start-ver=1.4
cd-journal=joma
no-vol=33
cd-vols=
no-issue=
article-no=
start-page=26
end-page=30
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2017
dt-pub=201704
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Structure and function of tegmentum vasculosum in avian cochlea
kn-title=鳥類内耳tegmentum vasculosum の構造と機能
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract= In spite of the importance of endocochlear DC potential (EP) and the K+-rich endolymph for the avian cochlea, the structure and function of the tegmentum vasculosum (TV) has not yet been fully elucidated, compared with those of the stria vascularis in the mammalian cochlea. In this study, we examined structural analysis of the epithelial cells, gene expressions of Na+-K+-ATPase (Atp1A1) and Kir4.1 (Kcnj10), and protein localizations of Na+-K+-ATPase and Kir4.1, in the TV. Tight junctional structures were observed between epithelial dark cells and light cells in the TV. Both Atp1a1 and Kcnj10 genes were detected in the TV. In addition, immunopositive signals for both Na+-K+-ATPase and Kir4.1 were recognized in the TV. These results indicate that Na+-K+-ATPase and Kir4.1 play roles in maintaining the EP and high K+ concentration of the endolymph. Further studies are needed to clarify the physiological functions of the TV. This is the first report which demonstrates that gene and protein expression data contribute to the avian inner ear homeostasis.
en-copyright=
kn-copyright=

en-aut-name=IkedaRisa
en-aut-sei=Ikeda
en-aut-mei=Risa
kn-aut-name=池田理佐
kn-aut-sei=池田
kn-aut-mei=理佐
aut-affil-num=1
ORCID=

en-aut-name=OtonoTsuyoshi
en-aut-sei=Otono
en-aut-mei=Tsuyoshi
kn-aut-name=乙野剛史
kn-aut-sei=乙野
kn-aut-mei=剛史
aut-affil-num=2
ORCID=

en-aut-name=IkedaNaoya
en-aut-sei=Ikeda
en-aut-mei=Naoya
kn-aut-name=池田直矢
kn-aut-sei=池田
kn-aut-mei=直矢
aut-affil-num=3
ORCID=

en-aut-name=SaitoNoboru
en-aut-sei=Saito
en-aut-mei=Noboru
kn-aut-name=齋藤昇
kn-aut-sei=齋藤
kn-aut-mei=昇
aut-affil-num=4
ORCID=

en-aut-name=AndoMotonori
en-aut-sei=Ando
en-aut-mei=Motonori
kn-aut-name=安藤元紀
kn-aut-sei=安藤
kn-aut-mei=元紀
aut-affil-num=5
ORCID=

affil-num=1
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科・理科教育講座・細胞生理学研究室

affil-num=2
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科・理科教育講座・細胞生理学研究室

affil-num=3
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科・理科教育講座・細胞生理学研究室

affil-num=4
en-affil=Laboratory of Animal Physiology and Pharmacology, Department of Animal Science, Graduate School of Environmental and Life Science, Okayama University
kn-affil=岡山大学大学院環境生命科学研究科・動物機能開発学講座・動物生理学研究室

affil-num=5
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科・理科教育講座・細胞生理学研究室
END

start-ver=1.4
cd-journal=joma
no-vol=34
cd-vols=
no-issue=
article-no=
start-page=21
end-page=27
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2018
dt-pub=201804
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Cytoskeletal elements in an acoelomorph worm, Praesagittifera naikaiensis
kn-title=無腸動物Praesagittifera naikaiensis における細胞骨格要素
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Acoel flatworms can move in a variety of ways such as muscular and ciliary movements via cytoskeletal elements and their neural regulations. However, those locomotive mechanisms have not yet been fully elucidated. In this study, we examined the distribution of cytoskeletal elements including filamentous actin (F-actin) and tubulin, and the neuroanatomical organization in an acoelomorph worm, Praesagittifera naikaiensis (P. naikaiensis). Video microscopy revealed the elongation/contraction and the bending/rotation processes, and the ciliary gliding movement of P. naikaiensis. Histochemical and morphological analysis demonstrated that F-actin networks of inner longitudinal and outer circular muscle fibers were positioned along the entire surface of the body, and that the average distance between the circular muscle fibers in the contracted organism was decreased in the anterior region compared with that in the elongated organism. Electron microscopy showed dense bodies on the muscle cells of P. naikaiensis, which indicates that those muscle cells have the appearance of vertebrate smooth muscle cells. Immunohistochemical analysis revealed that -tubulin-positive signals on the ciliary microtubules had close contact with the F-actin network, and that neurite bundles labelled with anti dSap47 antibody as a neuronal marker run along the anterior-posterior body axis. These results indicate that the well-organized cytoskeletal elements and their neural control systems are preserved in P. naikaiensis, and that their mechanisms involved in those regulation systems are similar to those vertebrate systems. Further studies are needed to clarify the physiological mechanisms underlying the muscular and ciliary movements in P. naikaiensis.
en-copyright=
kn-copyright=

en-aut-name=IkedaRisa
en-aut-sei=Ikeda
en-aut-mei=Risa
kn-aut-name=池田理佐
kn-aut-sei=池田
kn-aut-mei=理佐
aut-affil-num=1
ORCID=

