JCB logo
Quantitative Colocalization Analysis Software
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 459K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tuvia, S.
Right arrow Articles by Korenstein, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tuvia, S.
Right arrow Articles by Korenstein, R.
Right arrowPubmed/NCBI databases
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*PHALLOIDIN
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1998//1551 $5.00
The Journal of Cell Biology, Volume 141, Number 7, , 1998 1551-1561

Articles

Mechanical Fluctuations of the Membrane–Skeleton Are Dependent on F-Actin ATPase in Human Erythrocytes



Shmuel Tuvia, Shlomo Levin, Arkady Bitler, and Rafi Korenstein

Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel-Aviv University, 69978 Tel-Aviv, Israel

Cell membrane fluctuations (CMF) of human erythrocytes, measured by point dark field microscopy, were shown to depend, to a large extent, on intracellular MgATP (Levin, S.V., and R. Korenstein. 1991. Biophys. J. 60:733–737). The present study extends that investigation and associates CMF with F-actin's ATPase activity. MgATP was found to reconstitute CMF in red blood cell (RBC) ghosts and RBC skeletons to their levels in intact RBCs, with an apparent Kd of 0.29 mM. However, neither non-hydrolyzable ATP analogues (AMP-PNP, ATP{gamma}S) nor hydrolyzable ones (ITP, GTP), were able to elevate CMF levels. The inhibition of ATPase activity associated with the RBC's skeleton, carried out either by the omission of the MgATP substrate or by the use of several inhibitors (vanadate, phalloidin, and DNase I), resulted in a strong decrease of CMF. We suggest that the actin's ATPase, located at the pointed end of the short actin filament, is responsible for the MgATP stimulation of CMF in RBCs.

Abbreviations used in this paper: CMF, cell membrane fluctuations; RBC, red blood cell.

We would like to acknowledge the help of A. Krol, Y. Zipser, A. Barbul, L. Mittelman, and A. Pinchasov.

This research was supported by grants from the Office of Naval Research (3N00014-94-1-5 to S. Levin and R. Korenstein) and the US-Israel Binational Science Foundation (No. 91-00209 to R. Korenstein and S. Levin). This research is part of a doctoral thesis by S. Tuvia.

Address all correspondence to Dr. R. Korenstein, Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel-Aviv University, 69978 Tel-Aviv, Israel. Tel.: 972-3-6406042. Fax: 972-3-6409113. E-mail: korens{at}post.tau.ac.il


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents