Papers - IDA Takanori
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The role of neuromedin U during inflammatory response in the common carp Reviewed
Kono T., Hamasuna S., Korenaga H., Iizasa T., Nagamine R., Ida T., Sakai M.
Fish and Shellfish Immunology 32 ( 1 ) 151 - 160 2012.1
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Fish and Shellfish Immunology
In the current study, we cloned and characterized the neuromedin U (NMU) gene from the common carp Cyprinus carpio L., and identified its participation in immune responses in the teleost. Five isoforms of the preproNMU genes were generated by alternative splicing and isolated from carp. The longest form of the carp preproNMU1 (isoform 1) cDNA was composed of 803 bp, and contained an 18 bp 5'-UTR, a 212 bp 3'-UTR and a 573 bp open reading frame, which translates into a peptide comprising 190 amino acid (aa) residues. The remaining carp preproNMU isoforms were composed of 175 (preproNMU2), 158 (preproNMU3), 150 (preproNMU4) and 133 (preproNMU5) aa residues. Isoforms 1-3 contained four processing signals (KR or RR), while isoforms 4 and 5 contained only two processing signals. High homology was demonstrated among fish and other vertebral NMU at the biologically active C-terminal region (aa position 175-182). Carp preproNMU transcript variants were identified in various tissues, and the expression pattern has been shown to change depending on feeding status. Moreover, it was shown that the expression of preproNMU3 and preproNMU5 was increased following treatment with bacterial or viral mimics. Finally, we investigated the functional aspect of carp NMU using a synthetic NMU peptide. The peptide was found to increase the expression of inflammation-related cytokine genes in intestinal cells within 1 h of treatment. In addition, the activation of phagocytic cells was also stimulated by the NMU peptide. The discovery of NMU in carp allows for a further understanding of immune regulation by biologically active substances. © 2011 Elsevier Ltd.
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2. 年少児・障がい者に対するアニマル・セラピーの試み(シンポジウム「各ライフステージでの特色ある心理・心身医学的手法の実践と成果」,第49回日本心身医学会九州地方会演題抄録(1))
久富 一郎, 津輪元 修一, 井田 隆徳, 秋坂 真史
心身医学 52 ( 8 ) 2012
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：一般社団法人 日本心身医学会
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Variety of acyl modifications in mammalian ghrelins. Reviewed
Ida T
Methods in enzymology 514 63 - 73 2012
Language：Japanese Publishing type：Research paper (scientific journal)
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HIRAGUCHI Tetsutaro, MAEDA Toru, SHIOTANI Hajime, IDA Takanori, KOJIMA Masayasu, OZAKI Mamiko
The Japanese journal of taste and smell research 18 ( 3 ) 295 - 298 2011.12
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：The Japanese Association for the Study of Taste and Smell
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Ida T., Takahashi T., Tominaga H., Sato T., Kume K., Yoshizawa-Kumagaye K., Nishio H., Kato J., Murakami N., Miyazato M., Kangawa K., Kojima M.
Biochemical and Biophysical Research Communications 414 ( 1 ) 44 - 48 2011.10
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Biochemical and Biophysical Research Communications
There are many orphan G protein-coupled receptors (GPCRs), for which ligands have not yet been identified, in both vertebrates and invertebrates, such as Drosophila melanogaster. Identification of their cognate ligands is critical for understanding the function and regulation of such GPCRs. Indeed, the discovery of bioactive peptides that bind GPCRs has enhanced our understanding of mechanisms underlying many physiological processes. Here, we identified an endogenous ligand of the Drosophila orphan GPCR, CG34381. The purified ligand is a peptide comprised of 28 amino acids with three intrachain disulfide bonds. The preprotein is coded for by gene CG14871. We designated the cysteine-rich peptide " trissin" (it means for triple S-S bonds) and characterized the structure of intrachain disulfide bonds formation in a synthetic trissin peptide. Because the expression of trissin and its receptor is reported to predominantly localize to the brain and thoracicoabdominal ganglion, trissin is expected to behave as a neuropeptide. The discovery of trissin provides an important lead to aid our understanding of cysteine-rich peptides and their functional interaction with GPCRs. © 2011 Elsevier Inc.
