Papers - MOMOTA Ryusuke

長鎖型XVIII型コラーゲンは新規膜結合型コラーゲンである可能性が高い

上野 智規, 米澤 朋子, 百田 龍輔, 佐々木 隆子, 大橋 俊孝, 水野 一乘

日本結合組織学会学術大会プログラム・抄録集   55回   147 - 147   2023.6

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XVIII型コラーゲン欠損マウスにおける皮膚創傷治癒の解析

米澤 朋子, 前川 明日華, 前場 崇宏, 百田 龍輔, 渋谷 千晶, 岩田 宗一郎, 大野 充昭, 大橋 俊孝

日本結合組織学会学術大会プログラム・抄録集   54回   119 - 119   2022.6

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Lack of collagen α6(IV) chain in mice does not cause severe-to-profound hearing loss or cochlear malformation, a distinct phenotype from nonsyndromic hearing loss with COL4A6 missense mutation. International journal

Shaoying Tang, Tomoko Yonezawa, Yukihide Maeda, Mitsuaki Ono, Takahiro Maeba, Toru Miyoshi, Ryusuke Momota, Yasuko Tomono, Toshitaka Oohashi

PloS one   16 ( 4 )   e0249909   2021

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Congenital hearing loss affects 1 in every 1000 births, with genetic mutations contributing to more than 50% of all cases. X-linked nonsyndromic hereditary hearing loss is associated with six loci (DFNX1-6) and five genes. Recently, the missense mutation (c.1771G>A, p.Gly591Ser) in COL4A6, encoding the basement membrane (BM) collagen α6(IV) chain, was shown to be associated with X-linked congenital nonsyndromic hearing loss with cochlear malformation. However, the mechanism by which the COL4A6 mutation impacts hereditary hearing loss has not yet been elucidated. Herein, we investigated Col4a6 knockout (KO) effects on hearing function and cochlear formation in mice. Immunohistochemistry showed that the collagen α6(IV) chain was distributed throughout the mouse cochlea within subepithelial BMs underlying the interdental cells, inner sulcus cells, basilar membrane, outer sulcus cells, root cells, Reissner's membrane, and perivascular BMs in the spiral limbus, spiral ligament, and stria vascularis. However, the click-evoked auditory brainstem response analysis did not show significant changes in the hearing threshold of Col4a6 KO mice compared with wild-type (WT) mice with the same genetic background. In addition, the cochlear structures of Col4a6 KO mice did not exhibit morphological alterations, according to the results of high-resolution micro-computed tomography and histology. Hence, loss of Col4a6 gene expression in mice showed normal click ABR thresholds and normal cochlear formation, which differs from humans with the COL4A6 missense mutation c.1771G>A, p.Gly591Ser. Therefore, the deleterious effects in the auditory system caused by the missense mutation in COL4A6 are likely due to the dominant-negative effects of the α6(IV) chain and/or α5α6α5(IV) heterotrimer with an aberrant structure that would not occur in cases with loss of gene expression.

DOI： 10.1371/journal.pone.0249909

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コラーゲン研究の新展開:基礎から創薬まで マウス皮膚創傷モデルにおけるXVIII型コラーゲンの解析

米澤 朋子, 前場 崇宏, Tang Shaoying, 大野 充昭, 百田 龍輔, 稲川 喜一, 大橋 俊孝

日本生化学会大会プログラム・講演要旨集   93回   [1S08e - 06]   2020.9

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Prolonged Tachycardia with Higher Heart Rate Is Associated with Higher ICU and In-hospital Mortality. Reviewed

Hayashi M, Taniguchi A, Kaku R, Fujimoto S, Isoyama S, Manabe S, Yoshida T, Suzuki S, Shimizu K, Morimatsu H, Momota R

Acta medica Okayama   73 ( 2 )   147 - 153   2019.4

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Tachycardia is common in intensive care units (ICUs). It is unknown whether tachycardia or prolonged tachycardia affects patient outcomes. We investigated the association between tachycardia and mortality in critically ill patients. This retrospective cohort study's primary outcome was patient mortality in the ICU and the hospital. We stratified the patients (n=476) by heart rate (HR) as LowHR, MediumHR, and HighHR groups. We also stratified them by their durations of HR >100 (prolonged HR; tachycardia): MildT, ModerateT, and SevereT groups. We determined the six groups' mortality. The ICU mortality rates of the LowHR, MediumHR, and HighHR groups were 1.0%, 1.5%, and 7.9%, respectively; significantly higher in the HighHR vs. LowHR group. The in-hospital mortality rates of these groups were 1%, 4.5%, and 14.6%, respectively; significantly higher in the HighHR vs. LowHR group. The ICU mortality rates of the MildT, ModerateT, and SevereT groups were 0.9%, 5.6%, and 57.1%, respectively. The mortality of the HRT=0 (i.e., all HR ≤ 100) patients was 0%. The in-hospital mortality rates of the MildT, ModerateT, and SevereT groups were 1.8%, 16.7%, and 85.7%, respectively; that of the HRT=0 patients was 0.5%. Both higher HR and prolonged tachycardia were associated with poor outcomes.

