The Experts below are selected from a list of 14169 Experts worldwide ranked by ideXlab platform
Lucia De Franceschi - One of the best experts on this subject based on the ideXlab platform.
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peroxiredoxin 2 expression is increased in β thalassemic mouse red cells but is displaced from the Membrane as a marker of oxidative stress
Free Radical Biology and Medicine, 2010Co-Authors: Alessandro Matte, Maria Estela Campanella, Mariarita Bertoldi, Antonella Pantaleo, Angela Siciliano, Daniela Spano, Franco Turrini, Lucia De FranceschiAbstract:Peroxiredoxin 2 (Prx2), the third most abundant cytoplasmic protein in red blood cells (RBCs), is involved in the defense against oxidative stress. Although much is known about Prx2 in healthy RBCs, its role in pathological RBCs remains largely unexplored. Here, we show that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of β-thalassemia (β-thal; Hbbth/th and Hbbth3/+ strains). We also demonstrate that the increased expression of Prx2 correlates with the severity of the disease and that the amount of Prx2 bound to the Membrane is markedly reduced in β-thal mouse RBCs. To explore the impact of oxidative stress on Prx2 Membrane association, we examined Prx2 dimerization and Membrane translocation in murine RBCs exposed to various oxidants (phenylhydrazine, PHZ; diamide; H2O2). PHZ-treated RBCs, which mimic the Membrane damage in β-thal RBCs, exhibited a kinetic correlation among Prx2 Membrane Displacement, intracellular methemoglobin levels, and hemichrome Membrane association, suggesting the possible masking of Prx2 docking sites by Membrane-bound hemichromes, providing a possible mechanism for the accumulation of oxidized/dimerized Prx2 in the cytoplasm and the increased Membrane damage in β-thal RBCs. Thus, reduced access of Prx2 to the Membrane in β-thal RBCs represents a new factor that could contribute to the oxidative damage characterizing the pathology.
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peroxiredoxin 2 expression is increased in β thalassemic mouse red cells but is displaced from the Membrane as a marker of oxidative stress
Free Radical Biology and Medicine, 2010Co-Authors: Alessandro Matte, Maria Estela Campanella, Mariarita Bertoldi, Antonella Pantaleo, Angela Siciliano, Daniela Spano, Franco Turrini, Philip S Low, Lucia De FranceschiAbstract:Peroxiredoxin 2 (Prx2), the third most abundant cytoplasmic protein in red blood cells (RBCs), is involved in the defense against oxidative stress. Although much is known about Prx2 in healthy RBCs, its role in pathological RBCs remains largely unexplored. Here, we show that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of beta-thalassemia (beta-thal; Hbb(th/th) and Hbb(th3/+) strains). We also demonstrate that the increased expression of Prx2 correlates with the severity of the disease and that the amount of Prx2 bound to the Membrane is markedly reduced in beta-thal mouse RBCs. To explore the impact of oxidative stress on Prx2 Membrane association, we examined Prx2 dimerization and Membrane translocation in murine RBCs exposed to various oxidants (phenylhydrazine, PHZ; diamide; H(2)O(2)). PHZ-treated RBCs, which mimic the Membrane damage in beta-thal RBCs, exhibited a kinetic correlation among Prx2 Membrane Displacement, intracellular methemoglobin levels, and hemichrome Membrane association, suggesting the possible masking of Prx2 docking sites by Membrane-bound hemichromes, providing a possible mechanism for the accumulation of oxidized/dimerized Prx2 in the cytoplasm and the increased Membrane damage in beta-thal RBCs. Thus, reduced access of Prx2 to the Membrane in beta-thal RBCs represents a new factor that could contribute to the oxidative damage characterizing the pathology.
Mariamagdalena Georgescu - One of the best experts on this subject based on the ideXlab platform.