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Ida T., Takahashi T., Tominaga H., Sato T., Kume K., Ozaki M., Hiraguchi T., Maeda T., Shiotani H., Terajima S., Sano H., Mori K., Yoshida M., Miyazato M., Kato J., Murakami N., Kangawa K., Kojima M.
Biochemical and Biophysical Research Communications 410 ( 4 ) 872 - 877 2011.7
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Biochemical and Biophysical Research Communications
A number of bioactive peptides are involved in regulating a wide range of animal behaviors, including food consumption. Vertebrate neuropeptide Y (NPY) is a potent stimulator of appetitive behavior. Recently, Drosophila neuropeptide F (dNPF) and short NPF (sNPF), the Drosophila homologs of the vertebrate NPY, were identified to characterize the functions of NPFs in the feeding behaviors of this insect. Dm-NPFR1 and NPFR76F are the receptors for dNPF and sNPF, respectively; both receptors are G protein-coupled receptors (GPCRs). Another GPCR (CG5811; NepYR) was indentified in Drosophila as a neuropeptide Y-like receptor. Here, we identified 2 ligands of CG5811, dRYamide-1 and dRYamide-2. Both peptides are derived from the same precursor (CG40733) and have no significant structural similarities to known bioactive peptides. The C-terminal sequence RYamide of dRYamides is identical to that of NPY family peptides; on the other hand, dNPF and sNPF have C-terminal RFamide. When administered to blowflies, dRYamide-1 suppressed feeding motivation. We propose that dRYamides are related to the NPY family in vertebrates, similar to dNPF and sNPF. © 2011 Elsevier Inc.
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Sato T., Nakashima Y., Nakamura Y., Ida T., Kojima M.
Journal of Molecular Neuroscience 43 ( 2 ) 193 - 199 2011.2
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Journal of Molecular Neuroscience
Ghrelin is a hormone that mediates a variety of physiological roles, such as stimulating appetite, initiating food intake, and modulating energy metabolism. Although it has been reported that a bolus injection of ghrelin decreases blood pressure, the effect of continuous ghrelin administration on vasoregulation has yet to be determined. We examined the longitudinal effect of ghrelin on vasoregulation using Dahl-Iwai salt-sensitive rats. In this model, a high-salt diet induced high blood pressure and increased ghrelin levels but reduced food intake. In salt-sensitive hypertension, cumulative food intake decreased, while both ghrelin messenger RNA levels and plasma ghrelin content increased. Continuous administration of a ghrelin receptor agonist, growth hormone releasing peptide-6 (GHRP-6), for 2 weeks by mini-osmotic pump did not change blood pressure values although the cumulative food intake recovered. In contrast, continuous administration of a ghrelin receptor antagonist, [D-Lys 3 ]-GHRP-6, induced early elevations in blood pressure without changes in heart rate. Quantitative RT-PCR revealed high expression levels of genes involved in the catecholamine biosynthetic pathway, tyrosine hydroxylase and dopamine-β-hydroxylase, after continuous [D-Lys 3 ]-GHRP-6 administration. These results indicate that continuous antagonism of the ghrelin receptor results in early induction of salt-sensitive hypertension in this animal model and suggests that increases in autonomic nervous activity induced by ghrelin receptor antagonism are responsible, as indicated by the high expression levels of genes in the catecholamine biosynthetic pathway. © 2010 Springer Science+Business Media, LLC.
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Comparison of feeding suppression by the anorexigenic hormones neuromedin U and neuromedin S in rats Reviewed
Nakahara K., Katayama T., Maruyama K., Ida T., Mori K., Miyazato M., Kangawa K., Murakami N.