DOI： 10.18926/AMO/56650

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Unripe peach (Prunus persica) extract ameliorates damage from UV irradiation and improved collagen XVIII expression in 3D skin model. Reviewed International journal

Tomoko Yonezawa, Ryusuke Momota, Hideki Iwano, Steven Zhao, Tomohiro Hakozaki, Chieko Soh, Shigetoyo Sawaki, Kazumi Toyama, Toshitaka Oohashi

Journal of cosmetic dermatology   2018.12

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INTRODUCTION: Collagen type XVIII regulates cellular activities of adjacent cells at the dermal-epidermal junction (DEJ). To investigate its possible changes during aging, we compared its mRNA levels and protein localization in skin samples from female participants aged 20-70 years old. In addition, we evaluated the beneficial effects of unripe peach extracts in a 3D skin model. METHODS: Sun-exposed or sun-protected female skin samples were compared by DNA array or by immunohistochemistry for basement membrane components. To evaluate protective effects of fresh unripe peach extract, UV-B irradiated human 3D skin models were incubated in the presence or absence of the extract, followed by measurements of mRNA levels by real-time PCR, or by immunohistochemistry. RESULTS: In aged skin samples, COL18A1 mRNA levels were lower and the protein localization exhibited less intensive signal by anti-collagen type XVIII immunostaining. As observed in the skin tissues, collagen type XVIII exists at the DEJ in the 3D skin model. Fresh unripe peach extract significantly improved mRNA levels and partially localizations of collagen type XVIII, suggesting that fresh unripe peach extract ameliorates DEJ damages caused by UV-B irradiation. CONCLUSION: Collagen type XVIII and fresh unripe peach extract can be promising protective cosmetic strategies against skin aging.

DOI： 10.1111/jocd.12841

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Network of anatomical texts (NAnaTex), an open-source project for visualizing the interaction between anatomical terms Reviewed

Ryusuke Momota, Aiji Ohtsuka

Anatomical Science International   93 ( 1 )   149 - 153   2018.1

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Tokyo  

Anatomy is the science and art of understanding the structure of the body and its components in relation to the functions of the whole-body system. Medicine is based on a deep understanding of anatomy, but quite a few introductory-level learners are overwhelmed by the sheer amount of anatomical terminology that must be understood, so they regard anatomy as a dull and dense subject. To help them learn anatomical terms in a more contextual way, we started a new open-source project, the Network of Anatomical Texts (NAnaTex), which visualizes relationships of body components by integrating text-based anatomical information using Cytoscape, a network visualization software platform. Here, we present a network of bones and muscles produced from literature descriptions. As this network is primarily text-based and does not require any programming knowledge, it is easy to implement new functions or provide extra information by making changes to the original text files. To facilitate collaborations, we deposited the source code files for the network into the GitHub repository (https://github.com/ryusukemomota/nanatex) so that anybody can participate in the evolution of the network and use it for their own non-profit purposes. This project should help not only introductory-level learners but also professional medical practitioners, who could use it as a quick reference.

DOI： 10.1007/s12565-017-0410-1

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Type IV collagen α6 chain is a regulator of keratin 10 in keratinization of oral mucosal epithelium Reviewed International journal

Komori, T., Ono, M., Hara, E.S., Ueda, J., Nguyen, H.T.T., Nguyen, H.T., Yonezawa, T., Maeba, T., Kimura-Ono, A., Takarada, T., Momota, R., Maekawa, K., Kuboki, T., Oohashi, T.

Scientific Reports   8 ( 1 )   2612 - 2612   2018

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Keratinized mucosa is of fundamental importance to maintain healthy gingival tissue, and understanding the mechanisms of oral mucosa keratinization is crucial to successfully manage healthy gingiva. Previous studies have shown a strong involvement of the basement membrane in the proliferation and differentiation of epithelial cells. Therefore, first, to identify the keratinized mucosa-specific basement membrane components, immunohistochemical analysis for the six alpha chains of type IV collagen was performed in 8-week-old mice. No difference in the expression pattern of type IV collagen α1(IV) and α2(IV) chains was observed in the keratinized and non-keratinized mucosa. Interestingly, however, type IV collagen α5(IV) and α6(IV) chains specifically were strongly detected in the keratinized mucosa. To analyze the functional roles of the type IV collagen isoform α6(IV) in oral mucosa keratinization, we analyzed Col4a6-knockout mice. Epithelial developmental delay and low levels of KRT10 were observed in new-born Col4a6-knockout mice. Additionally, in vitro experiments with loss-of function analysis using human gingival epithelial cells confirmed the important role of α6(IV) chain in epithelial keratinization. These findings indicate that α112:α556 (IV) network, which is the only network that includes the α6(IV) chain, is one regulator of KRT10 expression in keratinization of oral mucosal epithelium.

DOI： 10.1038/s41598-018-21000-0

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Effects of aerobic exercise on capillary architecture of extensor digitorum Longus in Rat Reviewed

Shinichiro Murakami, Masahiro Sakita, Hiroyo Kondo, Miho Kanazashi, Masayuki Tanaka, Minoru Tanaka, Aiji Ohtuka, Ryusuke Momota, Hidemi Fujino

FASEB JOURNAL   28 ( 1 )   2014.4

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致死となるマルチプレキシン(XV/XVIII型コラーゲン)変異ショウジョウバエの解析

百田 龍輔, 楢崎 正博, 小見山 高明, 内藤 一郎, 二宮 善文, 大塚 愛二

日本結合組織学会学術大会・マトリックス研究会大会合同学術集会プログラム・抄録集   45回・60回   86 - 86   2013.6

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Drosophila type XV/XVIII collagen mutants manifest integrin mediated mitochondrial dysfunction, which is improved by cyclosporin A and losartan Reviewed International journal

Ryusuke Momota, Masahiro Narasaki, Takaaki Komiyama, Ichiro Naito, Yoshifumi Ninomiya, Aiji Ohtsuka

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY   45 ( 5 )   1003 - 1011   2013.5

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：PERGAMON-ELSEVIER SCIENCE LTD  

