Biomechanical properties of intermediate filaments: from tissues to single filaments and back

Kreplak, Laurent; Fudge, Douglas S.

doi:10.1002/bies.20514

Cited by 108 publications

(96 citation statements)

References 92 publications

(136 reference statements)

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“…Recent measurements show that the structure of IFs leads to single filament mechanics that are different from both actin and microtubules (Guzman et al, 2006;Kiss et al, 2006;Kreplak and Fudge, 2007;Kreplak et al, 2005). Imaging measurements suggest that the persistence length for vimentin filaments is on the order of 1 μm, one order of magnitude smaller than for F-actin and three orders of magnitude smaller than for microtubules (Mucke et al, 2004).…”

Section: B Mechanics Of Ifsmentioning

confidence: 99%

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Chapter 19 Mechanical Response of Cytoskeletal Networks

Gardel

Kasza

Brangwynne

et al. 2008

Methods in Cell Biology

202

201

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The cellular cytoskeleton is a dynamic network of filamentous proteins, consisting of filamentous actin (F-actin), microtubules, and intermediate filaments. However, these networks are not simple linear, elastic solids; they can exhibit highly nonlinear elasticity and athermal dynamics driven by ATP-dependent processes. To build quantitative mechanical models describing complex cellular behaviors, it is necessary to understand the underlying physical principles that regulate force transmission and dynamics within these networks. In this chapter, we review our current understanding of the physics of networks of cytoskeletal proteins formed in vitro. We introduce rheology, the technique used to measure mechanical response. We discuss our current understanding of the mechanical response of F-actin networks, and how the biophysical properties of F-actin and actin cross-linking proteins can dramatically impact the network mechanical response. We discuss how incorporating dynamic and rigid microtubules into F-actin networks can affect the contours of growing microtubules and composite network rigidity. Finally, we discuss the mechanical behaviors of intermediate filaments.

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Section: B Mechanics Of Ifsmentioning

confidence: 99%

“…The particular architecture of IFs is important for understanding their unique mechanical properties Kreplak and Fudge, 2007). The assembly of IFs is quite complex and distinct from the assembly process of F-actin or microtubules (Herrmann and Aebi, 1998;Herrmann et al, 1999).…”

Section: A Introductionmentioning

confidence: 99%

Chapter 19 Mechanical Response of Cytoskeletal Networks

Gardel

Kasza

Brangwynne

et al. 2008

Methods in Cell Biology

202

201

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“…Furthermore, -keratin materials have different forms in nature, varying from the filamentous type of hair and wool to the laminations of cattle horn. The specific form of -keratin is thought to be mainly determined by the network of hydrogen-bonds (Kitchener and Vincent, 1987), covalent disulphide bonds (Hearle, 2000) and intermolecular cross-links such as ionic interactions and van der Waals bonds (Fraser et al, 1986;Parry, 1996;Kreplak and Fudge, 2007). Previous experimental studies found a progressive increase of water mobility and a decrease in structural rigidity of -keratin with hydration (Speakman, 1928;King, 1945).…”

Section: Hydration Dependence Of Mechanical Propertiesmentioning

confidence: 99%

Experimental study on the mechanical properties of the horn sheaths from cattle

Zhao

Feng

et al. 2010

Journal of Experimental Biology

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SUMMARYBovine horn is composed of a sheath of keratin overlying a bony core. Previous studies of the bovine horn sheath have focused mainly on its morphology and compositions. In the present paper, we performed a series of uniaxial tension, three-point bending, and fracture tests to investigate the structural and mechanical properties of the horn sheaths from subadult cattle, Bos taurus. The effects of hydration on the mechanical properties were examined and their variations along the longitudinal direction of the horn sheath were addressed. Scanning electron microscopy of the fracture surfaces showed that the horn sheath has a layered structure and, more interestingly, the laminae have a rippled appearance. The Young's modulus and tensile strength increase from 850MPa and 40MPa at 19% water content to 2.3GPa and 154MPa at 0% water content, respectively. The Poisson's ratio of the horn sheath was about 0.38. The critical stress intensity factor was about 4.76MPam 1/2 at an intermediate hydration (8% water content), greater than that at 0% water content (3.86MPam 1/2 ) and 19% water content (2.56MPam 1/2 ). The bending properties of the samples varied along the length of the horn. The mean flexural moduli of the specimens in the distal, middle and proximal parts were about 6.26GPa, 5.93GPa and 4.98GPa, respectively; whereas the mean yield strength in the distal segment was about 152.4MPa, distinctly higher than that in the middle (135.7MPa) and proximal parts (116.4MPa). This study deepens our understanding of the relationships among optimal structure, property and function of cattle horn sheaths.

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“…In contrast, intermediate filaments exhibit strain hardening at high tensile strains without rupture. 7,9,12 Every cell type is composed of different types and amounts of specific cytoskeleton fibers. Simple epithelia, such as the pancreatic cancer cells we investigated here, have a well-developed keratin intermediate filament network in addition to actin and microtubules.…”

Section: Introductionmentioning

confidence: 99%

Elastic moduli of living epithelial pancreatic cancer cells and their skeletonized keratin intermediate filament network

Walter¹,

Busch²,

Seufferlein

et al. 2011

Biointerphases

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In simple epithelia, such as living epithelial pancreatic cancer cells (Panc-1), unusual amounts of keratin filaments can be found, which makes these cells an ideal model system to study the role of keratin for cell mechanical properties. In this work, the elastic moduli of Panc-1 cells and their extracted in-situ subcellular keratin intermediate filament network are determined and compared with each other. For this, the living adherent cells and their extracted keratin network were probed with local quasistatic indentation testing during large deformations using the Atomic Force Microscope (AFM). We determined the elastic modulus of the skeletonized but structurally intact keratin network to be in the order of 10 Pa, while the living cell elastic modulus ranged from 100 to 500 Pa. By removing microfilaments, microtubules, membranes and soluble cytoplasmic components during keratin network extraction, we excluded effects caused by crosslinking with other filamentous fibers and from the viscosity of the cytoplasm. Thus, the determined elastic modulus equals the actual elastic modulus inherent to such a keratin filamentous network. In our assessment of the effective mechanical contribution of the architecturally intact, skeletonized keratin network to living cell mechanics, we come to the conclusion that it plays only a very limited role. Evidently, the quantitative dominance of keratin in these cells does not reflect a strong influence on determining the cell's elastic modulus. Instead, keratin like other filamentous structures in the cell's scaffolding, e.g., F-actin and microtubuli, is one part of a greater whole

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Biomechanical properties of intermediate filaments: from tissues to single filaments and back

Cited by 108 publications

References 92 publications

Chapter 19 Mechanical Response of Cytoskeletal Networks

Chapter 19 Mechanical Response of Cytoskeletal Networks

Experimental study on the mechanical properties of the horn sheaths from cattle

Elastic moduli of living epithelial pancreatic cancer cells and their skeletonized keratin intermediate filament network

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