Journal of Endocrinology 207 ( 2 ) 185 - 193 2010.11
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Journal of Endocrinology
We compared the central mechanisms of feeding suppression by the anorexigenic hormones neuromedin U (NMU) and neuromedin S (NMS) in rats. I.c.v. injection of either NMU or NMS dose dependently decreased 3-h food intake during the first quarter of a dark period. Pretreatment involving i.c.v. injection of a specific anti-NMS IgG blocked the suppression of food intake induced by i.c.v.- and i.p.-injected leptin, but anti-NMU IgG elicited no blockade. Quantitative PCR analysis revealed that i.c.v. injection of NMU or NMS caused a dose-dependent increase in CRH and proopiomelanocortin mRNA expression in the paraventricular nucleus (PVN) and arcuate nucleus (Arc) respectively. In tissue cultures of the Arc, secretion of α-melanocyte-stimulating hormone was stimulated by NMU and NMS, with more potent stimulation by NMS. The time-course curves of the increase in neuronal firing rate in Arc slices in response to NMU and NMS showed almost the same pattern, with a peak 10-15 min after treatment, whereas the time-course curves for the PVN slices differed between NMU and NMS. These results suggest that NMS and NMU may share anorexigenic effects, depending on physiological conditions. © 2010 Society for Endocrinology.
DOI： 10.1677/JOE-10-0081
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Purification and characterization of caprine ghrelin and its effect on growth hormone release Reviewed
Ida T., Miyazato M., Lin X., Kaiya H., Sato T., Nakahara K., Murakami N., Kangawa K., Kojima M.
Journal of Molecular Neuroscience 42 ( 1 ) 99 - 105 2010.9
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Journal of Molecular Neuroscience
Ghrelin, a novel peptide modified by n-octanoic acid at the third serine residue (Ser 3 ), serves as an endogenous ligand for the growth hormone secretagogue receptor (GHS-R) 1a. The octanoyl modification at Ser 3 is essential for receptor binding or growth hormone release. Here, we report the purification of caprine ghrelin and its physiological role in goats. The major form of caprine ghrelin is a 27 amino acid peptide that is octanoylated (C8:0) at Ser 3 and lacks Gln 14 , which is present in rat and human ghrelin. Additionally, we identified various acyl modifications in caprine ghrelin: nonanoic (C9:0), decanoic (10:0), unsaturated octanoic acids (C8:1), and an unidentified fatty acid modification. We observed that differences in acyl modifications affected GHS-R1a activation. In addition, administration of synthetic bovine ghrelin increased plasma growth hormone (GH) levels in goats. Thus, the present study indicates a structural divergence in caprine ghrelin and suggests that ghrelin is involved in GH release in ruminants. © 2010 Springer Science+Business Media, LLC.
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Neuromedin U is necessary for normal gastrointestinal motility and is regulated by serotonin Reviewed
Nakashima Y., Ida T., Sato T., Nakamura Y., Takahashi T., Mori K., Miyazato M., Kangawa K., Kusukawa J., Kojima M.
Annals of the New York Academy of Sciences 1200 104 - 111 2010.7
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Annals of the New York Academy of Sciences
Neuromedin U (NMU) was originally isolated from porcine spinal cord and shown to be distributed in numerous tissues, including the gastrointestinal tract. However, little is known about the role of NMU in the regulation of gastrointestinal functions. We established a radioimmunoassay system that is exceptionally specific for mouse NMU and found high NMU content in the gastrointestinal tract, particularly in the Auerbach's and Meissner's plexi, suggesting a possible role of NMU in gastrointestinal motility. NMU promoted small intestinal transit, and NMU deficiency resulted in lowered intestinal motility rate and diminished the effect of serotonin-induced defecation and diarrhea. These results indicate that NMU promotes intestinal transit and maintains intestinal homeostasis. © 2010 New York Academy of Sciences.
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Takahashi T., Ida T., Sato T., Nakashima Y., Nakamura Y., Tsuji A., Kojima M.
