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2,077 results on '"Konno, K."'

112. Site occupancy of Ga and Nb in Nd12.5Fe(sub bal)Ga0.3Nb0.2B6.2 during the hydrogenation, disproportionation, desorption, and recombination process

Author

Konno, K., Matsuura, M., Ikuta, N., Sakurai, M., and Mishima, C.

Subjects
Niobium -- Chemical properties, Gallium compounds -- Chemical properties, Disproportionation -- Analysis, Hydrogenation -- Analysis, Physics
Abstract

The effect of small additives of Ga and Nb in Nd12.5Fe(sub bal)Ga0.3Nb0.2B6.2 on their local structure during homogenization, disproportionation, desorption and recombination (HDDR) process is examined. The Fe(4c) sites of the recombined Nd2Fe14B crystal are occupied by Ga in the recombined state whereas a stable NdFeB compound is formed by Nb that remains undecomposed throughout the HDDR process

Published
2002

116. Magnetic properties of RCO3B2 (R=rare earth) compounds

Author

Ido, H., Nashima, O., Ito, T., Kaneda, T., Saito, Y., Konno, K., Yoshida, H., and Motokawa, M.

Subjects
Magnetism -- Research, Cobalt -- Research, Rare earth metals -- Research, Electric fields -- Analysis, Crystals -- Research, Physics
Abstract

A study was conducted to analyze the crystalline electric field at rare earth sites and the induced magnetic moment at a cobalt site in RCo3B2 compounds. The compounds were prepared using an arc furnace. High field magnetization processes were measured at different temperatures. Experimental results indicated that the crystal field parameter is very large and supports a significant magnetic moment induced at the cobalt site.

Published
1999

117. High frequency response of p-i-n photodiodes analyzed by an analytical model in Fourier space.

Author

Konno, K., Matsushima, O., Navarro, D., and Miura-Mattausch, M.

Subjects
*FREQUENCIES of oscillating systems, *SEMICONDUCTOR doping, *SOLUTION (Chemistry), *ELECTRICAL engineering, *PHOTODIODES, *DIFFUSION, *OSCILLATIONS
Abstract

A formulation of carrier transport in vertical p-i-n photodiodes is presented in Fourier space, taking into account diffusion effects of carriers outside the intrinsic region. High frequency response of photodiodes is investigated using the model. Calculated results show that diffusion limits the cutoff frequency characteristics of photodiodes with short intrinsic region length. Photocurrent calculations via the spectral method are in excellent agreement with two-dimensional device simulator results. The model can be utilized in circuit simulation because of its reduced computational runtime. [ABSTRACT FROM AUTHOR]

Published
2004
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119. Al-substitution effects on the magnetic properties of RCo5 (R=Y, Pr, Nd, and Sm) (Hard Magnets)

Author

Konno, K., Ido, H., Cheng, S.F., Sankar, S. G., and Wallace, W.E.

Subjects
Rare earth metals -- Research, Magnetization -- Research, Physics
Abstract

The effect of Al substitution on the magnetic characteristics of RCo5 (R=Y, Pr, Nd and Sm) was investigated using magnetic measurements. The results showed that Al substitution caused a considerable decrease in the in the Curie temperature, the Co-sublattice moment and the magnetocrystalline anisotropy of the R sublattice. The value of the Co-sublattice moments were determined by their directions in the crystal.

Published
1993

121. Comparison of gel-forming properties of silver carp (Hypophthalmichthys molitrix) surimi prepared in different seasons

Author

C. Yuan; Fukuda, Y., Kaneniwa, M.; S. Chen, Y. Cheng, X. Wang, and Konno, K.

Subjects
Gelation -- Research, Carp -- Research, Surimi -- Research, Business, Food/cooking/nutrition
Abstract

The gel-forming properties of silver carp surimi prepared in different seasons are compared. It was found that surimi prepared in winter and spring formed gel at 30 degree Celsius, while autumn and summer surimi required a higher temperature of 40 degree Celsius for gel formation.

Published
2005

122. P4289The impact of transient slow flow/no-reflow during rotational atherectomy on clinical outcomes

Author

Kyono, H., primary, Nakashima, M., additional, Takamura, S., additional, Nakaya, H., additional, Nishide, S., additional, Nara, Y., additional, Sasaki, K., additional, Katayama, T., additional, Nagura, F., additional, Kawashima, H., additional, Hioki, H., additional, Watanabe, Y., additional, Konno, K., additional, Yokoyama, N., additional, and Kozuma, K., additional

Published
2017
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125. Effects of temperatures and carbon dioxide nanobubbles on superior electric storage for anodically oxidized films of AlY10 amorphous alloy.