Vertebrate collagen types XV and XVIII are broadly distributed basement membrane components, classified into a structurally distinct subgroup called "multiplexin collagens". Mutations in mammalian multiplexins are identified in some degenerative diseases such as Knobloch syndrome 1 (KNO1) or skeletal/cardiac myopathies, however, these progressive properties have not been elucidated. Here we investigated Drosophila mutants of Multiplexin (Mp), the only orthologue of vertebrate collagen types XV and XVIII, to understand the pathogenesis of multiplexin-related diseases. The mp mutants exhibited morphological changes in cardiomyocytes and progressive dysfunction of the skeletal muscles, reminiscent phenotypes observed in Col15a1-null mice. Ultrastructural analysis revealed morphologically altered mitochondria in mutants' indirect flight muscles (IFMs), resulting in severely attenuated ATP production and enhanced reactive oxygen species (ROS) production. In addition, mutants' IFMs exhibited diminished PPS integrin clustering and abolished focal adhesion kinase (FAK) phosphorylation. Furthermore, mutants' defective IFMs are improved by the administrations of cyclosporin A, an inhibitor against mitochondrial permeability transition pore (mPTP) opening or losartan, an angiotensin II type 1 receptor (AT1R) blocker. Thus, our results suggest that Mp modulates mPTP opening and AT1R activity through its binding to integrin and that lack of Mp causes unregulated mPTP opening and AT1R activity, leading to mitochondrial dysfunctions. Hence, our results provide new insights towards the roles of multiplexin collagens in mitochondrial homeostasis and may serve as pharmacological evidences for the potential use of cyclosporin A or losartan for the therapeutic strategies. (C) 2013 Elsevier Ltd. All rights reserved.

DOI： 10.1016/j.biocel.2013.02.001

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Architecture of the subendothelial elastic fibers of small blood vessels and variations in vascular type and size Reviewed

Akira Shinaoka, Ryusuke Momota, Eri Shiratsuchi, Mitsuko Kosaka, Kanae Kumagishi, Ryuichi Nakahara, Ichiro Naito, Aiji Ohtsuka

Microscopy and Microanalysis   19 ( 2 )   406 - 414   2013.4

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Most blood vessels contain elastin that provides the vessels with the resilience and flexibility necessary to control hemodynamics. Pathophysiological hemodynamic changes affect the remodeling of elastic components, but little is known about their structural properties. The present study was designed to elucidate, in detail, the three-dimensional (3D) architecture of delicate elastic fibers in small vessels, and to reveal their architectural pattern in a rat model. The fine vascular elastic components were observed by a newly developed scanning electron microscopy technique using a formic acid digestion with vascular casts. This method successfully visualized the 3D architecture of elastic fibers in small blood vessels, even arterioles and venules. The subendothelial elastic fibers in such small vessels assemble into a sheet of meshwork running longitudinally, while larger vessels have a higher density of mesh and thicker mesh fibers. The quantitative analysis revealed that arterioles had a wider range of mesh density than venules
the ratio of density to vessel size was higher than that in venules. The new method was useful for evaluating the subendothelial elastic fibers of small vessels and for demonstrating differences in the architecture of different types of vessels. © Microscopy Society of America 2013.

DOI： 10.1017/S1431927612014341

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XV/XVIII型コラーゲンの新たな生物学的機能の探索

百田 龍輔, 内藤 一郎, 二宮 善文, 大塚 愛二

解剖学雑誌   87 ( 2 )   44 - 44   2012.6

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Abnormalities in the Fiber Composition and Capillary Architecture in the Soleus Muscle of Type 2 Diabetic Goto-Kakizaki Rats Reviewed

Shinichiro Murakami, Naoto Fujita, Hiroyo Kondo, Isao Takeda, Ryusuke Momota, Aiji Ohtsuka, Hidemi Fujino

SCIENTIFIC WORLD JOURNAL   2012   680189   2012

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Type 2 diabetes mellitus is linked to impaired skeletal muscle glucose uptake and storage. This study aimed to investigate the fiber type distributions and the three-dimensional (3D) architecture of the capillary network in the skeletal muscles of type 2 diabetic rats. Muscle fiber type transformation, succinate dehydrogenase (SDH) activity, capillary density, and 3D architecture of the capillary network in the soleus muscle were determined in 36-week-old Goto-Kakizaki (GK) rats as an animal model of nonobese type 2 diabetes and age-matched Wistar (Cont) rats. Although the soleus muscle of Cont rats comprised both type I and type IIA fibers, the soleus muscle of GK rats had only type I fibers. In addition, total SDH activity in the soleus muscle of GK rats was significantly lower than that in Cont rats because GK rats had no high-SDH activity type IIA fiber in the soleus muscle. Furthermore, the capillary diameter, capillary tortuosity, and microvessel volume in GK rats were significantly lower than those in Cont rats. These results indicate that non-obese diabetic GK rats have muscle fiber type transformation, low SDH activity, and reduced skeletal muscle capillary content, which may be related to the impaired glucose metabolism characteristic of type 2 diabetes.

DOI： 10.1100/2012/680189

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Drosophila type XV/XVIII collagen, Mp, is involved in Wingless distribution Reviewed International journal

Ryusuke Momota, Ichiro Naito, Yoshifumi Ninomiya, Aiji Ohtsuka

MATRIX BIOLOGY   30 ( 4 )   258 - 266   2011.5

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：ELSEVIER SCIENCE BV  

Multiplexin (Mp) is the Drosophila orthologue of vertebrate collagens XV and XVIII. Like them, Mp is widely distributed in the basement membranes of the developing embryos, including those of neuroblasts in the central and peripheral nervous systems, visceral muscles of the gut, and contractile cardioblasts. Here we report the identification of mutant larvae bearing piguBac transposon insertions that exhibit decrease Mp production associated with abdominal cuticular and wing margin defects, malformation of sensory organs and impaired sensitivity to physical stimuli. Additional findings include the abnormal ultrastructure of fatbody associated with abnormal collagen IV deposition, and reduced Wingless deposition. Collectively, these findings are consistent with the notion that Mp is required for the proper formation and/or maintenance of basement membrane, and that Mp may be involved in establishing the Wingless signaling gradients in the Drosophila embryo. (C) 2011 Elsevier B.V. All rights reserved.