Journal of Biochemistry 146 ( 5 ) 675 - 682 2009.11
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Journal of Biochemistry
Ghrelin was originally isolated from rat stomach as an endogenous ligand for the GH secretagogue receptor. The major active form of ghrelin is a 28-amino acid peptide modified by an n-octanoic acid on the serine 3 residue, and this lipid modification is essential for the biological activity of ghrelin. However, it is not clear whether prohormone convertase (PC) and ghrelin O-acyltransferase (GOAT) are the minimal requirements for synthesis of acyl-modified ghrelin in cultured cells. By using three cultured cell lines, TT, AtT20 and COS-7, in which the expression levels of processing proteases and GOAT vary, we examined the processing patterns of ghrelin precursor. We found that not only PC1/3 but also both PC2 and furin could process proghrelin to the 28-amino acid ghrelin. Moreover, the presence of PC and GOAT in the cells, as well as n-octanoic acid in the culture medium, was necessary to produce n-octanoyl ghrelin.
DOI： 10.1093/jb/mvp112
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Ohgusu H., Shirouzu K., Nakamura Y., Nakashima Y., Ida T., Sato T., Kojima M.
Biochemical and Biophysical Research Communications 386 ( 1 ) 153 - 158 2009.8
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Biochemical and Biophysical Research Communications
Ghrelin is a peptide hormone in which serine 3 is modified by n-octanoic acid through GOAT (ghrelin O-acyltransferase). However, the enzymological properties of GOAT remain to be elucidated. We analyzed the in vitro activity of GOAT using the recombinant enzyme. Unexpectedly, although the main active form of ghrelin is modified by n-octanoic acid, GOAT had a strong preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor. Moreover, a four-amino acid peptide derived from the N-terminal sequence of ghrelin can be modified by GOAT, indicating that these four amino acids constitute the core motif for substrate recognition by the enzyme. © 2009 Elsevier Inc. All rights reserved.
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Miyazato M., Mori K., Ida T., Kojima M., Murakami N., Kangawa K.
Regulatory Peptides 145 ( 1-3 ) 37 - 41 2008.1
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Regulatory Peptides
We identified a novel 36-amino acid neuropeptide in rat brain as an endogenous ligand for the G protein-coupled receptors FM-3/GPR66 and FM-4/TGR-1, which were identified to date as the neuromedin U (NMU) receptors, and designated this peptide neuromedin S (NMS) because it was specifically expressed in the suprachiasmatic nucleus (SCN) of the hypothalamus. NMS shared a C-terminal core structure with NMU. NMS mRNA was highly expressed in the central nervous system, spleen and testis. In rat brain, NMS expression was restricted to the ventrolateral portion of the SCN and has a diurnal peak under light/dark cycling, but remains stable under constant darkness. Intracerebroventricular (ICV) administration of NMS in rats induced nonphotic type phase shifts in the circadian rhythm of locomotor activity. ICV injection of NMS also decreased 12-h food intake during the dark period in rats. This anorexigenic effect was more potent than that observed with the same dose of NMU. ICV administration of NMS increased proopiomelanocortin (POMC) mRNA expression in the arcuate nucleus (Arc) and corticotropin-releasing hormone mRNA in the paraventricular nucleus, and induced c-Fos expression in the POMC neurons in the Arc. These findings suggest that NMS is implicated in the regulation of circadian rhythm and feeding behavior. © 2007 Elsevier B.V. All rights reserved.
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Ghrelin deficiency does not influence feeding performance Reviewed
Sato T., Kurokawa M., Nakashima Y., Ida T., Takahashi T., Fukue Y., Ikawa M., Okabe M., Kangawa K., Kojima M.
Regulatory Peptides 145 ( 1-3 ) 7 - 11 2008.1
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Regulatory Peptides
Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor that is synthesized predominantly in the stomach. Previous studies demonstrated that ghrelin stimulates growth hormone release and food intake. These data suggested that antagonism of ghrelin could serve as a useful treatment for eating disorders and obesity. To study the role of endogenous ghrelin in feeding performance further, we generated ghrelin-deficient (ghrl -/- ) mice. Unexpectedly, ghrl -/- mice exhibited normal growth, cumulative food intake, reproduction, histological characters, and serum parameters. There were no differences in feeding patterns between ghrl +/+ and ghrl -/- mice. Ghrl -/- mice displayed normal responses to scheduled feedings as seen for ghrl +/+ mice. Memory-related feeding performances of ghrl -/- mice were indistinguishable from ghrl +/+ littermates. These data indicate that ghrelin is not critical for feeding performance. © 2007 Elsevier B.V. All rights reserved.
