JaLCDOI 10.18926/AMO/48557
FullText URL 66_3_183.pdf
Author Tanabe, Kenji| Takei, Kohji|
Abstract Charcot-Marie-Tooth disease (CMT) is an inherited neuronal disorder, and is induced by mutations of various genes associated with intracellular membrane traffic and cytoskeleton. A large GTPase, dynamin, which is known as a fission protein for endocytic vesicles, was identified as a gene responsible for dominant-intermediate CMT type 2B (DI-CMT2B). Of these mutants, the PH domain, which is required for interaction with phosphoinositides, was mutated in several families. Interestingly, the expression of a deletion mutant, 551Δ3, did not impair endocytosis, but induced abnormal accumulation of microtubules. Recent evidence has shown that dynamin 2 regulates the dynamic instability of microtubules, and 551Δ3 lacks this function. We propose a model for the regulation of the dynamic instability of microtubules by dynamin 2 and discuss the relationship between dynamin 2 and CMT.
Keywords neuropathy Charcot-Marie-Tooth disease membrane traffic dynamin microtubules
Amo Type Review
Published Date 2012-06
Publication Title Acta Medica Okayama
Volume volume66
Issue issue3
Publisher Okayama University Medical School
Start Page 183
End Page 190
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
Copyright Holders CopyrightⒸ 2012 by Okayama University Medical School
File Version publisher
Refereed True
PubMed ID 22729098
Web of Sience KeyUT 000305669700001
Author Yamada, Hiroshi| Padilla-Parra, Sergi| Park, Sun Joo| Itoh, Toshiki| Chaineau, Mathilde| Monaldi, Ilaria| Cremona, Ottavio| Benfenati, Fabio| Camilli, Pietro De| Coppey-Moisan, Maïté| Tramier, Marc| Galli, Thierry| Takei, Kohji|
Published Date 2011-04-01
Publication Title 岡山医学会雑誌
Volume volume123
Issue issue1
Content Type Journal Article
Author Tanabe, Kenji| Takei, Kohji|
Published Date 2010-08-02
Publication Title 岡山医学会雑誌
Volume volume122
Issue issue2
Content Type Journal Article
JaLCDOI 10.18926/AMO/30954
FullText URL fulltext.pdf
Author Nakanishi, Akira| Abe, Tadashi| Watanabe, Masami| Takei, Kohji| Yamada, Hiroshi|
Abstract <p>Testicular Sertoli cells highly express dynamin 2 and amphiphysin 1. Here we demonstrate that dynamin 2 is implicated in phosphatidylserine (PS)-dependent phagocytosis in Sertoli cells. Immunofluorescence and dual-live imaging revealed that dynamin 2 and amphiphysin 1 accumulate simultaneously at ruffles. These proteins are specifically bound <i>in vitro</i>. Over-expression of dominant negative dynamin 2 (K44A) inhibits liposome-uptake and leads to the mis-localization of amphiphysin 1. Thus, the cooperative function of dynamin 2 and amphiphysin 1 in PS-dependent phagocytosis is strongly suggested.</p>
Keywords dynamin amphiphysin phagocytosis testis
Amo Type Original Article
Published Date 2008-12
Publication Title Acta Medica Okayama
Volume volume62
Issue issue6
Publisher Okayama University Medical School
Start Page 385
End Page 391
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
File Version publisher
Refereed True
Web of Sience KeyUT 000262025000005
Author 成島 道樹| Kobayashi, Naoya| 興津 輝| 田中 斎仁| 李 順愛| 陳 勇| 三木 厚| 田中 公章| 中路 修平| 竹居 孝二| Alejandro, Soto Gutierrez| Jorge, David Rivas-Carrillo| Nalu, Navarro-Alvarez| Hee-Sook, Jun| Karen, A Westerman| 野口 洋文| Jonathan, R T Lakey| Philippe, Leboulch| 田中 紀章| Ji-Won, Yoon|
Published Date 2007-05-01
Publication Title 岡山医学会雑誌
Volume volume119
Issue issue1
Content Type Journal Article
JaLCDOI 10.18926/AMO/32823
FullText URL fulltext.pdf
Author Nakanishi, Akira| Kinuta, Keiko| Abe, Tadashi| Araki, Kenta| Yoshida, Yumi| Liang, Shuang| Li, Shun-Ai| Takei, Kohji| Kinuta, Masahiro|
Abstract <p>Administration of phenylhydrazine to rabbits resulted in the denaturation of hemoglobins in erythrocytes, causing the formation of intracellular precipitates known as Heinz bodies, severe hemolytic anemia, and reticulocytosis. To elucidate the molecular mechanism of the destabilization, we allowed human oxyhemoglobins to react aerobically with phenylhydrazine. After treatment with acetic acid/HCl and H2SO4/methanol, the chloroform extract contained blue-green pigments of major products accompanied by different minor products. Each product was isolated by column chromatography. By fast-atom-bombardment mass spectrometry (FAB-MS) and proton nuclear magnetic resonance (1H-NMR) spectrometry, dimethyl esters of N-phenylprotoporphyrin IX and meso, N-diphenylprotoporphyrin IX were determined. Other major products also were determined to be dimethyl esters of triphenyl-and tetraphenyl-substituted protoporphyrins by FAB-MS. The formation of meso, N-diphenylprotoporphyrin indicated that the addition of a phenyl radical to the meso-carbon atom of the protoporphyrin ring occurred. Triphenyl and tetraphenyl adducts also indicated the formation of phenyl radicals in the aerobic reaction of phenylhydrazine with oxyhemoglobins. From these results, we suggest that the formation of phenyl radicals and the replacement of heme with phenyl-substituted protoporphyrins cause the destabilization of hemoglobins to induce Heinz bodies and hemolytic anemia with phenylhydrazine.</p>
Keywords phenylhydrazine hemoglobin protoporphyrin fast-atom-bombardment mass spectrometry(FAB-MS) proton nuclear magnetic resonance(H-NMR)spectrometry
Amo Type Article
Published Date 2003-10
Publication Title Acta Medica Okayama
Volume volume57
Issue issue5
Publisher Okayama University Medical School
Start Page 249
End Page 256
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
File Version publisher
Refereed True
PubMed ID 14679403
Web of Sience KeyUT 000186186000006