5 results on '"Intracellular signalling"'
Search Results
2. Mechanical oscillations in biological tissues as a result of delayed rest-length changes
- Author
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Universitat Politècnica de Catalunya. Departament de Matemàtiques, Universitat Politècnica de Catalunya. LACÀN - Mètodes Numèrics en Ciències Aplicades i Enginyeria, Muñoz Romero, José, Dingle, Monica, Wenzel, Manuel, Universitat Politècnica de Catalunya. Departament de Matemàtiques, Universitat Politècnica de Catalunya. LACÀN - Mètodes Numèrics en Ciències Aplicades i Enginyeria, Muñoz Romero, José, Dingle, Monica, and Wenzel, Manuel
- Abstract
Oscillatory behavior in tissue biology is ubiquitous and may be observed in the form of either chemical or mechanical signals. We present here and solve a mechanical cell model that exhibits oscillations emerging from delayed viscoelastic rheological laws. These include a time delay between the mechanical response and the rest-length changes, which evolve proportionally to the delayed cell deformation and use a remodeling rate parameter. We show that different regimes (no oscillatory response, sustained oscillations, and unstable oscillations) are obtained for different values of the delay or the remodeling rate. The results are analytically demonstrated in a one-dimensional problem with one and two cells that are represented by simple line elements. Oscillations of the cell deformations are obtained whenever different delays coexist, or when the delay is size-dependent. We also extend our results to a multicellular two-dimensional vertex model that includes the same rheological law, and which inherits the presence of critical values of the delay or remodeling rate. We numerically show that indeed the size-dependent rest-length changes induce oscillations in the cell shapes and areas., Peer Reviewed, Preprint
- Published
- 2018
3. Role of material-driven fibronectin fibrillogenesis in cell differentiation
- Author
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Universitat Politècnica de València. Departamento de Ingeniería Electrónica - Departament d'Enginyeria Electrònica, Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada, Ministerio de Educación, National Science Foundation, EEUU, Salmerón Sánchez, Manuel, Rico Tortosa, Patricia María, Moratal Pérez, David, Lee, Ted T., Schwarzbauer, Jean E., Garcia, Andres J., Universitat Politècnica de València. Departamento de Ingeniería Electrónica - Departament d'Enginyeria Electrònica, Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada, Ministerio de Educación, National Science Foundation, EEUU, Salmerón Sánchez, Manuel, Rico Tortosa, Patricia María, Moratal Pérez, David, Lee, Ted T., Schwarzbauer, Jean E., and Garcia, Andres J.
- Abstract
Fibronectin (FN) is a ubiquitous extracellular matrix protein (ECM) protein that is organized into fibrillar networks by cells through an integrin-mediated process that involves contractile forces. This assembly allows for the unfolding of the FN molecule, exposing cryptic domains that are not available in the native globular FN structure and activating intracellular signalling complexes. However, organization of FN into a physiological fibrillar network upon adsorption on a material surface has not been observed. Here we demonstrate cell-free, material-induced FN fibrillogenesis into a biological matrix with enhanced cellular activities. We found that simple FN adsorption onto poly(ethyl acrylate) surfaces, but not control polymers, triggered FN organization into a fibrillar network via interactions in the amino-terminal 70 kDa fragment, which is involved in the formation of cell-mediated FN fibrils. Moreover, the material-driven FN fibrils exhibited enhanced biological activities in terms of myogenic differentiation compared to individual FN molecules and even type I collagen. Our results demonstrate that molecular assembly of FN can take place at the material interface, giving rise to a physiological protein network similar to fibrillar matrices assembled by cells. This research identifies material surfaces that trigger the organization of extracellular matrix proteins into biological active fibrils and establishes a new paradigm to engineer ECM-mimetic biomaterials.
- Published
- 2011
4. Role of material-driven fibronectin fibrillogenesis in cell differentiation
- Author
-
Universitat Politècnica de València. Departamento de Ingeniería Electrónica - Departament d'Enginyeria Electrònica, Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada, Ministerio de Educación, National Science Foundation, EEUU, Salmerón Sánchez, Manuel, Rico Tortosa, Patricia María, Moratal Pérez, David, Lee, Ted T., Schwarzbauer, Jean E., Garcia, Andres J., Universitat Politècnica de València. Departamento de Ingeniería Electrónica - Departament d'Enginyeria Electrònica, Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada, Ministerio de Educación, National Science Foundation, EEUU, Salmerón Sánchez, Manuel, Rico Tortosa, Patricia María, Moratal Pérez, David, Lee, Ted T., Schwarzbauer, Jean E., and Garcia, Andres J.