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Identification and functional analysis of a novel ligand for G protein-coupled receptor, Neuromedin S Reviewed
Miyazato M, et al.
Regul Pept 145 ( 1-3 ) 37 - 41 2008.1
Language：English Publishing type：Research paper (scientific journal)
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Structure of Mammalian and Nonmammalian Ghrelins Reviewed
Kojima M., Ida T., Sato T.
Vitamins and Hormones 77 31 - 46 2007.11
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Vitamins and Hormones
The discovery of ghrelin has elucidated the role of the stomach as an important organ in the regulation of growth hormone (GH) release and energy homeostasis. Ghrelin is a peptide hormone in which Ser3 Thr3 in frogs) is modified by an n-octanoic acid; this modification is essential for ghrelin's activity. Ghrelin and motilin, another gastric peptide, structurally and functionally define a peptide superfamily; these two factors may have evolved from a common ancestral peptide. Ghrelin is found in both mammalian species as well as nonmammalian species, such as frogs, birds, and fish. Moreover, ghrelin structure, particularly that of the acyl-modification regions, is highly conserved throughout vertebrate species. All of the ghrelin peptides that have been identified are modified by a fatty acid, primarily n-octanoic acid. These discoveries implicate ghrelin as an essential hormone in the maintenance of GH release and energy homeostasis in vertebrates. © 2007 Elsevier Inc. All rights reserved.
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Central control of bone remodeling by neuromedin U Reviewed
Sato S., Hanada R., Kimura A., Abe T., Matsumoto T., Iwasaki M., Inose H., Ida T., Mieda M., Takeuchi Y., Fukumoto S., Fujita T., Kato S., Kangawa K., Kojima M., Shinomiya K., Takeda S.
Nature Medicine 13 ( 10 ) 1234 - 1240 2007.10
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Nature Medicine
Bone remodeling, the function affected in osteoporosis, the most common of bone diseases, comprises two phases: bone formation by matrix-producing osteoblasts and bone resorption by osteoclasts. The demonstration that the anorexigenic hormone leptin inhibits bone formation through a hypothalamic relay suggests that other molecules that affect energy metabolism in the hypothalamus could also modulate bone mass. Neuromedin U (NMU) is an anorexigenic neuropeptide that acts independently of leptin through poorly defined mechanisms. Here we show that Nmu-deficient (Nmu -/- ) mice have high bone mass owing to an increase in bone formation; this is more prominent in male mice than female mice. Physiological and cell-based assays indicate that NMU acts in the central nervous system, rather than directly on bone cells, to regulate bone remodeling. Notably, leptin- or sympathetic nervous system-mediated inhibition of bone formation was abolished in Nmu -/- mice, which show an altered bone expression of molecular clock genes (mediators of the inhibition of bone formation by leptin). Moreover, treatment of wild-type mice with a natural agonist for the NMU receptor decreased bone mass. Collectively, these results suggest that NMU may be the first central mediator of leptin-dependent regulation of bone mass identified to date. Given the existence of inhibitors and activators of NMU action, our results may influence the treatment of diseases involving low bone mass, such as osteoporosis. © 2007 Nature Publishing Group.
DOI： 10.1038/nm1640
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Purification and characterization of feline ghrelin and its possible role Reviewed
Ida T., Miyazato M., Naganobu K., Nakahara K., Sato M., Lin X., Kaiya H., Doi K., Noda S., Kubo A., Murakami N., Kangawa K.
