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549 results on '"Hattori, Shunji"'

152. Improved RNA Extraction Method Using the BioMasher and BioMasher Power-Plus

Author

YAMAMOTO, Takuji, primary, NAKASHIMA, Kentaro, additional, MARUTA, Yukio, additional, KIRIYAMA, Tomomi, additional, SASAKI, Michi, additional, SUGIYAMA, Shunpei, additional, SUZUKI, Kana, additional, FUJISAKI, Hitomi, additional, SASAKI, Jun, additional, KAKU-USHIKI, Yuko, additional, TANIDA, Masatoshi, additional, IRIE, Shinkichi, additional, and HATTORI, Shunji, additional

Published
2012
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155. Activin A Binds to Perlecan through Its Pro-region That Has Heparin/Heparan Sulfate Binding Activity

Author

Li, Shaoliang, primary, Shimono, Chisei, additional, Norioka, Naoko, additional, Nakano, Itsuko, additional, Okubo, Tetsuo, additional, Yagi, Yoshiko, additional, Hayashi, Maria, additional, Sato, Yuya, additional, Fujisaki, Hitomi, additional, Hattori, Shunji, additional, Sugiura, Nobuo, additional, Kimata, Koji, additional, and Sekiguchi, Kiyotoshi, additional

Published
2010
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158. Tracing Conformational Transition of Abnormal Prion Proteins during Interspecies Transmission by Using Novel Antibodies

Author

Ushiki-Kaku, Yuko, primary, Endo, Ryo, additional, Iwamaru, Yoshifumi, additional, Shimizu, Yoshihisa, additional, Imamura, Morikazu, additional, Masujin, Kentaro, additional, Yamamoto, Takuji, additional, Hattori, Shunji, additional, Itohara, Shigeyoshi, additional, Irie, Shinkichi, additional, and Yokoyama, Takashi, additional

Published
2010
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167. Medical-grade collagen peptide in injectables provides antioxidant protection.

Author

Kobayashi, Kyo, Maehata, Yojiro, Okada, Yasue, Kusubata, Masashi, Hattori, Shunji, Tanaka, Keisuke, Miyamoto, Chihiro, Yoshino, Fumihiko, Yoshida, Ayaka, Tokutomi, Fumiaki, Wada-Takahashi, Satoko, Komatsu, Tomoko, Otsuka, Takero, Takahashi, Shun-Suke, and Lee, Masaichi-Chang-Il

Subjects
COLLAGEN, HYDROXYL group, SUPEROXIDES, HYDROGEN peroxide, OXIDATION
Abstract

Medical-grade collagen peptide is used as an additive agent in pharmaceutical formulations; however, it is unknown as to whether the compound exerts antioxidant effects in vitro. In this study, we evaluated the antioxidant effects of medical-grade collagen peptide on reactive oxygen species such as hydroxyl radical, superoxide anion radical and singlet oxygen using electron spin resonance and spin trapping. We confirmed that medical-grade collagen peptide directly inhibited hydroxyl radical generated by the Fenton reaction or by ultraviolet irradiation of hydrogen peroxide, and singlet oxygen. In addition, an antioxidant effect of medical-grade collagen peptide on singlet oxygen was observed in peptide fractions 12-22. The total amount of antioxidant amino acids (Gly, Hyp, Glu, Ala, Cys, Met and His) constituted more than half of the total amino acids in these fractions. These results suggest that the observed antioxidant properties of medical-grade collagen peptide are due to the compound containing antioxidant amino acids. Medical-grade collagen peptide, which is used in pharmaceuticals, and especially in injectables, could provide useful antioxidant properties to protect the active ingredient from oxidation. [ABSTRACT FROM AUTHOR]

Published
2015
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177. Systematic Separation and Purification of Elastase, Gelatinase (Matrix Metalloproteinase 9), and Collagenase (Matrix Metalloproteinase 8) from Polymorphonuclear Leukocytes in Dialyzers Previously Used by Patients with Renal Failure