DOI： 10.1016/j.matbio.2011.03.008

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微小血管内皮下弾性線維構造とその血行動態との関係

品岡 玲, 百田 龍輔, 小阪 美津子, 内藤 一郎, 中原 龍一, 大塚 愛二

日本結合組織学会学術大会・マトリックス研究会大会合同学術集会プログラム・抄録集   43回・58回   105 - 105   2011.5

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Language：Japanese   Publisher：日本結合組織学会・マトリックス研究会  

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ショウジョウバエmultiplexinの生物学的機能

百田 龍輔, 内藤 一郎, 二宮 善文, 大塚 愛二

日本結合組織学会学術大会・マトリックス研究会大会合同学術集会プログラム・抄録集   43回・58回   72 - 72   2011.5

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II型糖尿病ラット(GOTO-KAKIZAKIラット)のヒラメ筋の筋線維タイプの変化

熊岸 加苗, 村上 慎一郎, 藤野 英己, 武田 功, 百田 龍輔, 近藤 浩代, 大塚 愛二

解剖学雑誌   85 ( 2 )   82 - 82   2010.6

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共焦点レーザー顕微鏡を用いたラットの遅筋と速筋の毛細血管構築の比較

村上 慎一郎, 熊岸 加苗, 藤野 英己, 武田 功, 百田 龍輔, 近藤 浩代, 大塚 愛二

解剖学雑誌   85 ( 2 )   82 - 82   2010.6

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非インスリン依存型糖尿病モデルラットのヒラメ筋の毛細血管構築、ミオシン重鎖アイソフォーム、及び酸化的リン酸化活性の変化

村上 慎一郎, 藤野 英己, 近藤 浩代, 武田 功, 百田 龍輔, 熊岸 加苗, 大塚 愛二

解剖学雑誌   85 ( Suppl. )   114 - 114   2010.3

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動脈の内弾性板線維配列 とくに断裂部の超微細構造解析

品岡 玲, 百田 龍輔, 内藤 一郎, 大塚 愛二

解剖学雑誌   85 ( Suppl. )   200 - 200   2010.3

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Comparison of Capillary Architecture between Slow and Fast Muscles in Rats Using a Confocal Laser Scanning Microscope Reviewed

Shinichiro Murakami, Hidemi Fujino, Isao Takeda, Ryusuke Momota, Kanae Kumagishi, Aiji Ohtsuka

ACTA MEDICA OKAYAMA   64 ( 1 )   11 - 18   2010.2

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：OKAYAMA UNIV MED SCHOOL  

The skeletal muscle is classified into 2 types, slow oxidative or fast glycolytic muscle. For further characterization, we investigated the capillary architecture in slow and fast muscles. The rat soleus and extensor digitorum longus (EDL) muscles were used as representatives of slow and fast muscles, respectively. To investigate capillary density, sections of both types of muscle were stained with alkaline phosphatase; the soleus muscle showed more intense reactivity, indicating that it had a denser capillary structure than the EDL muscle. We then injected fluorescent contrast medium into samples of both muscle types for light and confocal-laser microscopic evaluation. The capillary density and capillary-to-fiber ratio were significantly higher, and the course of the capillaries was more tortuous, in the soleus muscle than in the EDL muscle. Capillary coursed more tortuously in the soleus than in the EDL muscle. Succinate dehydrogenase (SDH) activity, an indicator of mitochondrial oxidative capacity, and vascular endothelial growth factor (VEGF) expression were also significantly higher in the soleus muscle. Thus, we conclude that slow oxidative muscle possess a rich capillary structure to provide demanded oxygen, and VEGF might be involved in the formation and/or maintenance of this highly capillarized architecture.

DOI： 10.18926/AMO/32859

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Comparison of Capillary Architecture between Slow and Fast Muscles in Rats Using a Confocal Laser Scanning Microscope Reviewed

Shinichiro Murakami, Hidemi Fujino, Isao Takeda, Ryusuke Momota, Kanae Kumagishi, Aiji Ohtsuka

ACTA MEDICA OKAYAMA   64 ( 1 )   11 - 18   2010.2

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The skeletal muscle is classified into 2 types, slow oxidative or fast glycolytic muscle. For further characterization, we investigated the capillary architecture in slow and fast muscles. The rat soleus and extensor digitorum longus (EDL) muscles were used as representatives of slow and fast muscles, respectively. To investigate capillary density, sections of both types of muscle were stained with alkaline phosphatase; the soleus muscle showed more intense reactivity, indicating that it had a denser capillary structure than the EDL muscle. We then injected fluorescent contrast medium into samples of both muscle types for light and confocal-laser microscopic evaluation. The capillary density and capillary-to-fiber ratio were significantly higher, and the course of the capillaries was more tortuous, in the soleus muscle than in the EDL muscle. Capillary coursed more tortuously in the soleus than in the EDL muscle. Succinate dehydrogenase (SDH) activity, an indicator of mitochondrial oxidative capacity, and vascular endothelial growth factor (VEGF) expression were also significantly higher in the soleus muscle. Thus, we conclude that slow oxidative muscle possess a rich capillary structure to provide demanded oxygen, and VEGF might be involved in the formation and/or maintenance of this highly capillarized architecture.