Author

Fukuhara, Mikio, Kuroda, Tomoyuki, Hasegawa, Fumihiko, Takahashi, Masayoshi, Suwa, Tomoyuki, Hashida, Toshiyuki, Sato, Kazuhisa, Nishijima, Masahiko, and Konno, K.

Subjects
AMORPHOUS alloys, TEMPERATURE effect, CAPACITORS, WATER clusters, CARBON oxides, CERAMIC capacitors, CARBON dioxide
Abstract

The effects of temperature and nanometer-sized bubbles (NBs) on a superior electric storage capacitor for anodically oxidized films of AlY10 amorphous alloys were determined at temperatures ranging from 275 to 298 K in 0.4 M H2SO4 solutions with NBs of ozone, oxygen, and carbon dioxide. The AAO specimen obtained by solution with carbon dioxide NBs at 278 K showed longer discharging time. The discharging time increases with increasing charging time and then saturates after around 70 s. The increment in temperature makes the structure from simple series capacitor with large capacitance to simple parallel capacitor with lower capacitance and larger resistance. The stability of NBs in water could be explained by enclosure in protonated polyhedral water clusters. The collapse of clusters with oxygen NBs result in the formation of OH− radicals and its resulting elution of Al, while carbon oxide NBs prevent the formation of OH− radicals, promoting sluggish oxidation that is required for the formation of AlO6 clusters. [ABSTRACT FROM AUTHOR]

Published
2019
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126. Voltage-gated Sodium Channels Isoform-specific Effects of Pompilidotoxins

Author

Schiavon, E, Stevens, M, Zaharenko, A, Konno, K, Tytgat, J, Wanke, E, Konno K, WANKE, ENZO, Schiavon, E, Stevens, M, Zaharenko, A, Konno, K, Tytgat, J, Wanke, E, Konno K, and WANKE, ENZO

Abstract

Pompilidotoxins (PMTXs, alpha and beta) are small peptides consisting of 13 amino acids purified from the venom of the solitary wasps Anoplius samariensis (alpha-PMTX) and Batozonellus maculifrons (beta-PMTX). They are known to facilitate synaptic transmission in the lobster neuromuscular junction, and to slow sodium channel inactivation. By using beta-PMTX, alpha-PMTX and four synthetic analogs with amino acid changes, we conducted a thorough study of the effects of PMTXs on sodium current inactivation in seven mammalian voltage-gated sodium channel (VGSC) isoforms and one insect VGSC (DmNa(v)1). By evaluating three components of which the inactivating current is composed (fast, slow and steady-state components), we could distinguish three distinct groups of PMTX effects. The first group concerned the insect and Na(v)1.6 channels, which showed a large increase in the steady-state current component without any increase in the slow component. Moreover, the dose-dependent increase in this steady-state component was correlated with the dose-dependent decrease in the fast component. A second group of effects concerned the Na(v)1.1, Na(v)1.2, Na(v)1.3 and Na(v)1.7 isoforms, which responded with a large increase in the slow component, and showed only a small steady-state component. As with the first group of effects, the slow component was dose-dependent and correlated with the decrease in the fast component. Finally, a third group of effects concerned Na(v)1.4 and Na(v)1.5, which did not show any change in the slow or steady-state component. These data shed light on the complex and intriguing behavior of VGSCs in response to PMTXs, helping us to better understand the molecular determinants explaining isoform-specific effects.