Author

Kobayashi, Takashi, primary, Nishikawa, Takeji, additional, Hattori, Shunji, additional, Yoshida, Naoki, additional, Takagi, Tamotsu, additional, Watanabe, Hideto, additional, Hori, Hisae, additional, and Nagai, Yutaka, additional

Published
2001
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180. Expression of collagenase in Flavobacterium psychrophilumisolated from cold-water disease-affected ayu (Plecoglossus altivelis)

Author

Nakayama, Hitoshi, Tanaka, Keisuke, Teramura, Naoko, and Hattori, Shunji

Abstract

The collagenase activity and the fpcolgene were examined in Flavobacterium psychrophilumisolates from cold-water disease (CWD)-affected ayu, Plecoglossus altivelis. Collagenase expression was closely related to the accumulated mortality of CWD-affected ayu. RT-qPCR and bacterial challenge experiments showed that F. psychrophilumayu isolate WA-1 expressed the fpcolgene more actively and was more virulent than ayu isolate WA-2. The amago (Oncorhynchus masou) isolate WB-1, which possesses a pseudo-fpcolgene, was not harmful to ayu. Hitherto, the well-studied metalloproteases Fpp1 and Fpp2 have been considered virulence factors. However, the most virulent isolate against ayu (WA-1) showed no Fpp activity because of a deletion mutation or an insertion of a transposon in the fppgenes. The less virulent WA-2 isolate showed only Fpp1 activity. Taken together, these results suggest that collagenolytic activity, but not Fpp activity, is related to the virulence of F. psychrophilumisolates in CWD-affected ayu.

Published
2016
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182. Acceleration of bone formation during fracture healing by injectable collagen powder and human basic fibroblast growth factor containing a collagen-binding domain from Clostridium histolyticum collagenase.

Author

Saito, Wataru, Uchida, Kentaro, Ueno, Masaki, Matsushita, Osamu, Inoue, Gen, Nishi, Nozomu, Ogura, Takayuki, Hattori, Shunji, Fujimaki, Hisako, Tanaka, Keisuke, and Takaso, Masashi

Abstract

Growth factor delivered with implantable biomaterials has been used to both accelerate and ensure healing of open fractures in human patients. However, a major limitation of implantable biomaterials is the requirement for open surgical placement. Here, we developed an injectable collagen material-based bone formation system consisting of injectable collagen powder with fibril morphology and collagen triple helix conformation, and basic fibroblast growth factor (bFGF) fused to the collagen-binding domain (CBD) of Clostridium histolyticum collagenase. The affinity of the CBD towards collagen was confirmed by the results of collagen-binding assays. Moreover, the combination of the collagen binding-bFGF fusion protein (CB-bFGF) with injectable collagen powder induced bone formation at protein concentrations lower than those required for bFGF alone in mice fracture models. Taken together, these properties suggest that the CB-bFGF/collagen powder composite is a promising injectable material for bone repair in the clinical setting. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 3049-3055, 2014. [ABSTRACT FROM AUTHOR]

Published
2014
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183. Acceleration of periosteal bone formation by human basic fibroblast growth factor containing a collagen-binding domain from Clostridium histolyticum collagenase.

Author

Uchida, Kentaro, Matsushita, Osamu, Naruse, Kouji, Mima, Takehiko, Nishi, Nozomu, Hattori, Shunji, Ogura, Takayuki, Inoue, Gen, Tanaka, Keisuke, and Takaso, Masashi

Abstract

Basic fibroblast growth factor 2 (bFGF) is a potent mitogen for mesenchymal cells, and the local application of recombinant bFGF accelerates bone union and defect repair. However, repeated dosing is required for sustained therapeutic effect as the efficacy of bFGF decreases rapidly following its diffusion from bone defect sites. Here, we attempted to develop a collagen-based bone formation system using a fusion protein (collagen binding-bFGF, CB-bFGF) consisting of bFGF and the collagen-binding domain (CBD) of Clostridium histolyticum collagenase. The addition of the CBD to bFGF did not modify its native biological activity, as shown by the capacity of the fusion protein to promote the in vitro proliferation of periosteal mesenchymal cells. The affinity of the fusion protein towards collagen and demineralized bone matrix (DBM) was also confirmed by collagen-binding assays. Moreover, in vivo periosteal bone formation assays showed that the combination of CB-bFGF with a collagen sheet induced periosteal bone formation at protein concentrations lower than those required for bFGF alone. In addition, grafts of DBM loaded with CB-bFGF accelerated new bone formation in rat femurs compared to the same concentration of bFGF administered alone. Taken together, these properties suggest that the CB-bFGF/collagen composite is a promising material for bone repair in the clinical setting. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 1737-1743, 2014. [ABSTRACT FROM AUTHOR]

Published
2014
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194. Measurement of solar UV radiation in Antarctica with collagen sheets.

Author

Takahashi, Tetsuya, Kondo, Tetsuo, Tanaka, Keisuke, Hattori, Shunji, Irie, Shinkichi, Kudoh, Sakae, Imura, Satoshi, and Kanda, Hiroshi

Subjects
COLLAGEN, AMINO acids, ULTRAVIOLET radiation, OZONE layer depletion, CITRIC acid
Abstract

Collagen sheets were used in a unique evaluation method to examine skin damage caused by ultraviolet (UV) light of short wavelength during a season of the Antarctic ozone hole. The collagen sheets were exposed outdoors for 25 and 50 d, in the spring when the ozone hole was formed and in the ozone-hole-free autumn. Extracts from the exposed collagen sheets were analyzed for total protein and terminal amino acid concentrations as an index of collagen fragmentation. The results show that the amount of extractable collagen and terminal amino acid concentration in the spring exposure were approximately double and five times higher, respectively, when compared with those in the autumn exposure. During the ozone hole occurrence, the terminal amino acid concentration of the extracted collagen was about five times higher when exposure lasted 50 d from mid-September to the end of October compared to when exposure lasted 25 d from mid-September to early October. This result could be attributed to a limited amount of short-wavelength UV radiation reaching the ground surface as a result of the low height of the sun in September, when the ozone hole occurred. In fact, UV radiation measurements taken at Syowa Station indicate that short-wavelength UV radiation in the range 290–295 nm was not detected until approximately 1–2 months after the beginning of the ozone hole occurrence. [ABSTRACT FROM AUTHOR]

Published
2012
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196. Delay of cell cycle progression and induction of death of cancer cells on type I collagen fibrils.

Author

Sasaki, Jun, Fujisaki, Hitomi, Adachi, Eijiro, Irie, Shinkichi, and Hattori, Shunji

Subjects
CELL cycle, CANCER cell growth, CELL death, COLLAGEN, FOCAL adhesion kinase, PROTEIN kinases, CELL proliferation
Abstract

Here, we report the behavior of three kinds of human cancer cell lines (Caco-2, MCF-7, HT-1080) on type I collagen substrates, which are in two-dimensional coated collagen or three-dimensional fibrils form. All tested cells on coated collagen adhered and proliferated. However, in the case of collagen fibrils, the proliferation of cancer cells was suppressed. Furthermore, Akt activation, which is known as a cell-survival signal, was inhibited in cells on collagen fibrils. But the activation of ERK1//2 was not completely inhibited. In Caco-2 cells, delay of cell cycle progression and cell death occurred at the same time. Thus, cell division and cell death occurred at equivalent rates on the collagen fibrils, and cell growth seemed to be stopped. These results imply that the fibril form of collagen plays a potential role in inhibiting the growth of cancer cells. [ABSTRACT FROM AUTHOR]

Published
2011
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