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A disintegrin and metalloproteinase with thrombospondin motifs 9 (ADAMTS9) expression by chondrocytes during endochondral ossification Reviewed

Kanae Kumagishi, Keiichiro Nishida, Tomoichiro Yamaai, Ryusuke Momota, Shigeru Miyaki, Satoshi Hirohata, Ichiro Naito, Hiroshi Asahara, Yoshifumi Ninomiya, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   72 ( 3 )   175 - 185   2009.11

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：INT SOC HISTOLOGY & CYTOLOGY  

A disintegrin and metalloproteinase with thrombospondin motifs 9 (ADAMTS9) is known to influence aggrecan degradation in endochondral ossification, but its role has not been well understood. In the present study, in vitro gene expression of ADAMTS9 was investigated by RT-PCR in ATDC5 cells in which experimentally chondrogenic differentiation had been induced. We also investigated the protein localization and gene expression pattern of ADAMTS9 in the tibia growth plate cartilage of male mice in a day 1 neonate, 7-week-old young adult, and a 12-week-old adult by immunohistochemistry and in situ hybridization and compared the results with the expression of proliferating cell nuclear antigen (PCNA) and type X collagen for the identification of proliferative and hypertrophic chondrocyte phenotypes, respectively. We found the gene expression of ADAMTS9 by ATDC5 cells as a dual mode, both before the expression of type X collagen and after hypertrophic differentiation. The immunoreactivity of ADAMTS9 was observed in chondrocytes of proliferative and hypertrophic zones in the growth plate. The population of ADAMTS9 positive cells decreased with age. The results of the present study suggest that ADAMTS9 might have a role in aggrecan cleavage around the chondrocytes to allow chondrocyte proliferation and hypertrophy.

DOI： 10.1679/aohc.72.175

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潰瘍性大腸炎における大腸粘膜下基底膜のIV型コラーゲンα鎖の解析

佐藤 博之, 内藤 一郎, 百田 龍輔, 小林 直哉, 大塚 愛二

日本消化器病学会雑誌   106 ( 臨増大会 )   A827 - A827   2009.9

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肺内気道-呼吸上皮とその基底膜を構成するIV型コラーゲンのα鎖解析

日根野谷 紀子, 内藤 一郎, 百田 龍輔, 佐渡 義一, 大塚 愛二

解剖学雑誌   84 ( 2 )   68 - 68   2009.6

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マウス成長軟骨におけるADAMTS-9発現とその役割について

熊岸 加苗, 西田 圭一郎, 百田 龍輔, 山合 友一朗, 廣畑 聡, Kadir Demircan, 内藤 一郎, 二宮 善文, 大塚 愛二

解剖学雑誌   84 ( Suppl. )   139 - 139   2009.3

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炎症性腸疾患における大腸粘膜下基底膜のIV型コラーゲンα鎖の解析

佐藤 博之, 内藤 一郎, 斉藤 健司, 百田 龍輔, 小林 直哉, 大塚 愛二

解剖学雑誌   84 ( Suppl. )   144 - 144   2009.3

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ラット腹側尾動脈の内弾性板の加齢性変化

品岡 玲, 百田 龍輔, 内藤 一郎, 大塚 愛二

解剖学雑誌   84 ( Suppl. )   180 - 180   2009.3

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ショウジョウバエXV/XVIII型コラーゲンDroleは正常な発生と基底膜の構造に重要である

百田 龍輔, 内藤 一郎, 二宮 善文, 大塚 愛二

解剖学雑誌   84 ( Suppl. )   130 - 130   2009.3

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Type IV collagen alpha chains of the basement membrane in the rat bronchioalveolar transitional segment Reviewed

Noriko Hinenoya, Ichiro Naito, Ryusuke Momota, Yoshikazu Sado, Kanae Kumagishi, Yoshifumi Ninomiya, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   71 ( 3 )   185 - 194   2008.11

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In the present study, we have analyzed the a(IV) chain distribution in the subepithelial basement membrane (BM) of the rat pulmonary airway from the bronchi to alveoli. We have furthermore analyzed the a(IV) chain distribution in the subepithelial BM of the bronchioalveolar duct junction (BADJ) using a(IV) chain specific monoclonal antibodies. Our results show that the BM of the bronchial and bronchiolar epithelium contains [al(IV)](2) a2(IV) and [ a5(IV)](2) a6(IV) molecules and confirmed that the alveolar BM consists of [a1(IV)](2) a2(IV) and a3(IV) a4(IV) a5(IV) molecules. There are also small regions in BADJ consisting of only [ a] (IV)](2) a2(IV) molecules without a3(IV) a4(IV) a5(IV) and [ a5(IV)](2) a6(IV) molecules. Moreover, the bronchioalveolar stem cells (BASCs) -primordial cells for bronchiolar Clara cells and alveolar type II (AT2) cells- lie adjacent to such small regions. These findings suggest that [ al(IV)](2) a2(IV) may be important for the BASCs to self-renew or to self-maintain themselves and that microenvironments produced by a(IV) chains may be important for cell differentiation.

DOI： 10.1679/aohc.71.185

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指紋に対応する細胞外マトリックス

内藤 一郎, 斎藤 健司, 百田 龍輔, 佐渡 義一, 二宮 善文, 大塚 愛二

解剖学雑誌   83 ( Suppl. )   219 - 219   2008.3

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ラット気管支・肺胞移行部における基底膜構成IV型コラーゲンのα鎖解析

日根野谷 紀子, 内藤 一郎, 百田 龍輔, 佐渡 義一, 大塚 愛二

解剖学雑誌   83 ( Suppl. )   204 - 204   2008.3

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The differential distribution of type IV collagen alpha chains in the subepithelial basement membrane of the human alimentary canal Reviewed

Hiroyuki Sato, Ichiro Naito, Ryusuke Momota, Yoshio Naomoto, Tomoki Yamatsuji, Yoshikazu Sado, Yoshifumi Ninomiya, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   70 ( 5 )   313 - 323   2007.12