- Abstract
Fibronectin (FN) is a ubiquitous extracellular matrix protein (ECM) protein that is organized into fibrillar networks by cells through an integrin-mediated process that involves contractile forces. This assembly allows for the unfolding of the FN molecule, exposing cryptic domains that are not available in the native globular FN structure and activating intracellular signalling complexes. However, organization of FN into a physiological fibrillar network upon adsorption on a material surface has not been observed. Here we demonstrate cell-free, material-induced FN fibrillogenesis into a biological matrix with enhanced cellular activities. We found that simple FN adsorption onto poly(ethyl acrylate) surfaces, but not control polymers, triggered FN organization into a fibrillar network via interactions in the amino-terminal 70 kDa fragment, which is involved in the formation of cell-mediated FN fibrils. Moreover, the material-driven FN fibrils exhibited enhanced biological activities in terms of myogenic differentiation compared to individual FN molecules and even type I collagen. Our results demonstrate that molecular assembly of FN can take place at the material interface, giving rise to a physiological protein network similar to fibrillar matrices assembled by cells. This research identifies material surfaces that trigger the organization of extracellular matrix proteins into biological active fibrils and establishes a new paradigm to engineer ECM-mimetic biomaterials.
- Published
- 2011
5. Modulatory effect of insulin on release of calcium from human fibroblasts by angiotensin II
- Author
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Ceolotto, G, Pessina, A, Iori, E, Monari, A, Trevisan, R, Winkleswski, P, Semplicini, A, Ceolotto G, Pessina AC, Iori E, Monari A, Trevisan R, Winkleswski P, Semplicini A, Ceolotto, G, Pessina, A, Iori, E, Monari, A, Trevisan, R, Winkleswski, P, Semplicini, A, Ceolotto G, Pessina AC, Iori E, Monari A, Trevisan R, Winkleswski P, and Semplicini A
- Abstract
Background. Angiotensin II stimulates synthesis and deposition of collagen and might contribute to the vascular and cardiac dysfunction associated with arterial hypertension. Insulin attenuates angiotensin II-induced responses of intracellular Ca2+ concentration ([Ca2+]) in many cell types but this effect is less in insulin-resistant states. The mechanisms of the interaction between insulin and angiotensin II are still not known. Objective. To characterize the effects of angiotensin II on intracellular [Ca2+] and the effects of insulin on the angiotensin II-induced response of intracellular [Ca2+] in human skin fibroblasts. Methods. Spectrofluorophotometric measurements of intracellular [Ca2+] in monolayers of cultured human skin fibroblasts from 15 normotensive patients were performed using Fura-2 at 510 nm emission with excitation wavelengths of 340 and 380 nm. Results. Basal intracellular [Ca2+] in quiescent (24 h serum-deprived) human fibroblasts was 75 ± 3 nmol/l (n = 20). Administration of angiotensin II elevated intracellular [Ca2+] dose-dependently with a concentration for half-maximal effect of 20 nmol/l. Administration of 100 nmol/l angiotensin II stimulated a rapid and transient increase in intracellular [Ca2+] (from 75 ± 3 to 130 ± 2 nmol/l, n = 20). Removal of extracellular calcium did not change peak intracellular [Ca2+], but it did reduce the time to recovery of [Ca2+] (from 64 ± 4 to 48 ± 2 s, n = 10, P < 0.01), suggesting that an angiotensin II-induced transmembrane calcium influx had occurred. This hypothesis was confirmed by quenching studies with manganese. The angiotensin II-induced changes in intracellular [Ca2+] were completely blocked by administration of 100 nmol/l of the angiotensin II type 1 receptor inhibitor losartan but not by administration of 100 nmol/l of the angiotensin II type 2 receptor blocker CGP42112A. Acute (20 min) exposure to 100 nmol/l insulin did not alter basal intracellular [Ca2+] in quiescent fibroblasts, but signifi
- Published
- 1998
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