JaLCDOI 10.18926/AMO/31681
FullText URL fulltext.pdf
Author Iguchi, Hiroki| Watanabe, Masami| Kamitani, Akihiro| Nagai, Atsushi| Hosoya, Osamu| Tsutsui, Kimiko| Kumon, Hiromi|
Abstract <p>Dynamin is a protein essential to endocytosis. Dynamin 2, a dynamin isoform, is expressed most intensely in testicular tissue; however, precise localization has never been studied. Therefore, we investigated the expression of dynamin 2 in rat testicular tissue using immunohistochemical methods, and discuss here the physiological function of this protein. Testicular tissues were obtained from Wistar rats at 10, 21 and 63 days of age. Immunohistochemistrical examination and Western blot analysis were conducted using dynamin 2 specific antibody. Western blot analysis showed that expression in 21- and 63-day-old rats was more intense than that in 10-day-old rats. Dynamin 2 expression was observed using immunohistochemical method in the seminiferous tubules of all rats. In the 63-day-old rats, the expression was intense, especially in spermatids in the earlier maturation stages and in spermatocytes, and was observed in Sertoli cells. However, in spermatids, the expression gradually declined as spermatids matured to spermatozoa. In the 21-day-old rats, the expression was evident in spermatocytes and Sertoli cells, but that in the 10-day-old rats was weak. Intense expression of dynamin 2 during spermatogenesis suggests that this protein plays an important role in this process.</p>
Keywords dynamin 2 endocytosis spermatogenesis
Amo Type Article
Published Date 2002-08
Publication Title Acta Medica Okayama
Volume volume56
Issue issue4
Publisher Okayama University Medical School
Start Page 205
End Page 209
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
File Version publisher
Refereed True
PubMed ID 12199526
Web of Sience KeyUT 000177382600006
JaLCDOI 10.18926/AMO/31512
FullText URL fulltext.pdf
Author Tsutsui, Ken| Tsutsui, Kimiko| Aoyama, Koji| Oda, Takuzo|
Abstract <p>The extent of homology between two protein fractions was compared by simple electrophoretic analysis. Nuclear proteins of several rodent cells of different origins were fractionated into acid-soluble and acid-insoluble fractions. The two protein fractions were subjected to polyacrylamide gel electrophoresis in separate gel systems, and protein bands with identical mobilities were sought either in all possible combinational pairs of cell types or in all cell types. The paired and overall homology indices calculated from these data and chi-square testing of the results indicated that acid-soluble nuclear nonhistone proteins are more homologous than acid-insoluble nuclear proteins. Several factors which might have affected the results were discussed.</p>
Keywords nuclear proteins protein homology polyacrylamide gel electrophoresis
Amo Type Article
Published Date 1985-04
Publication Title Acta Medica Okayama
Volume volume39
Issue issue2
Publisher Okayama University Medical School
Start Page 99
End Page 104
ISSN 0386-300X
NCID AA00508441
Content Type Journal Article
language 英語
File Version publisher
Refereed True
PubMed ID 4003115
Web of Sience KeyUT A1985AGK4600003
Author Tsutsui, Kimiko|
Published Date 1978-08
Publication Title 岡山医学会雑誌
Volume volume90
Issue issue7-8
Content Type Journal Article
Author Tsutsui, Kimiko M .|
Published Date 2009-12-01
Publication Title 岡山医学会雑誌
Volume volume121
Issue issue3
Content Type Others
Author Sano, Kuniaki| Miyaji, Mary| Tsutsui, M. Kimiko| Tsutsui, Ken|
Published Date 2009-12-01
Publication Title 岡山医学会雑誌
Volume volume121
Issue issue3
Content Type Journal Article
Author 筒井 公子|
Published Date 2002-05-30
Publication Title 岡山医学会雑誌
Volume volume114
Issue issue1
Content Type Others
Author 筒井 公子|
Published Date 2004-09-30
Publication Title 岡山医学会雑誌
Volume volume116
Issue issue2
Content Type Journal Article
Author 筒井 公子|
Published Date 1978-03-31
Publication Title
Content Type Thesis or Dissertation