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We studied distribution patterns of type IV collagen a chains in the subepithelial basement membrane (SBM) of the human gastrointestinal tract - the esophagus through the anal canal - by immunofluorescent microscopy using alpha(IV) chain-specific monoclonal antibodies. The alpha 1(IV), alpha 2(IV), alpha 5(IV), and alpha 6(IV) chains were found in the SBM throughout the tract, indicating the localization of [alpha 1(IV)](2) alpha 2(IV) and [alpha 5(IV)](2) alpha 6(IV) heterotrimeric molecules. The [alpha 1(IV)](2) alpha 2(IV) molecule was continuously stained, while the [alpha 5(IV)]2 alpha 6(IV) molecule was weakly stained in gastric glands and small intestinal crypts. In addition, the SBM at the luminal surface epithelium of the stomach and large intestine contained small amounts of alpha 3(IV) and alpha 4(IV) chains which combined to form the alpha 3(IV) alpha 4(IV) alpha 5(IV) heterotrimeric molecule with alpha 5(IV) chain. The SBM beneath the villous epithelium of the small intestine was also demonstrated to have an alpha 3(IV) chain and alpha 4(IV) chain. Considering the specific locations of the type IV collagen trimers throughout the gastrointestinal SBM, the supramolecular network containing the alpha 3(IV) alpha 4(IV) alpha 5(IV) molecule appears to function as a selective permeability barrier and/or as a protection against chemical stress from the luminal digestive enzymes.

DOI： 10.1679/aohc.70.313

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Intermediate filaments of endoskeleton within human erythrocytes. Reviewed

Kazutaka Terasawa, Takehito Taguchi, Ryusuke Momota, Ichiro Naito, Aiji Ohtsuka

BLOOD   110 ( 11 )   516A - 516A   2007.11

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DOI： 10.1182/blood.V110.11.1734.1734

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The distribution of type IV collagen alpha chains in the mouse ovary and its correlation with follicular development Reviewed

Kazuyo Nakano, Ichiro Naito, Ryusuke Momota, Yoshikazu Sado, Haruko Hasegawa, Yoshifumi Ninomiya, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   70 ( 4 )   243 - 253   2007.11

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The present study aims to identify a chains of type IV collagen in the basement membrane of the mouse ovarian follicle and examine their changes during follicular development using immunofluorescence microscopy with specific monoclonal antibodies. The basement membrane of the serous mesothelium enveloping the ovary contained all a chains of type IV collagen, alpha 1(IV) through alpha 6(IV) chains. Primordial follicles showed a distinct immunoreactivity against all six a chains in their basement membranes. Immunolabeling for alpha 3(IV) and alpha 4(IV) chains was almost eliminated in the primary follicles. In basement membranes of secondary and Graafian follicles, the immunofluorescent reaction of a3(IV) and a4(IV) chains disappeared in Graafian follicles, a partial reduction in fluorescent immunostaining intensity to alpha 5(IV) and alpha 6(IV) chains was observed; only alpha 1(IV) and alpha 2(IV) chains were not degraded throughout follicular development. On atretic follicles, in addition to alpha 1(IV) and a2(IV) chains, alpha 3(IV), alpha 4(IV), alpha 5(IV) and alpha 6(IV) chains frequently persisted. A basement membrane-like matrix within the follicular granulosa cell layer, such as the focimatrix (focal intraepithelial matrix) and/or Call-Exner body, was also recognized in mouse secondary and Graafian follicles and contained alpha 1(IV), alpha 2(IV), alpha 5(IV) and alpha 6(IV) chains but not alpha 3(IV) and alpha 4(IV) chains. We expect that the decrease in alpha(IV) chains prompts follicular development and is a prerequisite condition for follicular maturation.

DOI： 10.1679/aohc.70.243

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The distributions of type IV collagen alpha chains in basement membranes of human epidermis and skin appendages Reviewed

Haruko Hasegawa, Ichiro Naito, Kazuyo Nakano, Ryusuke Momota, Keiichiro Nishida, Takehito Taguchi, Yoshikazu Sado, Yoshifumi Ninomiya, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   70 ( 4 )   255 - 265   2007.11

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Distributions of type IV collagen a chains in the basement membrane (BM) of human skin and its appendages were analyzed by immunofluorescent microscopy using chain-specific monoclonal antibodies. The basement membrane beneath the epidermis contained [alpha 1(IV)]2 alpha 2(IV) and [ alpha 5(IV)]2 alpha 6(IV) but no alpha 3(IV) alpha 4(IV) alpha 5(IV); this held true for at the eccrine sweat glands and glandular ducts, sebaceous glands, hair follicles, and arrector muscles of hair. The secretary portion of the eccrine sweat glands was rich in [alpha 1(IV)]2 alpha 2(IV) and had less [ alpha 5(IV)]2 alpha 6(IV), while [alpha 5(IV)]2 alpha 6(IV) was abundant in the ductal portion. In the subepidermal zone, alpha 5(IV)/ alpha 6(IV) chain negative spots (1.9-15.0 mu m) were frequently observed. Triple staining samples (Mel.2, alpha 2(IV) and alpha 5(IV) chains) showed that about 50% of epidermal melanocytes colocalized with such spots. Results suggest that these alpha 5(IV)/ alpha 6(IV) chain negative spots of the subepidermal basement membrane have a particular relationship with melanocytes and are sites for certain interactions between the two.

