Search

Your search keyword '"Hyodo, Susumu"' showing total 537 results
Start Over Author "Hyodo, Susumu"
537 results on '"Hyodo, Susumu"'

151. Corrigendum to “Identification of mRNAs coding for mammalian-type melanin-concentrating hormone and its receptors in the scalloped hammerhead shark Sphyrna lewini” [Gen. Comp. Endocrinol. 179 (2012) 78–87]

Author

Mizusawa, Kanta, primary, Amiya, Noriko, additional, Yamaguchi, Yoko, additional, Takabe, Souichirou, additional, Amano, Masafumi, additional, Breves, Jason P., additional, Fox, Bradley K., additional, Gordon Grau, E., additional, Hyodo, Susumu, additional, and Takahashi, Akiyoshi, additional

Published
2014
Full Text
View/download PDF

154. Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya

Author

Falcón, Jack, primary, Coon, Steven L., additional, Besseau, Laurence, additional, Cazaméa-Catalan, Damien, additional, Fuentès, Michaël, additional, Magnanou, Elodie, additional, Paulin, Charles-Hubert, additional, Boeuf, Gilles, additional, Sauzet, Sandrine, additional, Jørgensen, Even H., additional, Mazan, Sylvie, additional, Wolf, Yuri I., additional, Koonin, Eugene V., additional, Steinbach, Peter J., additional, Hyodo, Susumu, additional, and Klein, David C., additional

Published
2013
Full Text
View/download PDF

157. Osmoregulation in elephant fish Callorhinchus Milii (Holocephali), with special reference to the rectal gland

Author

Hyodo, Susumu, Bell, Justin D., Healy, Jillian M., Kaneko, Toyoji, Hasegawa, Sanae, Takei, Yoshio, Donald, John, Toop, Tes, Hyodo, Susumu, Bell, Justin D., Healy, Jillian M., Kaneko, Toyoji, Hasegawa, Sanae, Takei, Yoshio, Donald, John, and Toop, Tes

Abstract

Osmoregulatory mechanisms in holocephalan fishes are poorly understood except that these fish are known to conduct urea-based osmoregulation as in elasmobranchs. We, therefore, examined changes in plasma parameters of elephant fish Callorhinchus milii, after gradual transfer to concentrated (120%) or diluted (80%) seawater (SW). In control fish, plasma Na and urea concentrations were about 300 mmol l–1 and 450 mmol l–1, respectively. These values were equivalent to those of sharks and rays, but the plasma urea concentration of elephant fish was considerably higher than that reported for chimaeras, another holocephalan. After transfer to 120% SW, plasma osmolality, urea and ion concentrations were increased, whereas transfer to 80% SW resulted in a fall in these parameters. The rises in ion concentrations were notable after transfer to 120% SW, whereas urea concentration decreased predominantly following transfer to 80% SW. In elephant fish, we could not find a discrete rectal gland. Instead, approximately 10 tubular structures were located in the wall of post-valvular intestine. Each tubular structure was composed of a putative salt-secreting component consisting of a single-layered columnar epithelium, which was stained with an anti-Na+,K+-ATPase serum. Furthermore, Na+,K+-ATPase activity in the tubular structures was significantly increased after acute transfer of fish to concentrated SW (115%). These results suggest that the tubular structures are a rectal gland equivalent, functioning as a salt-secreting organ. Since the rectal gland of elephant fish is well developed compared to that of Southern chimaera, the salt-secreting ability may be higher in elephant fish than chimaeras, which may account for the lower plasma NaCl concentration in elephant fish compared to other chimaeras. Since elephant fish have also attracted attention from a viewpoint of genome science, the availabil

Published
2007

161. The fifth neurohypophysial hormone receptor is structurally related to the V2-type receptor but functionally similar to V1-type receptors

Author

Yamaguchi, Yoko, primary, Kaiya, Hiroyuki, additional, Konno, Norifumi, additional, Iwata, Eri, additional, Miyazato, Mikiya, additional, Uchiyama, Minoru, additional, Bell, Justin D., additional, Toop, Tes, additional, Donald, John A., additional, Brenner, Sydney, additional, Venkatesh, Byrappa, additional, and Hyodo, Susumu, additional

Published
2012
Full Text
View/download PDF

162. Cloning of two members of the calcitonin-family receptors from stingray, Dasyatis akajei: Possible physiological roles of the calcitonin family in osmoregulation

Author

Suzuki, Nobuo, primary, Sekiguchi, Toshio, additional, Satake, Honoo, additional, Kato, Kanoko, additional, Nishiyama, Yudai, additional, Takahashi, Hideya, additional, Danks, Janine A., additional, Martin, T. John, additional, Hattori, Atsuhiko, additional, Nakano, Masaki, additional, Kakikawa, Makiko, additional, Yamada, Sotoshi, additional, Ogoshi, Maho, additional, Hyodo, Susumu, additional, Yamaguchi, Yoko, additional, Chowdhury, Vishwajit S., additional, Hayakawa, Kazuichi, additional, Funahashi, Hisayuki, additional, Sakamoto, Tatsuya, additional, and Sasayama, Yuichi, additional

Published
2012
Full Text
View/download PDF

166. List of Contributors

Author

Amano, Masafumi, Ando, Hironori, Andoh, Tadashi, Daubnerova, Ivana, Donald, John A., Forgan, Leonard G., Haraguchi, Shogo, Hayakawa, Yoichi, Hirako, Satoshi, Hyodo, Susumu, Iguchi, Taisen, Inui, Akio, Kageyama, Haruaki, Kaiya, Hiroyuki, Kakizawa, Sho, Kanda, Shinji, Kaneko, Hiroyuki, Kataoka, Hiroshi, Katayama, Hidekazu, Kato, Takashi, Katsu, Yoshinao, Katsuura, Goro, Kawada, Tsuyoshi, Kimura, Atsushi P., Kobayashi, Yuki, Konno, Norifumi, Konogami, Tadafumi, Minakata, Hiroyuki, Mita, Masatoshi, Miyagawa, Shinichi, Miyazato, Mikiya, Mizoguchi, Akira, Mizusawa, Kanta, Mori, Kenji, Morishita, Fumihiro, Moriyama, Shunsuke, Nagasaki, Hiroshi, Nagata, Shinji, Nakagawa, Yoshiaki, Nakamachi, Tomoya, Niimi, Teruyuki, Ogino, Yukiko, Ogoshi, Maho, Ohira, Tsuyoshi, Ohki-Hamazaki, Hiroko, Ohtaki, Hirokazu, Ohyama, Yoshihiko, Oka, Yoshitaka, Okamoto, Naoki, Osugi, Tomohiro, Park, Min Kyun, Saito, Kazuki, Saito, Yumiko, Sakai, Takafumi, Sakamoto, Hirotaka, Sakamoto, Tatsuya, Satake, Honoo, Sato, Tomomi, Sekiguchi, Toshio, Shimizu, Munetaka, Shinki, Toshimasa, Shinoda, Tetsuro, Sonobe, Haruyuki, Suzuki, Koichi, Suzuki, Nobuo, Tachibana, Tetsuya, Takahashi, Akiyoshi, Takahashi, Toshio, Takei, Yoshio, Takenoya, Fumiko, Takeuchi, Sakae, Tanaka, Yoshiaki, Tanizaki, Yuta, Tsukada, Takehiro, Tsukamoto, Yusuke, Tsutsui, Kazuyoshi, Tsutsui, Naoaki, Ubuka, Takayoshi, Ukena, Kazuyoshi, Wada, Nobuhiro, Watanabe, Jun, Wong, Marty K.S., Xu, Zhifang, Yaginuma, Toshinobu, Yamauchi, Kiyoshi, Yuge, Shinya, and Zitnan, Dusan

Published
2015
Full Text
View/download PDF

173. Differential expression of insulin-like growth factor I and II mRNAs during embryogenesis and early larval development in rabbitfish, Siganus guttatus

Author

Ayson, Felix G., de Jesus, Evelyn Grace T., Moriyama, Shunsuke, Hyodo, Susumu, Funkenstein, Bruria, Gertler, Arieh, Kawauchi, Hiroshi, Ayson, Felix G., de Jesus, Evelyn Grace T., Moriyama, Shunsuke, Hyodo, Susumu, Funkenstein, Bruria, Gertler, Arieh, and Kawauchi, Hiroshi

