The Experts below are selected from a list of 39342 Experts worldwide ranked by ideXlab platform
Ralph A. Nixon - One of the best experts on this subject based on the ideXlab platform.
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the slow axonal transport of Cytoskeletal Proteins
Current Opinion in Cell Biology, 1998Co-Authors: Ralph A. NixonAbstract:Abstract Once presumed to be relatively uniform, the axonal cytoskeleton can vary markedly in size and composition along its length. New studies emphasize the interactiveness of neurofilaments and identify a family of Cytoskeletal Proteins that may cross-link the various Cytoskeletal polymers of the axon, and anchor this network to the membrane skeleton. These and other findings support a model of the axonal cytoskeleton as a stationary but dynamic structure. Current evidence continues to support the possibility that axonally transported polymers/oligomers and/or monomers may serve as precursors to the cytoskeleton in different situations. Although the motors for slow transport of Cytoskeletal Proteins remain elusive, possible candidates are emerging.
Yoshiaki Komiya - One of the best experts on this subject based on the ideXlab platform.
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organization and slow axonal transport of Cytoskeletal Proteins under normal and regenerating conditions
Molecular Neurobiology, 1992Co-Authors: Tomoko Tashiro, Yoshiaki KomiyaAbstract:The organization of the axonal cytoskeleton was investigated by analyzing the solubility and transport profile of the major Cytoskeletal Proteins in motor axons of the rat sciatic nerve under normal and regenerating conditions. When extracted with the Triton-containing buffer at low temperature, 50% of tubulin and 30% of actin were recovered in the insoluble form resistant to further depolymerizing treatments. Most of this cold-insoluble form was transported in slow component a (SCa), the slower of the two subcomponents of slow axonal transport, whereas the cold-soluble form showed a biphasic distribution between SCa and SCb (slow component b).
Tomoko Tashiro - One of the best experts on this subject based on the ideXlab platform.
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organization and slow axonal transport of Cytoskeletal Proteins under normal and regenerating conditions
Molecular Neurobiology, 1992Co-Authors: Tomoko Tashiro, Yoshiaki KomiyaAbstract:The organization of the axonal cytoskeleton was investigated by analyzing the solubility and transport profile of the major Cytoskeletal Proteins in motor axons of the rat sciatic nerve under normal and regenerating conditions. When extracted with the Triton-containing buffer at low temperature, 50% of tubulin and 30% of actin were recovered in the insoluble form resistant to further depolymerizing treatments. Most of this cold-insoluble form was transported in slow component a (SCa), the slower of the two subcomponents of slow axonal transport, whereas the cold-soluble form showed a biphasic distribution between SCa and SCb (slow component b).
Manouchehr Nakhjavani - One of the best experts on this subject based on the ideXlab platform.
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The Degree of Resistance of Erythrocyte Membrane Cytoskeletal Proteins to Supra-Physiologic Concentrations of Calcium: An In Vitro Study
Journal of Membrane Biology, 2014Co-Authors: Ebrahim Mostafavi, Arash Aghajani Nargesi, Zaniar Ghazizadeh, Mehrdad Larry, Roya Horabad Farahani, Afsaneh Morteza, Alireza Esteghamati, Claude Vigneron, Manouchehr NakhjavaniAbstract:Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic concentration is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane Cytoskeletal Proteins. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 A mu M and 1.25 mM calcium solutions. Membrane Cytoskeletal Proteins were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic concentrations of calcium (1.25 mM) induced a significant proteolysis in membrane Cytoskeletal Proteins, compared with magnesium (p \textless 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 +/- A 0.3 vs. 5.3 +/- A 0.6, p < 0.001), while spectrin (39.9 +/- A 1.0 vs. 40.3 +/- A 2.0, p = 0.393) and band-6 (6.3 +/- A 0.3 vs. 6.8 +/- A 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum concentrations (250 A mu M). Aggregation of membrane Cytoskeletal Proteins was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium concentration and aggregation of erythrocyte membrane Cytoskeletal Proteins (R (2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane Cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on Cytoskeletal Proteins need to be further investigated at extended periods of time in disease states.
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The degree of resistance of erythrocyte membrane Cytoskeletal Proteins to supra-physiologic concentrations of calcium: an in vitro study.
The Journal of Membrane Biology, 2014Co-Authors: Ebrahim Mostafavi, Arash Aghajani Nargesi, Zaniar Ghazizadeh, Mehrdad Larry, Roya Horabad Farahani, Afsaneh Morteza, Alireza Esteghamati, Claude Vigneron, Manouchehr NakhjavaniAbstract:Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic concentration is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane Cytoskeletal Proteins. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 µM and 1.25 mM calcium solutions. Membrane Cytoskeletal Proteins were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic concentrations of calcium (1.25 mM) induced a significant proteolysis in membrane Cytoskeletal Proteins, compared with magnesium (p < 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 ± 0.3 vs. 5.3 ± 0.6, p < 0.001), while spectrin (39.9 ± 1.0 vs. 40.3 ± 2.0, p = 0.393) and band-6 (6.3 ± 0.3 vs. 6.8 ± 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum concentrations (250 µM). Aggregation of membrane Cytoskeletal Proteins was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium concentration and aggregation of erythrocyte membrane Cytoskeletal Proteins (R(2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane Cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on Cytoskeletal Proteins need to be further investigated at extended periods of time in disease states.
Ebrahim Mostafavi - One of the best experts on this subject based on the ideXlab platform.
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The Degree of Resistance of Erythrocyte Membrane Cytoskeletal Proteins to Supra-Physiologic Concentrations of Calcium: An In Vitro Study
Journal of Membrane Biology, 2014Co-Authors: Ebrahim Mostafavi, Arash Aghajani Nargesi, Zaniar Ghazizadeh, Mehrdad Larry, Roya Horabad Farahani, Afsaneh Morteza, Alireza Esteghamati, Claude Vigneron, Manouchehr NakhjavaniAbstract:Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic concentration is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane Cytoskeletal Proteins. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 A mu M and 1.25 mM calcium solutions. Membrane Cytoskeletal Proteins were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic concentrations of calcium (1.25 mM) induced a significant proteolysis in membrane Cytoskeletal Proteins, compared with magnesium (p \textless 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 +/- A 0.3 vs. 5.3 +/- A 0.6, p < 0.001), while spectrin (39.9 +/- A 1.0 vs. 40.3 +/- A 2.0, p = 0.393) and band-6 (6.3 +/- A 0.3 vs. 6.8 +/- A 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum concentrations (250 A mu M). Aggregation of membrane Cytoskeletal Proteins was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium concentration and aggregation of erythrocyte membrane Cytoskeletal Proteins (R (2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane Cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on Cytoskeletal Proteins need to be further investigated at extended periods of time in disease states.
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The degree of resistance of erythrocyte membrane Cytoskeletal Proteins to supra-physiologic concentrations of calcium: an in vitro study.
The Journal of Membrane Biology, 2014Co-Authors: Ebrahim Mostafavi, Arash Aghajani Nargesi, Zaniar Ghazizadeh, Mehrdad Larry, Roya Horabad Farahani, Afsaneh Morteza, Alireza Esteghamati, Claude Vigneron, Manouchehr NakhjavaniAbstract:Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic concentration is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane Cytoskeletal Proteins. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 µM and 1.25 mM calcium solutions. Membrane Cytoskeletal Proteins were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic concentrations of calcium (1.25 mM) induced a significant proteolysis in membrane Cytoskeletal Proteins, compared with magnesium (p < 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 ± 0.3 vs. 5.3 ± 0.6, p < 0.001), while spectrin (39.9 ± 1.0 vs. 40.3 ± 2.0, p = 0.393) and band-6 (6.3 ± 0.3 vs. 6.8 ± 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum concentrations (250 µM). Aggregation of membrane Cytoskeletal Proteins was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium concentration and aggregation of erythrocyte membrane Cytoskeletal Proteins (R(2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane Cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on Cytoskeletal Proteins need to be further investigated at extended periods of time in disease states.