DOI： 10.1679/aohc.70.255

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赤血球の両凹形態を維持する細胞質内骨格(Cytoplasmic endoskeleton maintaining the biconcave shape of erythrocytes)

寺沢 和貴, 田口 勇仁, 百田 龍輔, 内藤 一郎, 大塚 愛二

解剖学雑誌   82 ( 3 )   114 - 114   2007.9

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ブタの神経筋接合部に局在するIV型コラーゲンα鎖の解析

山内 健太朗, 内藤 一郎, 森 雄市, 百田 龍輔, 長谷川 治子, 二宮 善文, 佐渡 義一, 田口 勇仁, 野村 信介, 大塚 愛二

解剖学雑誌   82 ( 3 )   112 - 112   2007.9

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ショウジョウバエXV/XVIII型コラーゲンの生物学的機能

百田 龍輔, 内藤 一郎, 二宮 善文, 大塚 愛二

日本結合組織学会学術大会・マトリックス研究会大会合同学術集会プログラム・抄録集   39回・54回   78 - 78   2007.5

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マウス成長軟骨におけるADAMTS-9発現の検討

熊岸 加苗, 西田 圭一郎, 百田 龍輔, 山合 友一朗, 広畑 聡, Demircan Kadir, 内藤 一郎, 二宮 善文, 大塚 愛二

解剖学雑誌   82 ( Suppl. )   150 - 150   2007.3

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IV型コラーゲンα鎖特異抗体反応基の抗原賦活法

森 雄一, 内藤 一郎, 百田 龍輔, 二宮 善文, 大塚 愛二

解剖学雑誌   82 ( Suppl. )   271 - 271   2007.3

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ヒト赤血球には内部細胞骨格が見られ、βアクチンとニューロフィラメント蛋白を含む

寺沢 和貴, 田口 勇仁, 百田 龍輔, 内藤 一郎, 大塚 愛二

解剖学雑誌   82 ( Suppl. )   231 - 231   2007.3

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ラットの腹側尾動脈の血管鋳型標本に見られた風変わりな刻印

品岡 玲, 百田 龍輔, 大塚 愛二, 内藤 一郎

解剖学雑誌   82 ( Suppl. )   150 - 150   2007.3

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Human erythrocytes possess a cytoplasmic endoskeleton containing beta-actin and neurofilament protein Reviewed

Kazutaka Terasawa, Takehito Taguchi, Ryusuke Momota, Ichiro Naito, Takuro Murakami, Aiji Ohtsuka

ARCHIVES OF HISTOLOGY AND CYTOLOGY   69 ( 5 )   329 - 340   2006.12

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The biconcave disc shape of mammalian erythrocytes has been considered to be maintained only with a membrane underlain by a membranous cytoskeleton. Our improved ion-etching/scanning electron microscopy and saponin-ethanol treatment combined with immunocytochemistry in the human red blood cell revealed the three-dimensional structure of this cytoplasmic endoskeleton apart from the classical membranous cytoskeleton. The endoskeletal meshwork images obtained by the saponin-ethanol treatment corresponded to those by the repeated ion-etching method. The actin-rich endoskeleton was divided into two layers, one superficial and the other deep. The superficial filaments were perpendicularly connected to the membranous cytoskeleton, while the deep filaments formed an irregularly directed complicated meshwork. In the transitional hillside region between the convex periphery and concave center, the endoskeletal filaments containing a neurofilament protein ran parallel to the hillside slope toward the concave center. The endoskeleton of the erythrocyte associating with the membranous cytoskeleton may serve to keep its unique biconcave disc shape deformable, pliable, and restorable against external circumstances.

DOI： 10.1679/aohc.69.329

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ADAMTS-ECM interaction modulates BMP developmental control Reviewed

J. Fessler, R. Momota, C. Cresse, K. Chavan, L. Fessler

MATRIX BIOLOGY   25   S30 - S30   2006.11

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DOI： 10.1016/j.matbio.2006.08.084

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血管基底膜IV型コラーゲンの免疫組織学的解析 共焦点レーザー顕微鏡を用いた三次元観察

森本 尊雅, 内藤 一郎, 百田 龍輔, 芳原 成美, 長谷川 治子, 田口 勇仁, 西田 圭一郎, 佐渡 義一, 二宮 善文, 大塚 愛二

解剖学雑誌   81 ( Suppl. )   155 - 155   2006.3

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基底膜の多様性 α(IV)鎖特異抗体をもちいた基底膜IV型コラーゲンα鎖の多様性解析

内藤 一郎, 長谷川 治子, 森本 尊雅, 百田 龍輔, 斉藤 健司, 佐渡 義一, 二宮 善文, 大塚 愛二

解剖学雑誌   81 ( Suppl. )   110 - 110   2006.3

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In situ preparation of colloidal iron by microwave irradiation for transmission electron microscopy Reviewed

S Nakatani, Naito, I, R Momota, N Hinenoya, K Horiuchi, K Nishida, A Ohtsuka

ACTA MEDICA OKAYAMA   60 ( 1 )   59 - 64   2006.2

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We attempted to prepare colloidal iron within tissues by means of microwave irradiation. Mouse tissue blocks were fixed with a mixture of paraformaldehyde and ferric chloride in a cacodylate buffer, immersed in a cacodylate buffered ferric chloride solution, and irradiated in a microwave processor. Colloidal iron was prepared within tissues or cells, and was observed in the form of electron dense fine granules (1-2 nm in diameter) by transmission electron microscopy. Collagen fibrils in the connective tissue showed colloidal iron deposition at regular periodical intervals. Cells in the splenic tissue showed that fine colloidal granules were deposited on the ribosomes but not on the nuclear chromatin. This finding suggests that ferric ions could not diffuse into the nucleus, which was surrounded by the nuclear envelope. The podocyte processes of the renal glomerulus were stained diffusedly. Though this microwave in situ colloidal iron preparation method has some limitations, it is convenient for use in biomedical specimen preparation in transmission electron microscopy.