Abstract

In rodents, the expression of insulin-like growth factor II (IGF-II) is higher than that of insulin-like growth factor I (IGF-I) during fetal life while the reverse is true after birth. We wanted to examine whether this is also true in fish and whether IGF-I and IGF-II are differentially regulated during different stages of embryogenesis and early larval development in rabbitfish. We first cloned the cDNAs of rabbitfish IGF-I and IGF-II from the liver. Rabbitfish IGF-I has an open reading frame of 558 bp that codes for a signal peptide of 44 amino acids (aa), a mature protein of 68 aa, and a single form of E domain of 74 aa. Rabbitfish IGF-II, on the other hand, has an open reading frame of 645 bp that codes for a signal peptide of 47 aa, a mature protein of 70 aa, and an E domain of 98 aa. On the amino acid level, rabbitfish IGF-I shares 68% similarity with IGF-II. We then examined the relative expression of the two IGFs in unfertilized eggs, during different stages of embryogenesis, and in early larval stages of rabbitfish by a semiquantitative reverse transcription-polymerase chain reaction. Primers that amplify the mature peptide region of both IGFs were used and PCR for both peptides was done simultaneously, with identical PCR conditions for both. The identity of the PCR products was confirmed by direct sequencing. Contrary to published reports for seabream and rainbow trout, IGF-I mRNA was not detected in rabbitfish unfertilized eggs; it was first expressed in larvae soon after hatching. IGF-II mRNA, however, was expressed in unfertilized eggs, albeit weakly, and was already strongly expressed during the cleavage stage. mRNAs for both peptides were strongly expressed in the larvae, although IGF-II mRNA expression was higher than IGF-I expression.

Published
2002

174. Milkfish (Chanos chanos) growth hormone cDNA cloning and mRNA expression in embryos and early larval stages.

Author

de Jesus, Evelyn Grace T., Ayson, Felix G., Amemiya, Yutaka, Moriyama, Shunsuke, Hyodo, Susumu, Hirano, Tetsuya, Kawauchi, Hiroshi, de Jesus, Evelyn Grace T., Ayson, Felix G., Amemiya, Yutaka, Moriyama, Shunsuke, Hyodo, Susumu, Hirano, Tetsuya, and Kawauchi, Hiroshi

Abstract

In an attempt to understand growth regulation in milkfish, the milkfish growth hormone (GH) and its cDNA were characterized and the expression of GH mRNA in embryos and larvae was examined by RT-PCR. The milkfish GH was purified from an alkaline extract of the pituitary by reverse-phase high-performance liquid chromatography and detected as an immuno-positive protein with anti-salmon GH serum. The complete sequence of milkfish pre-GH was determined by cDNA cloning and nucleotide sequencing. On the basis of the N-terminal amino acid analysis of the native protein, the pre-GH was found to consist of a signal peptide of 22 amino acids and a mature protein of 188 amino acids. Milkfish GH shows higher amino acid sequence identity with GHs of carps (91–94%) and salmonids (70%) than with GHs of more advanced teleosts (<60%) in good accordance with its taxonomic position in teleosts. It has five half Cys residues, four of which are at positions homologous with those of other known GHs and the extra Cys with those of carp GHs. The molecular weight of milkfish GH was estimated to be 22 kDa, which is comparable to the theoretical value. This suggests that milkfish GH is a simple protein, although it has two potential N-glycosylation sites. Semiquantitative RT-PCR showed that GH mRNA expression was relatively weak in embryos and newly hatched larvae but was already strong in 2-day old and older larvae.

Published
2002

178. Centrally administered adrenomedullin 5 activates oxytocin-secreting neurons in the hypothalamus and elevates plasma oxytocin level in rats

Author

Otsubo, Hiroki, primary, Hyodo, Susumu, additional, Hashimoto, Hirofumi, additional, Kawasaki, Makoto, additional, Suzuki, Hitoshi, additional, Saito, Takeshi, additional, Ohbuchi, Toyoaki, additional, Yokoyama, Toru, additional, Fujihara, Hiroaki, additional, Matsumoto, Tetsuro, additional, Takei, Yoshio, additional, and Ueta, Yoichi, additional

Published
2009
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results