Skip Navigation



Journal of Biochemistry Advance Access published online on March 26, 2007

Journal of Biochemistry, doi:10.1093/jb/mvm080
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
141/5/747    most recent
mvm080v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yamaguchi, T.
Right arrow Articles by Terada, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamaguchi, T.
Right arrow Articles by Terada, S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Japanese Biochemical Society

Membrane Perturbations of Erythrocyte Ghosts by Spectrin Release+

Takeo Yamaguchi1, Ozaki Shinnosuke, Taiji Shimomura and Shigeyuki Terada

Department of Chemistry, Faculty of Science, Fukuoka University, Jonan-ku, Fukuoka, 814-0180

1 To whom correspondence should be addressed. Takeo Yamaguchi, Nanakuma, Jonan-ku, Fukuoka, Japan, 814-0180, TEL: 092-871-6631(ex 6242), FAX: 092-865-6030 E-mail: takeo{at}fukuoka-u.ac.jp

Received January 25, 2007; Accepted March 8, 2007


   Abstract

The cytoskeleton plays an important role in the stability and function of the membrane. Spectrin release from erythrocyte ghosts makes the membrane more fragile. However, the detail of membrane fragility has remained unclear. In the present study, the effects of incubation temperatures and polyamines on the membrane structure of ghosts under hypotonic conditions have been examined. Upon exposure of ghosts to a hypotonic buffer at 0 ~ 37 °C, reduction of ghost volume, spectrin release, and decrease of band 3-cytoskeleton interactions were clearly observed above 30 °C. However, such changes were completely inhibited by spermine and spermidine. Interestingly, conformational changes of spectrin induced at 37 or 49 °C were not suppressed by both polyamines. Flow cytometry of fluorescein isothiocyanate-labeled ghosts exposed to 37 °C demonstrated the two peaks corresponding to ghosts with normal spectrin content and decreased one. Taken together, these results indicate that the degree of spectrin release from the membrane under hypotonic conditions is not same in all ghosts, and that polyamines inhibit the spectrin release followed by changes in the membrane structure, but not conformational changes of spectrin.

Key Words: band 3, erythrocyte, flow cytometry, polyamine, spectrin


+ This work was partly supported by a grant from the Central Research Institute of Fukuoka University.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.