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In situ preparation of colloidal iron by microwave irradiation for transmission electron microscopy Reviewed

S Nakatani, Naito, I, R Momota, N Hinenoya, K Horiuchi, K Nishida, A Ohtsuka

ACTA MEDICA OKAYAMA   60 ( 1 )   59 - 64   2006.2

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：OKAYAMA UNIV MED SCHOOL  

We attempted to prepare colloidal iron within tissues by means of microwave irradiation. Mouse tissue blocks were fixed with a mixture of paraformaldehyde and ferric chloride in a cacodylate buffer, immersed in a cacodylate buffered ferric chloride solution, and irradiated in a microwave processor. Colloidal iron was prepared within tissues or cells, and was observed in the form of electron dense fine granules (1-2 nm in diameter) by transmission electron microscopy. Collagen fibrils in the connective tissue showed colloidal iron deposition at regular periodical intervals. Cells in the splenic tissue showed that fine colloidal granules were deposited on the ribosomes but not on the nuclear chromatin. This finding suggests that ferric ions could not diffuse into the nucleus, which was surrounded by the nuclear envelope. The podocyte processes of the renal glomerulus were stained diffusedly. Though this microwave in situ colloidal iron preparation method has some limitations, it is convenient for use in biomedical specimen preparation in transmission electron microscopy.

DOI： 10.18926/AMO/30753

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Differential expression of mouse alpha 5(IV) and alpha 6(IV) collagen genes in epithelial basement membranes Reviewed

K Saito, Naito, I, T Seki, T Oohashi, E Kimura, R Momota, Y Kishiro, Y Sado, H Yoshioka, Y Ninomiya

JOURNAL OF BIOCHEMISTRY   128 ( 3 )   427 - 434   2000.9

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：JAPANESE BIOCHEMICAL SOC  

We first completed the primary structure of the mouse alpha 5(IV) and alpha 6(IV) chains, from which synthetic peptides were produced and alpha chain-specific monoclonal antibodies were raised. Expression of collagen IV genes in various basement membranes underlying specific organ epithelia was analyzed by immunohistochemical staining using these monoclonal antibodies and other antibodies from human and bovine sequences. It was possible to predict the presence of the three collagen TV molecules: [alpha 1(IV)](2) alpha 2(IV), alpha 3(IV)alpha 4(IV)alpha 5(IV), and [alpha 5(IV)](2)alpha 6(IV), In skin basement membrane two of the three forms, [alpha 1(IV)](2)alpha 2(IV) and [alpha 5(IV)](2)alpha 6(IV), were detected. The alpha 3(IV)alpha 4(IV)alpha 5(IV) molecule was observed as the major form in glomerulus, alveolus, and choroid plexus, where basement membranes function as filtering units. The molecular form [alpha 5(IV)](2)alpha 6(IV) was present in basement membranes in tubular organs such as the epididymis, where the tubes need to expand in diameter. Thus, the distribution of the basement membranes with different molecular composition is consistent with tissue-specific function.

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Organization and expression of basement membrane collagen IV genes and their roles in human disorders Reviewed

Y Sado, M Kagawa, Naito, I, Y Ueki, T Seki, R Momota, T Oohashi, Y Ninomiya

JOURNAL OF BIOCHEMISTRY   123 ( 5 )   767 - 776   1998.5

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Six distinct genes have been identified as belonging to the type IV collagen gene family. They can be organized into three sets, i.e., COL4A1/COL4A2, COL4A3/COL4A4, and COL4A5/COL4A6, which are localized on three different chromosomes in humans, 13, 2, and X, respectively, Within each set the genes are aligned head-to-head and their expression is regulated by bidirectional promoters between the genes. Transcriptional regulation of the COL4A1/COL4A2 set has been well characterized, The transcription of COL4A6 seems to be controlled by two alternative promoters. While collagen IV molecules composed of alpha 1 and alpha 2 chains are broadly distributed, molecules comprising combinations of the other four chains, alpha 3-alpha 6, are important components of specialized basement membranes, The precise chain composition of triple-helical molecules assembled from the alpha 3-alpha 6 chains is not entirely clear, but it is hypothesized that alpha 3-alpha 5 chains and alpha 5 and alpha 6 chains form heterotrimeric molecules. Several pieces of evidence indicate that alpha 3/alpha 4/alpha 5 molecules and alpha 5/alpha 6 molecules are components of the basement membrane network, This helps explain the observation that the kidney and skin basement membranes from patients with Alport syndrome caused by mutations in the alpha 5 coding gene, COL4A5, are defective in the alpha 3, alpha 4, and alpha 6 chains together with the alpha 5 chain. Large deletions involving the COL4A5 and COL4A6 genes have been found in rare cases of diffuse leiomyomatosis associated with Alport syndrome.

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Two genes, COL4A3 and COL4A4 coding for the human alpha 3(IV) and alpha 4(IV) collagen chains are arranged head-to-head on chromosome 2q36 Reviewed

R Momota, M Sugimoto, T Oohashi, K Kigasawa, H Yoshioka, Y Ninomiya

FEBS LETTERS   424 ( 1-2 )   11 - 16   1998.3

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We first isolated and characterized genomic DNA fragments that cover the 5' flanking sequences of COL4A3 and COL4A4 encoding the human basement membrane alpha 3(IV) and alpha 4(IV) collagen chains, respectively. Nucleotide sequence analysis indicated that the two genes are arranged head-to-head. To determine transcription start site for COL4A4 gene, we performed RACE and RNase protection assays, indicating that there are two alternative transcripts presumably derived from two different promoters. Interestingly, one transcription start site (from exon 1') of COL4A4 is only 5 bp away from the reported transcription start site of COL4A3, whereas the other transcript (from exon 1) starts 373 nucleotides downstream from the first one, generating the two kinds of transcripts that differ in the 5' UTR regions. Expression of these two transcripts appears tissue-specific; exon 1 transcript was expressed predominantly in epithelial cells, while exon 1' transcript showed rather ubiquitous and low expression. The nucleotide sequence of the promoter region is composed of dense CpG dinucleotides, GC boxes, CTC boxes and a CCAAT box but no TATA box. These results provide information to delineate the promoter activity for the tissue-specific expression of the six type IV collagen genes and basement membrane assembly in different tissues and organs. (C) 1998 Federation of European Biochemical Societies.

DOI： 10.1016/S0014-5793(98)00128-8

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