en-aut-name=FujiwaraChiho
en-aut-sei=Fujiwara
en-aut-mei=Chiho
kn-aut-name=藤原稚穂
kn-aut-sei=藤原
kn-aut-mei=稚穂
aut-affil-num=2
ORCID=

en-aut-name=HamadaMayuko
en-aut-sei=Hamada
en-aut-mei=Mayuko
kn-aut-name=濱田麻友子
kn-aut-sei=濱田
kn-aut-mei=麻友子
aut-affil-num=3
ORCID=

en-aut-name=SakamotoTatsuya
en-aut-sei=Sakamoto
en-aut-mei=Tatsuya
kn-aut-name=坂本竜哉
kn-aut-sei=坂本
kn-aut-mei=竜哉
aut-affil-num=4
ORCID=

en-aut-name=SaitoNoboru
en-aut-sei=Saito
en-aut-mei=Noboru
kn-aut-name=齋藤昇
kn-aut-sei=齋藤
kn-aut-mei=昇
aut-affil-num=5
ORCID=

en-aut-name=AndoMotonori
en-aut-sei=Ando
en-aut-mei=Motonori
kn-aut-name=安藤元紀
kn-aut-sei=安藤
kn-aut-mei=元紀
aut-affil-num=6
ORCID=

affil-num=1
en-affil=Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科

affil-num=2
en-affil=Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科

affil-num=3
en-affil=Ushimado Marine Institute, Faculty of Science, Okayama University
kn-affil=岡山大学・理学部附属臨海実験所

affil-num=4
en-affil=Ushimado Marine Institute, Faculty of Science, Okayama University
kn-affil=岡山大学・理学部附属臨海実験所

affil-num=5
en-affil=Graduate School of Environmental and Life Science, Okayama University
kn-affil=岡山大学大学院環境生命科学研究科

affil-num=6
en-affil=Graduate School of Education, Okayama University
kn-affil=岡山大学大学院教育学研究科
END

start-ver=1.4
cd-journal=joma
no-vol=30
cd-vols=
no-issue=
article-no=
start-page=7
end-page=7
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2014
dt-pub=201404
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Abnormality of water homeostasis of Muscular dystrophic chicken
kn-title=筋ジストロフィーニワトリの水分代謝異常
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=The muscular dystrophy chicken has been studying as model animal of muscular dystrophy for more
than 50 years. Recently, the mutation of WW domain containing E3 ubiquitin protein ligase 1 (WWP1)
gene has been identified as a responsible for muscular dystrophy chicken. We observed that muscular
dystrophy chicken not only showed the degeneration of skeletal muscles but also produced watery feces.
Therefore, we examined the possibility of abnormalities in water metabolism of muscular dystrophy
chicken. We first analyzed plasma osmolality and gene expression of aquaporin 2 (AQP2), AQP3 and
alpha subunit of the amiloride-sensitive epithelial sodium channel (αENaC) in muscular dystrophy
chicken and White Leghorn chicken under normal physiological conditions at five-week old.
Subsequently, we analyzed these same parameters after one-day water-deprivation. The main findings of
our study are that: I) the plasma osmolality was significantly higher in muscular dystrophic chicken than
in White Leghorn; II) kidney αENaC mRNA expression was significantly lower in muscular dystrophic
chicken than in White Leghorn; III) AQP2 and AQP3 mRNA expressions in muscular dystrophic chicken
were similar in White Leghorn. We suggest that the mutation of WWP1 may cause the abnormality of
sodium absorption, and thus muscular dystrophic chicken become hypernatremic.
en-copyright=
kn-copyright=

en-aut-name=SaitoNoboru
en-aut-sei=Saito
en-aut-mei=Noboru
kn-aut-name=齋藤昇
kn-aut-sei=齋藤
kn-aut-mei=昇
aut-affil-num=1
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学大学院環境生命科学研究科
END

start-ver=1.4
cd-journal=joma
no-vol=59
cd-vols=
no-issue=1
article-no=
start-page=1
end-page=12
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2020
dt-pub=2020
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Immunocytochemical Analysis of α-Tubulin Distribution Before and After Rapid Axopodial Contraction in the Centrohelid Raphidocystis contractilis
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=The centrohelid Raphidocystis contractilis is a heliozoan that has many radiating axopodia, each containing a bundle of microtubules. Although the rapid contraction of the axopodia at nearly a video rate (30 frames/s) is induced by mechanical stimuli, the mechanism underlying this phenomenon in R. contractilis has not yet been elucidated. In the present study, we described for the first time an adequate immunocytochemical fixation procedure for R. contractilis and the cellular distribution of α-tubulin before and after rapid axopodial contraction. We developed a flow-through chamber equipped with a micro-syringe pump that allowed the test solution to be injected at a flow rate below the threshold required to induce rapid axopodial contraction. Next, we used this injection method for evaluating the effects of different combinations of two fixatives (paraformaldehyde or glutaraldehyde) and two buffers (phosphate buffer or PHEM) on the morphological structure of the axopodia. A low concentration of glutaraldehyde in PHEM was identified as an adequate fixative for immunocytochemistry. The distribution of α-tubulin before and after rapid axopodial contraction was examined using immunocytochemistry and confocal laser scanning fluorescence microscopy. Positive signals were initially detected along the extended axopodia from the tips to the bases and were distributed in a non-uniform manner within the axopodia. Conversely, after the induction of a rapid axopodial contraction, these positive signals accumulated in the peripheral region of the cell. These results indicated that axopodial microtubules disassemble into fragments and/ or tubulin subunits during rapid axopodial contraction. Therefore, we hypothesize that the mechanism of extremely rapid axopodial contraction accompanied by cytoskeletal microtubule degradation in R. contractilis involves microtubule-severing at multiple sites.
en-copyright=
kn-copyright=