Published
2010

131. General lectures (II)

Author

Segawa, K., Nakazawa, S., Koide, N., Imai, K., Matsuo, N., Yamamoto, Y., Shiobara, M., Shimada, H., Kawai, K., Machida, K., Okabe, N., Hoshi, Y., Koizumi, Y., Watanuki, T., Hiroshima, Y., Matsusaka, Y., Katase, K., Sakuma, Y., Matoba, N., Murata, N., Toyama, Y., Murai, S., Nukaga, A., Ishimatsu, N., Watanabe, Y., Abe, M., Ono, Y., Hirai, K., Iwabuchi, S., Suzuki, K., Aoki, T., Masamura, K., Yoshida, K., Ikeuchi, J., Nagao, F., Kobayashi, A., Toriie, S., Nakajima, M., Kohli, M., Ida, K., Kawai, K., Masuda, M., Hattori, T., Fujita, S., Tamada, T., Inoue, K., Usui, T., Yamaya, S., Ohtsuka, K., Shiraki, Y., Fujishima, S., Tochikubo, O., Miyamoto, S., Ueda, A., Asano, K., Kunisada, M., Miyake, H., Fujii, Y., Yoshimoto, S., Hiramatsu, K., Nakano, S., Takeda, T., Kitamura, K., Horiguchi, Y., Okada, K., Okada, M., Kuwabara, T., Tanaka, M., Konno, K., Hattori, T., Isobe, K., Iwasaki, A., Unoura, T., Matsumoto, M., Yoshida, T., Takahashi, I., Abe, M., Maeda, H., Hayashi, T., Koizumi, H., Iwasaki, M., Takahashi, K., Honda, T., Ariga, K., Mohri, S., Suga, Y., Ono, T., Kobayashi, K., Mizuno, T., Sameshima, Y., Shiozaki, Y., Sasakawa, M., Hiramatsu, A., Ikehara, K., Nagata, T., Tatsumi, K., Abe, M., Aoki, M., Iwasaki, S., Aizawa, T., Kajiwara, K., Sata, K., Omata, S., Imamura, K., Kondo, K., Sajima, H., Sato, Y., Kiryu, H., Mimoto, S., Masuoka, T., Kira, K., Mizumoto, R., Kuratsuka, H., Honjo, I., Hojo, Y., Nakajima, H., Tosaka, T., Arai, O., Kobayashi, N., Obata, N., Ito, S., Takaoka, T., Uragami, Y., Kitamura, Y., Kishi, S., Fujii, S., Okuda, H., Hirano, K., Kano, H., Ogino, M., Ueda, Y., Nishiwaki, K., Iwamura, N., Aoki, T., Hiramatsu, K., Kamada, T., Suematsu, T., Fusamoto, H., Okuda, H., Abe, H., Katayama, S., Yamaguchi, K., Fukuda, M., Ishii, T., Kaito, I., Sato, S., Sasaki, H., Onodera, H., Yamanaka, M., Akagi, K., Miyazaki, S., Okumura, M., Omae, T., Nakamura, Y., Wada, M., Nakai, Y., Inoue, S., Arima, T., Yamasaki, S., Takano, T., Katsuta, Y., Yano, T., Isoda, K., Aramaki, T., Fukuda, N., Ichikawa, T., Okumura, H., Adachi, Y., Inoue, R., Iwasaki, Y., Tanaka, S., Yamamoto, T., Wakisaka, G., Nakaya, H., Takase, S., Ikegami, F., Takada, A., Kobayashi, K., Takeuchi, J., Kato, Y., Funayama, A., Kakumu, S., Ito, S., Okuyama, S., Taoka, Y., Endo, T., Chizuka, R., Yanagida, T., Chizuka, S., Usui, H., Ando, T., Takai, T., Wakahara, T., Kojima, M., Fukazawa, T., Takahashi, Y., Miyamura, S., Urakawa, T., Shima, T., Miyaji, K., Okazaki, T., Kashimura, S., Koyama, K., Yamauchi, H., Matsuo, Y., Takagi, Y., Muto, I., Owada, Y., Otowa, T., Sato, T., Naito, C., Okada, K., Sugawara, K., Nokiba, T., Fujii, Y., Kido, H., Sasaki, M., Sugai, Y., Nishimura, G., Nanbu, H., Kamiyama, Y., Yamada, T., Yamaoka, Y., Takeda, H., Ohsawa, T., Kamano, T., Mizukami, T., Kitamura, O., Ozawa, K., Takasan, H., Honjo, I., Miyasaki, R., Katayama, T., Amakawa, T., Hirose, K., Furukawa, Y., Noguchi, M., Okamoto, M., Maezawa, H., Tanaka, N., Yamada, S., Hisata, T., Hata, C., Sawa, J., Kato, Y., Mituda, Y., Oohira, S., Hayasaka, A., Okuyama, T., Fukui, S., Takeda, T., Furuichi, T., Yamamitsu, S., Yamauchi, K., Konishi, Y., Maeda, S., Setoyama, S., Otsuji, S., Ibata, T., Niu, H., Ogawa, A., Tujioka, E., Maeda, T., Takewa, M., Matumoto, T., Tamada, K., Maeda, A., Sumita, H., Iseki, Y., Yukawa, S., Nitta, Y., Isida, K., Nomoto, H., Setoyama, S., Maeda, S., Otsuji, S., Sato, R., Sato, G., Toyokawa, S., Yamamoto, G., Ohtomi, S., Haga, M., Ueno, Y., Fukuda, M., Endo, R., Yokota, T., Ohsawa, J., Kohno, A., Ohtoshi, E., Yasugi, H., Ichikawa, H., Mizumoto, R., Honjo, I., Ando, K., Suzuki, H., Nishiwaki, T., Kishimoto, T., Miki, T., Takeshige, K., Sawada, M., Hidemura, R., Yamamoto, S., Itoh, S., Kashiwagi, T., Kishida, M., Imamura, O., Suematus, T., Kamada, T., Sakoda, K., Kawada, T., Arima, Y., Kamimura, T., Takesue, M., Katsuki, T., Akita, H., Yakeishi, Y., Takehisa, I., Miyasato, K., Yoshida, H., Hidemura, R., Kubota, K., Aoki, S., Suzuki, S., Kishimoto, T., Miyahara, T., Ando, K., Nishiwaki, T., Miki, T., Takeshige, K., Sawada, M., Itoh, S., Yamamoto, S., Fujiwara, K., Sakai, T., Oda, T., Igarashi, S., Fukuhara, M., Tsujii, T., Tamura, T., Matsuoka, Y., Takahashi, H., Sakamoto, T., Fukuda, S., Oku, M., Matsui, T., Morita, T., Oyazato, Y., Kimura, K., Moriya, W., Fukui, S., Suzuki, K., Morimoto, S., Tsuiki, S., Shoji, K., Nakai, Y., Hata, M., Kubo, J., Yoshizawa, K., Nagayama, K., Ozawa, Y., Yoshida, M., Horiguchi, M