Journal of Biochemistry Advance Access published online on March 26, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm080
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© 2007 The Japanese Biochemical Society
Membrane Perturbations of Erythrocyte Ghosts by Spectrin Release+
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 |
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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.