en-aut-name=IkedaRisa
en-aut-sei=Ikeda
en-aut-mei=Risa
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=KurokawaMiki
en-aut-sei=Kurokawa
en-aut-mei=Miki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=MuraiMomoka
en-aut-sei=Murai
en-aut-mei=Momoka
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=SaitoNoboru
en-aut-sei=Saito
en-aut-mei=Noboru
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=AndoMotonori
en-aut-sei=Ando
en-aut-mei=Motonori
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

affil-num=1
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=

affil-num=2
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=

affil-num=3
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=

affil-num=4
en-affil=Laboratory of Animal Physiology and Pharmacology, Department of Animal Science, Graduate School of Environmental and Life Science, Okayama University
kn-affil=

affil-num=5
en-affil=Laboratory of Cell Physiology, Department of Science Education, Graduate School of Education, Okayama University
kn-affil=
en-keyword=heliozoa
kn-keyword=heliozoa
en-keyword=immunocytochemistry
kn-keyword=immunocytochemistry
en-keyword=microtubule
kn-keyword=microtubule
en-keyword=glutaraldehyde
kn-keyword=glutaraldehyde
en-keyword=confocal microscopy
kn-keyword=confocal microscopy
END

start-ver=1.4
cd-journal=joma
no-vol=104
cd-vols=
no-issue=
article-no=
start-page=55
end-page=59
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2015
dt-pub=20150201
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=Effect of fasting and re-feeding on aquaporin gene expression in liver and kidney of the chicken
kn-title=ニワトリにおける肝臓と腎臓のアクアポリン（AQP）遺伝子発現に対する絶食と再給餌の影響
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=　Aquaporin (AQP) which is a water channel, is also including the group (aquaglyceroporin) letting glycerol or urea go through as well as a water molecule. In mammals, AQP7 and AQP9 which are aquaglyceroporin have a role in the transportation of glycerol related to the gluconeogenesis in the liver. It is reported that AQP9 increases uptake of glycerol in the liver, when blood glucose level decreases. This study investigated the effect of AQP9 and AQP7
mRNA levels in liver and kidney in relation to the fasting and the re-feeding in the chicks. The purpose of this study was to determine whether the functions of AQP9 and AQP7 in the chicks are similar to mammals. One-day old chicks were kept with free access to water and food until 7-days
old. At 7-days old, chicks were divided into three groups of 6 chicks : a control groups with free access to food and water and a fasting group with free access to water but not to water for 24 hours, a re-feeding group with free access to
food and water for 6 hours after fasting treatment. At the end of the experiments all the chicks were sacrificed and blood and tissues (liver and kidney) were taken for measurement of blood glucose levels and mRNA levels. Total RNA extracted and reverse transcription was performed. AQP7 and AQP9 and the phosphoenolpyruvate carboxykinase (PEPCK) mRNA levels were measured by using real-time PCR. In the fasting group, body weight significantly decreased as compared with control group, but
blood glucose levels did not decrease. In the re-feeding groups, blood glucose levels significantly increased as compared with control group and fasting group. In the liver, the fasting and the re-feeding treatment did not affect AQP7 and AQP9 mRNA levels. In the kidney, the fasting did not affect AQP7 and AQP9 mRNA levels, but the re-feeding treatment significantly increased AQP7 and AQP9 mRNA levels. In the liver, PEKCK mRNA levels
significantly decreased in fasting group and further decreased in the re-feeding group. The re-feeding treatment significantly increased PEPCK mRNA levels in the kidney. From these results, kidney may play a roll in the increase of
blood glucose levels at the re-feeding. But, a roll in gluconeogenesis of liver is not clear in the chicks. Therefore, further study is necessary to understand the gluconeogenesis in the chicks.
en-copyright=
kn-copyright=

en-aut-name=SaitoNoboru
en-aut-sei=Saito
en-aut-mei=Noboru
kn-aut-name=齋藤昇
kn-aut-sei=齋藤
kn-aut-mei=昇
aut-affil-num=1
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学農学部
en-keyword=chicken
kn-keyword=chicken
en-keyword=aquaporin
kn-keyword=aquaporin
en-keyword=plasma glucose
kn-keyword=plasma glucose
en-keyword=fasting
kn-keyword=fasting
en-keyword=liver
kn-keyword=liver
END