Domestic Animal Endocrinology 32 ( 2 ) 93 - 105 2007.2
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Domestic Animal Endocrinology
Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3 , has been isolated from rat and human stomach as an endogenous ligand for the growth hormone secretagogue receptor. Here, we purified feline ghrelin and examined its possible physiological role in cats. The major active form of feline ghrelin is a 28-amino acid peptide octanoylated (C8:0) at Ser 3 ; except for one amino acid residue replacement, this structure is identical to those of rat and human ghrelins. However, much structural divergence in peptide length and fatty acid modification was observed in feline ghrelin: peptides consisting of 27 or 26 amino acids lacking Gln 14 and/or Arg 28 were found, and the third serine residue was modified by octanoic acid (C8:0), decanoic acid (10:0), or unsaturated fatty acids (C8:1, C10:1 and C10:2). In agreement with the structural divergence, two kinds of cDNA with different lengths were isolated. Administration of synthetic rat ghrelin increased plasma growth hormone levels in cats, with a potency similar to that in rat or human. Plasma levels of ghrelin in cats increased approximately 2.5-fold after fasting. The present s tudy indicates the existence of structural divergence in feline ghrelin and suggests that, as in other animals, ghrelin may play important roles in GH release and feeding in cats. © 2006 Elsevier Inc. All rights reserved.
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Date Y., Shimbara T., Koda S., Toshinai K., Ida T., Murakami N., Miyazato M., Kokame K., Ishizuka Y., Ishida Y., Kageyama H., Shioda S., Kangawa K., Nakazato M.
Cell Metabolism 4 ( 4 ) 323 - 331 2006.10
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Cell Metabolism
Ghrelin, a gastrointestinal peptide, stimulates feeding when administered peripherally. Blockade of the vagal afferent pathway abolishes ghrelin-induced feeding, indicating that the vagal afferent pathway may be a route conveying orexigenic ghrelin signals to the brain. Here, we demonstrate that peripheral ghrelin signaling, which travels to the nucleus tractus solitarius (NTS) at least in part via the vagus nerve, increases noradrenaline (NA) in the arcuate nucleus of the hypothalamus, thereby stimulating feeding at least partially through α- 1 and β- 2 noradrenergic receptors. In addition, bilateral midbrain transections rostral to the NTS, or toxin-induced loss of neurons in the hindbrain that express dopamine β hydroxylase (an NA synthetic enzyme), abolished ghrelin-induced feeding. These findings provide new evidence that the noradrenergic system is necessary in the central control of feeding behavior by peripherally administered ghrelin. © 2006 Elsevier Inc. All rights reserved.
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Neuromedin S is a novel anorexigenic hormone Reviewed
Ida T., Mori K., Miyazato M., Egi Y., Abe S., Nakahara K., Nishihara M., Kangawa K., Murakami N.
Endocrinology 146 ( 10 ) 4217 - 4223 2005.10
Language：Japanese Publishing type：Research paper (scientific journal) Publisher：Endocrinology
A novel 36-amino acid neuropeptide, neuromedin S (NMS), has recently been identified in rat brain and has been shown to be an endogenous ligand for two orphan G protein-coupled receptors, FM-3/GPR66 and FM-4/TGR-1. These receptors have been identified as neuromedin U (NMU) receptor type 1 and type 2, respectively. In this study, the physiological role of the novel peptide, NMS, on feeding regulation was investigated. Intracerebroventricular (icv) injection of NMS decreased 12-h food intake during the dark period in rats. This anorexigenic effect was more potent and persistent than that observed with the same dose of NMU. Neuropeptide Y, ghrelin, and agouti-related protein-induced food intake was counteracted by co-administration of NMS. Icv administration of NMS increased proopiomelanocortin mRNA expression in the arcuate nucleus (Arc) and CRH mRNA in the paraventricular nucleus (PVN). Pretreatment with SHU9119 (antagonist for α-MSH) and α-helical corticotropin-releasing factor-(9-41) (antagonist for CRH) attenuated NMS-induced suppression of 24-h food intake. After icv injection of NMS, Fos-immunoreactive cells were detected in both the PVN and Arc. When neuronal multiple unit activity was recorded in the PVN before and after icv injection of NMS, a significant increase in firing rate was observed 5 min after administration, and this increase continued for 100 min. These results suggest that the novel peptide, NMS, may be a potent anorexigenic hormone in the hypothalamus, and that expression of proopiomelanocortin mRNA in the Arc and CRH mRNA in the PVN may be involved in NMS action on feeding. Copyright © 2005 by The Endocrine Society.
DOI： 10.1210/en.2005-0107