期刊
BIOPHYSICAL JOURNAL
卷 101, 期 10, 页码 2341-2350出版社
CELL PRESS
DOI: 10.1016/j.bpj.2011.09.050
关键词
-
类别
资金
- National Institutes of Health [S10 RR17291, F31NS056467]
- New York University
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0741914] Funding Source: National Science Foundation
Erythrocytes possess a spectrin-based cytoskeleton that provides elasticity and mechanical stability necessary to survive the shear forces within the microvasculature. The architecture of this membrane skeleton and the nature of its intermolecular contacts determine the mechanical properties of the skeleton and confer the characteristic biconcave shape of red cells. We have used cryo-electron tomography to evaluate the three-dimensional topology in intact, unexpanded membrane skeletons from mouse erythrocytes frozen in physiological buffer. The tomograms reveal a complex network of spectrin filaments converging at actin-based nodes and a gradual decrease in both the density and the thickness of the network from the center to the edge of the cell. The average contour length of spectrin filaments connecting junctional complexes is 46 +/- 15 nm, indicating that the spectrin heterotetramer in the native membrane skeleton is a fraction of its fully extended length (similar to 190 nm). Higher-order oligomers of spectrin were prevalent, with hexamers and octamers seen between virtually every junctional complex in the network. Based on comparisons with expanded skeletons, we propose that the oligomeric state of spectrin is in a dynamic equilibrium that facilitates remodeling of the network as the cell changes shape in response to shear stress.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据