., Machii, A., Nitta, Y., Aiso, Y., Kitahara, N., Kitazawa, E., Fukuda, K., Saiti, N., Murakami, Y., Nao, Y., Okazaki, I., Funatsu, K., Maruyama, K., Takagi, B., Yasuraoka, S., Ishii, K., Matsuzaki, S., Takahashi, H., Ishii, H., Kamegaya, K., Sambe, K., Ishikawa, H., Tajima, Y., Kuroda, A., Ishihara, Y., Sato, N., Ishikawa, I., Noro, T., Kakumoto, Y., Mekjian, H. S., Thomford, N. R., Yokomura, T., Adachi, S., Yamamoto, A., Saito, I., Kawamura, A., Miyata, M., Kasai, S., Kawanishi, N., Tamaki, A., Mito, M., Kasai, Y., Hasumi, A., Uchiyama, T., Tachikawa, Y., Takanashi, T., Kanke, T., Matsuda, K., Takanashi, T., Kanke, T., Matsuda, K., Hamana, G., Sakuma, M., Sugita, T., Tomita, K., Yamasaki, S., Tsuzuki, T., Uekusa, M., Matsuzaki, M., Takagi, B., Tsuchiya, M., Uchimura, M., Murohisa, T., Muto, Y., Ishigaki, J., Waki, S., Tsuchiya, R., Sho, M., Furukawa, M., Suzuki, N., Nagashima, H., Matsushiro, T., Saitoh, T., Nakamura, N., Hatanaka, T., Kobayashi, N., Nakamura, Y., Sato, T., Tooi, K., Tanaka, Y., Kadokura, N., Okada, Y., Yanakgi, I., Tanaka, N., Sekiya, V. M., Adachi, K., Miyashita, M., Moriyama, Y., Onda, M., Yoshioka, M., Teraoka, T., Shimizu, Y., Fujishima, G., Ookawa, K., Miki, M., Shirota, A., Aihara, K., Shiga, T., Sano, H., Hayashi, S., Hori, M., Sato, H., Chuman, Y., Tsukase, S., Nakahara, N., Ehira, S., Setoyama, S., Nishimata, H., Irisa, T., Tokutome, K., Nakashima, Y., Koga, H., Yokoyama, H., Otsuji, T., Chujo, Y., Yamamoto, T., Gotoda, S., Uchiyama, S., Kosaki, G., Ohkura, H., Mukojima, T., Hattori, N., Sasaki, O., Soejima, K., Inokuchi, K., Utsunomiya, J., Maki, T., Iwama, T., Matsunaga, Y., Shimomura, T., Nakajima, T., Ichikawa, S., Miyanaga, T., Sengoku, K., Hamaguchi, E., Aoki, N., Nomura, T., Matsuoka, A., Suzuki, N., Nagahama, A., Kazumi, T., Miyawaki, H., Sakamoto, T., Miyasaki, K., Kato, K., Miyazaki, Y., Harada, N., Yamada, K., Tashiro, S., Sakai, K., Ho, N., Murayama, H., Yada, M., Sakabe, T., Shimizu, H., Kuroki, M., Nishida, S., Kato, K., Ishiyama, S., Yukawa, K., Hayashi, M., Soh, K., Doi, K., Fukuda, M., Nakagawa, A., Yukawa, E., Uematsu, Y., Nara, K., Hattori, H., Watanabe, M., Yoshida, H., Sato, K., Okuse, S., Sato, K., Murotani, T., Takasu, S., Konta, M., Uchiya, T., Fujimaki, N., Yoshida, K., Yoshikawa, K., Uchida, M., Nakamura, N., Nagao, F., Kawana, S., Tamura, K., Hashimoto, T., Kobayashi, K., Hara, T., Nosaka, J., Fukui, O., Inaba, E., Otsukasa, S., Sanada, K., Hiraide, H., Senyo, G., Ootani, A., Nakayama, T., Takei, S., Miki, H., Tanaka, M., Minota, S., Nakayama, K., Nakagawa, K., Shiraishi, T., Kawauchi, H., Nagaya, H., Mizushima, K., Tachimi, Y., Namiki, M., Masuda, K., Mitsutani, N., Mukuta, T., Koizumi, T., Takeuchi, T., Nemoto, T., Takabayashi, H., Takagi, M., Hongo, Y., Kojima, H., Nishimura, M., Hino, S., Hirayama, J., Nakamura, M., Irisa, T., Koga, S., Hirayama, C., Kikuch, S., Ito, M., Hidano, S., Ooya, T., Banno, H., Tomura, A., Kato, K., Koyama, T., Takei, T., Tomimura, T., Yamauchi, M., Kobayashi, K., Nakaya, Y., Takase, S., Kato, Y., Takeuchi, J., Ikegami, F., Matsuda, Y., Takada, A., Udo, K., Kojima, M., Hukuda, N., Kametani, M., Miyagawa, T., Wakahara, T., Takahashi, Y., Imaeda, T., Senda, K., Fujita, S., Okubo, H., Kanoda, K., Miyashita, B., Ishizuka, H., Goto, T., Oto, K., Kaneda, H., Hase, M., Matsuda, J., Kawai, T., Ikehara, H., Baba, S., Ishii, M., Tozawa, T., Inoue, E., Mizuno, N., Saeki, S., Nakaji, T., Narabayashi, T., Okuno, T., Yamada, H., Tanno, M., Chiba, K., Iio, M., Shibata, K., Furuhashi, F., Mizuochi, K., Ohashi, S., Kato, K., Nakano, M., Otsuka, S., Irie, M., Akima, M., Maruyama, Y., Oyamada, F., Nagata, E., Kubo, Y., Arishima, T., Otsuyama, Y., Kaneto, A., Shimogawa, Y., Tanigawa, K., Okabe, N., Nakajima, K., Onishi, S., Kasahara, A., Shimizu, T., Ikehara, Y., Tajima, H., Okamoto, A., Komibuchi, T., Negoro, T., Nihonsugi, A., Ishii, M., Tozawa, T., Ogawa, Y., Otani, H., Ishida, M., Yashima, H., Shoji, K., Tsuiki, S., Morimoto, S., Nakai, Y., Ryo, M., Ozawa, Y., Tanaka, T., Horiguchi, M., Taketa, K., Watanabe, A., Yumoto, Y., Tanaka, A., Takesue, A., Aoe, H., Ueda, M., Shimamura, J., Kosaka, K., Kashiwara, E., Orita, K., Konaga, E., Suzuki, K., Tanaka, S., Kaneda, S., Ogawa, K., Tamura, H., Okanishi, S., Ueda, T., Horie, H., Kamachi, M., Asihara, T., Daido, R., Izumi, T., Kurihara, M., Sumida, M., Haraikawa, M., Hayakawa, H., Shirakabe, H., Yasui, A., Noguchi, M., Okamoto, M., Furukawa, Y., Miyasaki, R., Hirose, K., Katayama, T., and Maezawa, H.

Published
1974
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136. Site occupancy of Ga and Nb in Nd[sub 12.5]Fe[sub bal]Ga[sub 0.3]Nb[sub 0.2]B[sub 6.2] during the hydrogenation, disproportionation, desorption, and recombination process.

Author

Konno, K., Matsuura, M., Ikuta, N., Sakurai, M., and Mishima, C.

Subjects
*GALLIUM, *NIOBIUM, *FLUORESCENCE spectroscopy
Abstract

The local structure changes around Ga and Nb in Nd[sub 12.5]Fe[sub bal]Ga[sub 0.3]Nb[sub 0.2]B[sub 6.2] during homogenization, disproportionation, and recombination processes are studied by fluorescence XAFS in order to understand the roles of Ga and Nb on the improvement of (BH)[sub max]. Comparing the observed XAFS of the GaK edge with the calculated ones, Ga is proved to occupy preferentially the Fe(4c) site in Nd[sub 2]Fe[sub 14]B structure after homogenization and recombination, while it dissolves in α-Fe after the disproportionation. On the other hand, XAFS results of the Nb K edge does not change in the whole hydrogenation, disproportionation, desorption, and recombination process; the XAFS results of Nb indicate the formation of a stable NbFeB phase in the homogenized state. [ABSTRACT FROM AUTHOR]

Published
2002
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139. Angiotensin II 1 receptor-mediated contraction of pulmonary artery and its modulation by prolylcarboxypeptidase

