Faculty Profiles - MOMOTA Ryusuke

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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