The origins and regulation of tissue tension: Identification of collagen tension-fixation process in vitro

Marenzana, Massimo; Wilson-Jones, Nick; Mudera, Vivek; Brown, Robert A.

doi:10.1016/j.yexcr.2005.11.005

Cited by 57 publications

(82 citation statements)

References 38 publications

(76 reference statements)

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“…Incorporation of rhPN into the collagen gels reversed both of these effects. Tissue culture plates provide an enormously stiff environment for cell growth with a reported elastic modulus of 2.78 GPa (Callister and Rethwisch, 2000), whereas 2 mg/ml collagen gels have an elastic modulus of approximately 300-400 Pa (Marenzana et al, 2006;Paszek et al, 2005). The elastic modulus of anchored collagen gels has not been reported.…”

Section: Discussionmentioning

confidence: 99%

Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair

Elliott

Wang

Guo

et al. 2012

Journal of Cell Science

128

154

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SummaryThe matricellular protein periostin is expressed in the skin. Although periostin has been hypothesized to contribute to dermal homeostasis and repair, this has not been directly tested. To assess the contribution of periostin to dermal healing, 6 mm full-thickness excisional wounds were created in the skin of periostin-knockout and wild-type, sex-matched control mice. In wild-type mice, periostin was potently induced 5-7 days after wounding. In the absence of periostin, day 7 wounds showed a significant reduction in myofibroblasts, as visualized by expression of a-smooth muscle actin (a-SMA) within the granulation tissue. Delivery of recombinant human periostin by electrospun collagen scaffolds restored a-SMA expression. Isolated wild-type and knockout dermal fibroblasts did not differ in in vitro assays of adhesion or migration; however, in 3D culture, periostin-knockout fibroblasts showed a significantly reduced ability to contract a collagen matrix, and adopted a dendritic phenotype. Recombinant periostin restored the defects in cell morphology and matrix contraction displayed by periostin-deficient fibroblasts in a manner that was sensitive to a neutralizing anti-b1-integrin and to the FAK and Src inhibitor PP2. We propose that periostin promotes wound contraction by facilitating myofibroblast differentiation and contraction.

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Section: Discussionmentioning

confidence: 99%

Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair

Elliott

Wang

Guo

et al. 2012

Journal of Cell Science

128

154

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“…3 It is also possible that these same cells produce a gradual contracture,* a permanent matrix shape change by the ratchet mechanism proposed and identified previously. 16,17 Observations so far, then, would suggest that the small, slow shape changes seen for PC collagen constructs are equivalent to the contractures seen in clinical scars.…”

Section: Examples Of Cell-matrix Model Systemsmentioning

confidence: 93%

Rapid Fabrication of Living Tissue Models by Collagen Plastic Compression: Understanding Three-Dimensional Cell Matrix Repair In Vitro

Cheema

Brown

2013

Advances in Wound Care

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Objective: To produce biomimetic collagen scaffolds for tissue modeling and as tissue-engineered implants. Approach: Control of collagen fibril material parameters in collagen hydrogel scaffolds by using plastic compression (PC), resulting in direct control of cell proliferation, cell migration, and cell-cell interaction. Results: We were able to control the density of collagen in such scaffolds from between 0.2% and 30%, and controllably layer the fibrils in the Z-plane. Cell migration was observed in gels where a gradient of collagen density was present. In these gels, cells preferentially migrated toward the collagen-dense areas. Cell proliferation rates were measurably higher in dense collagen gels. Innovation: The use of PC to control material properties of collagen hydrogels results in collagen scaffolds that are biomimetic. These collagen gels reproduce the relevant matrix-mechanical environment in which behavior is more representative of that found in vivo. Conclusion: The material properties of native collagen type I gels can be engineered to match those found in tissues in vivo to elicit more biomimetic cell behavior.

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“…Interestingly, these changes were linked to altered TGF-b signaling in Lmna À/À cells and wnt/b-catenin signaling in HGPS cells (Van Berlo et al 2005;Hernandez et al 2010). While it is well known that Rho-activated cell contractility and tension modulate the expression of ECM components in a TGF-b-dependent manner (Chapados et al 2006;Marenzana et al 2006;Meyer-ter-Vehn et al 2006), the role of A-type lamins in this ''mechanobiological gene circuit'' is still unclear (Buxboim et al 2014).…”

Section: Molecular Mechanisms Of Lamins In Mechanosensing/signaling 'mentioning

confidence: 99%

Lamins at the crossroads of mechanosignaling

2015

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The intermediate filament proteins, A-and B-type lamins, form the nuclear lamina scaffold adjacent to the inner nuclear membrane. B-type lamins confer elasticity, while A-type lamins lend viscosity and stiffness to nuclei. Lamins also contribute to chromatin regulation and various signaling pathways affecting gene expression. The mechanical roles of lamins and their functions in gene regulation are often viewed as independent activities, but recent findings suggest a highly cross-linked and interdependent regulation of these different functions, particularly in mechanosignaling. In this newly emerging concept, lamins act as a ''mechanostat'' that senses forces from outside and responds to tension by reinforcing the cytoskeleton and the extracellular matrix. A-type lamins, emerin, and the linker of the nucleoskeleton and cytoskeleton (LINC) complex directly transmit forces from the extracellular matrix into the nucleus. These mechanical forces lead to changes in the molecular structure, modification, and assembly state of A-type lamins. This in turn activates a tension-induced ''inside-out signaling'' through which the nucleus feeds back to the cytoskeleton and the extracellular matrix to balance outside and inside forces. These functions regulate differentiation and may be impaired in lamin-linked diseases, leading to cellular phenotypes, particularly in mechanical load-bearing tissues.

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The origins and regulation of tissue tension: Identification of collagen tension-fixation process in vitro

Cited by 57 publications

References 38 publications

Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair

Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair

Rapid Fabrication of Living Tissue Models by Collagen Plastic Compression: Understanding Three-Dimensional Cell Matrix Repair In Vitro

Lamins at the crossroads of mechanosignaling

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