Author

J. Tamaoki, K. Isono, Etsuko Tagaya, Atsushi Chiyotani, F. Sugimoto, and Konno K

Subjects
Male, medicine.medical_specialty, Endothelium, Pyridines, Physiology, medicine.drug_class, Tetrazoles, Carboxypeptidases, In Vitro Techniques, Pulmonary Artery, Arginine, Nitric Oxide, Losartan, Muscle, Smooth, Vascular, Angiotensin Receptor Antagonists, chemistry.chemical_compound, Dogs, Isometric Contraction, Physiology (medical), Internal medicine, Hypoxic pulmonary vasoconstriction, Renin–angiotensin system, medicine, Animals, Protease Inhibitors, Receptor, Receptors, Angiotensin, Chemistry, Angiotensin II, Biphenyl Compounds, Phosphoramidon, Imidazoles, Receptor antagonist, NG-Nitroarginine Methyl Ester, medicine.anatomical_structure, Endocrinology, cardiovascular system, Endothelium, Vascular, medicine.symptom, Vasoconstriction
Abstract

To determine the subtype of angiotensin II (ANG II) receptor involved in the contraction of pulmonary artery and to elucidate its possible modulation by endogenous peptidases, we studied canine isolated pulmonary arterial rings under isometric conditions in vitro. Addition of ANG II caused a concentration-dependent contraction, an effect that was not altered by the ANG II 2 receptor antagonist EXP655 but was depressed by the ANG II 1 receptor antagonist DuP 753 so that the ANG II response curves were displaced to higher concentration by 1.5–2.0 log U (P < 0.001). Pretreatment of tissues with the prolylcarboxypeptidase (PCP) inhibitor p-methylphenyl sulfonyl-fluoride potentiated the ANG II-induced contraction, with the concentration required to produce a half-maximal effect of ANG II being decreased from 4.1 +/- 0.9 x 10(-9) to 3.8 +/- 0.5 x 10(-10) M (P < 0.001), whereas other peptidase inhibitors such as p-chloromercuriphenyl sulfonic acid, amastatin, and phosphoramidon had no effect. The p-methylphenyl sulfonylfluoride-induced potentiation was abolished by the removal of endothelium, but it was still observed in the presence of NG-nitro-L-arginine methyl ester in the endothelium-intact tissues. The PCP activity in the tissues was reduced by the removal of endothelium from 645 +/- 88 to 91 +/- 29 nmol.mg protein-1.h-1 (P < 0.001), and cultured endothelium had the activity of 404 +/- 39 nmol.mg protein-1.h-1. These results suggest that ANG II contracts pulmonary artery via ANG II 1 receptor and that PCP localized to the endothelium may have a modulatory role in the ANG II-induced pulmonary vasoconstriction.

Published
1994

140. Effect of histamine on airway transepithelial potential difference in vivo

Author

Mitsuko Kondo, Konno K, Hisashi Takemura, Atsushi Chiyotani, Satomi Takeuchi, Etsuko Tagaya, and Jun Tamaoki

Subjects
Chemistry, Pharmacology, Amiloride, chemistry.chemical_compound, In vivo, Immunology, medicine, Channel blocker, Early phase, Airway, Ion transporter, Histamine, Transepithelial potential difference, medicine.drug
Abstract

Histamine is one of the important mediators that causes a variety of allergic inflammatory responses in the airway. In the present study, to determine the effect of histamine on ion transport function across the airway mucosa, we measured transepithelial potential difference (PD) of rabbit tracheal mucosa under open-circuit conditionsin vivo. A high impedance voltmeter was used to measure PD between a fluid-filled and perfused recording bridge located on the airway surface and a reference bridge in the subcutaneous space. Addition of histamine to the perfusate produced a biphasic response of PD consisting of a rapid decrease within 15 sec and the subsequent plateau, which was followed by a sustained increase after 5 min of addition. Pretreatment of tracheal mucosa with the Na channel blocker amiloride greatly inhibited the early phase reduction of PD in response to histamine, but had no effect on the late phase elevation. On the other hand, pretreatment with the Cl channel blocker diphenylamine-2-carboxylate inhibited the late phase increase of PD completely.These results indicate that early and late responses of PD are dependent on Na and Cl, respectivly, and suggest that histamine may inhibit Na absorption and stimulate Cl secretion in the airway mucosa.

