Yoshida M, Miyazato M, Kojima M, Ozaki M
Zoological letters 1 35 2015
Language：Japanese Publishing type：Research paper (scientific journal)
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Physiological roles of ghrelin on obesity Reviewed
Sato T., Ida T., Nakamura Y., Shiimura Y., Kangawa K., Kojima M.
Obesity Research and Clinical Practice 8 ( 5 ) e405 - e413 2014.9
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Obesity Research and Clinical Practice
© 2013 Asian Oceanian Association for the Study of Obesity. Ghrelin is a stomach hormone that acts as an endogenous ligand of orphan G-protein coupled receptor. Ghrelin has various physiological functions, such as the stimulation of growth hormone release and of appetite, and fat accumulation. Ghrelin is the only peripheral hormone to transmit satiety signal. Mature ghrelin peptide is consisted of 28 amino acid residues, and is unusual among peptide hormones in that Ser3 is n-octanoylated to obtain. Furthermore, this modification is essential for ghrelin's activity. In order to add this side chain to acyl ghrelin, it is necessary for the recently discovered enzyme, ghrelin-O-acyl transferase (GOAT). Therefore, to understand of ghrelin's functions, it is useful to obtain the knowledge on structures and functions of ghrelin, ghrelin receptor and GOAT. Here, we review our current understanding of the structures and functions of ghrelin, and the relation between obesity and ghrelin. Finally, we referred to the ghrelin and related substances as a drug design target for obesity.
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More Drosophila enteroendocrine peptides: Orcokinin B and the CCHamides 1 and 2 Reviewed
Veenstra JA, Ida T
Cell Tisuue Res 357 ( 3 ) 607 - 621 2014.5
Language：English Publishing type：Research paper (scientific journal)
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Mori M., Mori K., Ida T., Sato T., Kojima M., Miyazato M., Kangawa K.
Frontiers in Endocrinology 3 ( DEC ) 2012.12
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Frontiers in Endocrinology
Neuromedin S (NMS) is a neuropeptide identified as another endogenous ligand for two orphan G protein-coupled receptors, FM-3/GPR66 and FM-4/TGR-1, which have also been identifiedastypes1and2receptorsforneuromedinUstructurallyrelatedtoNMS.Although expressionofNMSmRNAisfoundmainlyinthebrain, spleen, andtestis, thedistributionof itspeptidehasnotyetbeeninvestigated. Usinganewlypreparedantiserum, wedeveloped a highly sensitive radioimmunoassay for rat NMS. NMS peptide was clearly detected in the ratbrainataconcentrationof68.3±3.4fmol/gwetweight, butitwashardlydetectedinthe spleenandtestis.AhighcontentofNMSpeptidewasfoundinthehypothalamus, midbrain, and pons-medulla oblongata, whereas abundant expression of NMS mRNA was detected only in the hypothalamus.These differing distributions of the mRNA and peptide suggest that nerve fibers originating from hypothalamic NMS neurons project into the midbrain, pons, or medulla oblongata. In addition, abundant expression of type 2 receptor mRNA was detected not only in the hypothalamus, but also in the midbrain and pons-medulla oblongata. These results suggest novel, unknown physiological roles of NMS within the brainstem. © 2012 Mori, Mori, Ida, Sato, Kojima, MiyazatoandKangawa.
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Ida T., Takahashi T., Tominaga H., Sato T., Sano H., Kume K., Ozaki M., Hiraguchi T., Shiotani H., Terajima S., Nakamura Y., Mori K., Yoshida M., Kato J., Murakami N., Miyazato M., Kangawa K., Kojima M.
Frontiers in Endocrinology 3 ( DEC ) 177 2012.12
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Frontiers in Endocrinology
There are many orphan G protein-coupled receptors (GPCRs) for which ligands have not yet been identified. One such GPCR is the bombesin receptor subtype 3 (BRS-3). BRS-3 plays a role in the onset of diabetes and obesity. GPCRs in invertebrates are similar to those in vertebrates. Two Drosophila GPCRs (CG30106 and CG14593) belong to the BRS-3 phylogenetic subgroup. Here, we succeeded to biochemically purify the endogenous ligands of Drosophila CG30106 and CG14593 from whole Drosophila homogenates using functional assays with the reverse pharmacological technique, and identified their primary amino acid sequences.The purified ligands had been termed CCHamide-1 and CCHamide-2, although structurally identical to the peptides recently predicted from the genomic sequence searching. In addition, our biochemical characterization demonstrated two N-terminal extended forms of CCHamide-2.When administered to blowflies, CCHamide-2 increased their feeding motivation. Our results demonstrated these peptides actually present as the major components to activate these receptors in living Drosophila. Studies on the effects of CCHamides will facilitate the search for BRS-3 ligands. © 2012 Ida, Takahashi, Tom-inaga, Sato, Sano, Kume, Ozaki, Hiraguchi, Shiotani, Terajima, Naka-mura, Mori, Yoshida, Kato, Murakami, Miyazato, Kangawa and Kojima.
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Variety of acyl modifications in mammalian ghrelins. Reviewed
Ida T.
Methods in enzymology 514 63 - 73 2012.12
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Methods in enzymology
Ghrelin, a 28-amino acid-long peptide with an n-octanoyl modification at Ser(3), has been isolated from rat and human stomachs as an endogenous ligand for the growth hormone secretagogue receptor. It is very important to study the ghrelin from mammals (especially, domestic animals) that serve as human companions, food resources, and model organisms. We purified feline and caprine ghrelin and observed that the administration of synthetic ghrelin increased plasma growth hormone (GH) levels in cats and goats. Therefore, we believe that ghrelin may play important roles in GH release in mammals. Copyright © 2012 Elsevier Inc. All rights reserved.
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Different distribution of neuromedin S (NMS) and its mRNA in the rat brain: NMS peptide is present not only in the hypothalamus as the mRNA, but also in the brainstem Reviewed
Mori M, Mori K, Ida T, Sato T, Kojima M, Miyazato M, Kangawa K
Frontiers in Endocrinol 3 ( 152 ) 2012.1
Language：English Publishing type：Research paper (scientific journal)