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• W2095683724 abstract "The erythrocyte's spectrin–actin membrane skeleton is directly shown to be capable of sustaining large, anisotropic strains. Photobleaching of an ∼1-μm stripe in rhodamine phalloidin-labeled actin appears stable up to at least 37°C, and is used to demonstrate large in-surface stretching during elastic deformation of the skeleton. Principal extension or stretch ratios of at least ∼200% and contractions down to ∼40%, both referenced to an essentially undistorted cell, are visually demonstrated in micropipette-imposed deformation. Such anisotropic straining is seen to be consistent at a qualitative level with now classic analyses (Evans. 1973. Biophys. J. 13:941–954) and is generally nonhomogeneous though axisymmetric down to the submicron scale. Local, direct measurements of stretching prove quantitatively consistent (within ∼10%) with integrated estimates that are based simply on a measured relative density distribution of actin. The measurements are also in close agreement with direct computation of mean spectrin chain extension in full statistical mechanical simulations of a coarse-grained network held in a micropipette. Finally, as a cell thermally fragments near ∼48°C, the patterned photobleaching demonstrates a destructuring of the surface network in a process that is more readily attributable to transitions in spectrin than in F-actin." @default.
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• W2095683724 date "1999-08-01" @default.
• W2095683724 modified "2023-10-13" @default.
• W2095683724 title "Direct Measures of Large, Anisotropic Strains in Deformation of the Erythrocyte Cytoskeleton" @default.
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• W2095683724 doi "https://doi.org/10.1016/s0006-3495(99)76937-7" @default.
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