Published
1994

141. Effects of Prostacyclin and Beraprost on Ciliary Motilitγ of Rabbit Airway Epithelium

Author

Kiyoshi Takeyama, Konno K, S Sakai, Etsuko Tagaya, Atsushi Chiyotani, and J. Tamaoki

Subjects
Male, medicine.medical_specialty, Prostacyclin, In Vitro Techniques, Biology, Epithelium, Internal medicine, Cyclic AMP, medicine, Animals, Cilia, Pharmacology, Tracheal Epithelium, Lagomorpha, General Medicine, biology.organism_classification, Epoprostenol, Beraprost, Trachea, Endocrinology, medicine.anatomical_structure, Respiratory epithelium, Rabbits, Intracellular, medicine.drug, Respiratory tract
Abstract

The effects of prostacyclin and its stable analog beraprost on ciliary beat frequency (CBF) of rabbit tracheal epithelium were studied by a microphoto-oscillation technique in vitro. Addition of these drugs increased CBF in a dose-dependent fashion: the maximal increase from the baseline value and the drug concentration required to produce a half-maximal effect were 13.3 +/- 2.0% (p < 0.05) and 1.8 +/- 0.4 x 10(-7) mol/l for prostacyclin and 30.8 +/- 3.4% (p < 0.001) and 1.6 +/- 0.5 x 10(-7) mol/l for beraprost. These effects were accompanied by the increase in intracellular cyclic AMP levels. Thus, prostacyclin and beraprost may stimulate ciliary motility and, hence, mucociliary transport through the production of cyclic AMP.

Published
1994

144. Chemical Defence and Toxins of Plants

Author

Yamane, H., Konno, K., Sabelis, M., Takabayashi, J., Sassa, T., Oikawa, H., Mander, L., Lui, H.W., and Population Biology (IBED, FNWI)

Subjects
Herbivore, Microbial pathogenesis, Chlorosis, Polyketide synthase, Botany, biology.protein, food and beverages, Wilting, Chemical defense, Biology
Abstract

Higher plants protect themselves by producing a variety of secondary metabolites and proteins that are involved in defense against herbivores as well as microbial pathogens. Concerning microbial pathogenesis in plants, in many cases, it is known that phytotoxins that are produced by plant pathogens play an important role in disease development causing chlorosis, necrosis, or wilting. This chapter mainly focuses on the chemical structures, distribution, and biosynthesis of defense-related natural products and phytotoxins.

Published
2010

145. Prostaglandin D2increases Cl secretion across canine tracheal epithelium through cyclooxygenase stimulation and cAMP production

Author

K. Isono, Takao Takizawa, Konno K, Noritaka Sakai, T. Kanemura, F. Yamauchi, Jun Tamaoki, and Atsushi Chiyotani

Subjects
Male, medicine.medical_specialty, Physiology, Prostaglandin, In Vitro Techniques, Epithelium, chemistry.chemical_compound, Dogs, Chlorides, Chloride Channels, Internal medicine, Cyclic AMP, Electrochemistry, medicine, Animals, Channel blocker, Transepithelial potential difference, Prostaglandin D2, Membrane Proteins, Transport inhibitor, Adenosine, Amiloride, Trachea, Endocrinology, chemistry, Prostaglandin-Endoperoxide Synthases, Respiratory epithelium, Female, medicine.drug
Abstract

Prostaglandin (PG) D2 is one cyclo-oxygenase product of arachidonic acid metabolites that may play a role in the pathogenesis of asthma. To determine the effect of PGD2 on ion transport by airway epithelium and its mechanism of action, we measured bioelectric properties of canine cultured tracheal epithelium under short-circuit conditions in vitro. PGD2 (10(-7) M) increased short-circuit current (Isc) from 5.5 +/- 1.2 to 14.1 +/- 2.9 microA cm-2 (means +/- SE, P less than 0.01) when added to the mucosal solution, and to 22.2 +/- 3.8 microA cm-2 (P less than 0.001) when added to the submucosal solution, an effect that was accompanied by the corresponding increases in transepithelial potential difference and conductance. These effects were dose-dependent. The PGD2-induced increase in Isc was not altered by preincubation of cells with autonomic antagonists (phentolamine, propranolol, atropine), the lipoxygenase inhibitor AA-861, the protein kinase C inhibitor H-7, or the Na channel blocker amiloride, but it was inhibited by each of indomethacin, piroxicam, the Cl channel blocker diphenylamine-2-carboxylate, the Cl transport inhibitor furosemide, and Cl-free medium. Intracellular adenosine 3',5'-cyclic monophosphate (cAMP) levels were dose-dependently increased by PGD2. These results suggest that PGD2 may selectively stimulate airway epithelial Cl secretion via cyclo-oxygenase- and cAMP-dependent pathway.

Published
1992

146. Lignified Materials as Medicinal Resources. V. Anti-HIV(Human Immunodeficiency Virus) Activity of Some Synthetic Lignins

Author

Naoki Yamamoto, Tsutomu Murakami, Konno K, Yutaka Kawazoe, T. Naoe, Hiroshi Sakagami, and Hideki Nagashima

Subjects
Reducing agent, Chemistry, virus diseases, General Chemistry, General Medicine, Antiviral Agents, Lignin, Virus, Ferulic acid, chemistry.chemical_compound, Cytopathogenic Effect, Viral, Biochemistry, Antigen, HIV-2, Drug Discovery, HIV-1, Caffeic acid, Humans, Cytotoxic T cell, Ceric ammonium nitrate
Abstract

A class of synthetic lignins (dehydrogenation polymers of p-coumaric acid, ferulic acid, and caffeic acid) inhibited cytopathogenicity of HIV-1 and HIV-2 infection. The ratio of cytotoxic to anti-HIV (human immunodeficiency virus) doses depended strongly on conditions during polymer preparation. The activity increased when polymers were treated with reducing agent NaBH4, whereas it decreased when treated with oxidizing agent ceric ammonium nitrate. The polymers inhibited expression of HIV-specific antigen in the infected cells and also inhibited HIV-binding to the cells, but not completely, even at doses that almost completely inhibited the HIV-induced cytopathogenic effect. These results suggest that lignin structure, regardless of whether synthetic or natural, may inhibit HIV replication by an unidentified process, and thus prove to be a new class of anti-HIV agents possibly effective in the treatment of AIDS (acquired immunodeficiency syndrome).

Published
1992

147. Neoplastic Alteration of a Membrane-associated Sialidase of Rat Liver

Author

Konno K, Shigeru Tsuiki, Junji Sagawa, and Taeko Miyagi

Subjects
Male, Rat liver, Cancer Research, Immunoprecipitation, Neuraminidase, Membrane sialidase, Biology, Sialidase, Article, Liver Neoplasms, Experimental, Gangliosides, Animals, Antiserum, Hepatoma, Fetus, Ganglioside, Cell Membrane, Liver Neoplasms, Brain, Rats, Inbred Strains, Precipitin, Precipitin Tests, Pathophysiology, Rats, Membrane, Liver, Oncology, Biochemistry
Abstract

Rat liver participate fraction contains two types of membrane‐associated and gangliosides‐hydrolyzing sialidase, which have been shown to be identical to two membrane‐associated sialidases of rat brain (I and II) chromatographically, immunologically and in substrate specificity. Chromatography on AH‐Sepharose 4B of the membrane sialidases of rat primary hepatoma induced by 3′‐methyl‐4‐dimethylaminoazobenzene (MeDAB) further revealed that hepatocarcinogenesis induces a marked decrease in sialidase II but no decrease in sialidase I. Using antisera against sialidases I and II of rat brain, immunoprecipitation studies of the solubilized particulate fractions of rat liver and MeDAB‐hepatoma gave results similar to those obtained chromatographically. Using the same immunological technique, sialidase II but not sialidase I was found to be decreased in AH109 A hepatoma and in regenerating and fetal liver.

Published
1990

148. Biochemical and Immunological Studies on Two Distinct Ganglioside-Hydrolyzing Sialidases from the Particulate Fraction of Rat Brain1

Author

Konno K, Shigeru Tsuiki, Taeko Miyagi, Junji Sagawa, and Shizuo Handa

Subjects
chemistry.chemical_classification, Ganglioside, Chromatography, biology, General Medicine, Sialidase, Biochemistry, Sepharose, NEU2, Enzyme, chemistry, Sephadex, biology.protein, Glycoprotein, Molecular Biology, Neuraminidase
Abstract

Ganglioside-hydrolyzing sialidase activity was solubilized from rat brain particulate fraction by using Triton X-100 plus sodium deoxycholate. When chromatographed on AH-Sepharose 4B, the solubilized activity was resolved into two peaks, which were designated sialidases I and II in order of elution. The two sialidases were purified by using sequential chromatographies on Octyl-Sepharose CL-4B, Phenyl-Sepharose CL-4B, and Sephadex G-200. Sialidase II was purified further by Mono Q-FPLC. Overall purification was 450- and 2,150-fold, for sialidases I and II, respectively. Purified sialidases I and II were maximally active at near pH 5.0 and exhibited M = 70,000 by gel filtration. Sialidase I hydrolyzed gangliosides but scarcely other substrates including 4-methylumbelliferyl-NeuAc (4MU-NeuAc). Sialidase II hydrolyzed oligosaccharides, glycoproteins, and 4MU-NeuAc although gangliosides appeared to be preferential substrates. Sialidase II cleaved GM2 much faster than sialidase I. An antibody raised in rabbits against sialidase I reacted with only sialidase I and an antibody against sialidase II reacted with only sialidase II. A subcellular distribution study suggested sialidase I in the synaptosomal membrane and sialidase II in the synaptosomal and lysosomal membranes, and this was verified by using the above antibodies.

Published
1990

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