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nherf1 ebp50 controls morphogenesis of 3d colonic glands by stabilizing pten and ezrin radixin moesin proteins at the apical Membrane
Neoplasia, 2014Co-Authors: Mariamagdalena Georgescu, Gilbert J Cote, Nitin K Agarwal, Charles L WhiteAbstract:Na(+)/H(+) exchanger 3 regulating factor 1/ezrin-radixin-moesin (ERM)-binding phosphoprotein 50 (NHERF1/EBP50), an adaptor molecule that interacts with the ERM-neurofibromatosis type 2 family of cytoskeletal proteins through its ERM-binding region and with phosphatase and tensin homolog (PTEN) and β-catenin through its PDZ domains, has been recently implicated in the progression of various human malignancies, including colorectal cancer (CRC). We report here that NHERF1 controls gland morphogenesis, as demonstrated in three-dimensional (3D) human intestinal glands developing from a single nonpolarized cell. Starting from the early two-cell developmental stage, NHERF1 concentrates at the cellular interface in a central Membrane disc that marks the apical pole delimiting the forming lumen. NHERF1 depletion leads to severe disruption of the apical-basal polarity, with formation of enlarged and distorted cell spheroids devoid of a central lumen. This characteristic and the increased number of mitoses in NHERF1-depleted spheroids, including multipolar ones, mimic high-grade dysplasia lesions observed in CRC progression. NHERF1 ERM-binding or PDZ-domain mutants fail to localize apically and impair gland formation most likely by outcompeting endogenous ligands, with the latter mutant completely aborting gland development. Examination of NHERF1 ligands showed that even if both ezrin and moesin colocalized with NHERF1 at the apical Membrane, moesin but not ezrin depletion disrupted morphogenesis similarly to NHERF1. NHERF1 depletion resulted also in Membrane Displacement of PTEN and nuclear translocation of β-catenin, events contributing to polarity loss and increased proliferation. These findings reveal an essential role of NHERF1 in epithelial morphogenesis and polarity and validate this 3D system for modeling the molecular changes observed in CRC.
Alessandro Matte - One of the best experts on this subject based on the ideXlab platform.
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peroxiredoxin 2 expression is increased in β thalassemic mouse red cells but is displaced from the Membrane as a marker of oxidative stress
Free Radical Biology and Medicine, 2010Co-Authors: Alessandro Matte, Maria Estela Campanella, Mariarita Bertoldi, Antonella Pantaleo, Angela Siciliano, Daniela Spano, Franco Turrini, Lucia De FranceschiAbstract:Peroxiredoxin 2 (Prx2), the third most abundant cytoplasmic protein in red blood cells (RBCs), is involved in the defense against oxidative stress. Although much is known about Prx2 in healthy RBCs, its role in pathological RBCs remains largely unexplored. Here, we show that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of β-thalassemia (β-thal; Hbbth/th and Hbbth3/+ strains). We also demonstrate that the increased expression of Prx2 correlates with the severity of the disease and that the amount of Prx2 bound to the Membrane is markedly reduced in β-thal mouse RBCs. To explore the impact of oxidative stress on Prx2 Membrane association, we examined Prx2 dimerization and Membrane translocation in murine RBCs exposed to various oxidants (phenylhydrazine, PHZ; diamide; H2O2). PHZ-treated RBCs, which mimic the Membrane damage in β-thal RBCs, exhibited a kinetic correlation among Prx2 Membrane Displacement, intracellular methemoglobin levels, and hemichrome Membrane association, suggesting the possible masking of Prx2 docking sites by Membrane-bound hemichromes, providing a possible mechanism for the accumulation of oxidized/dimerized Prx2 in the cytoplasm and the increased Membrane damage in β-thal RBCs. Thus, reduced access of Prx2 to the Membrane in β-thal RBCs represents a new factor that could contribute to the oxidative damage characterizing the pathology.
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peroxiredoxin 2 expression is increased in β thalassemic mouse red cells but is displaced from the Membrane as a marker of oxidative stress
Free Radical Biology and Medicine, 2010Co-Authors: Alessandro Matte, Maria Estela Campanella, Mariarita Bertoldi, Antonella Pantaleo, Angela Siciliano, Daniela Spano, Franco Turrini, Philip S Low, Lucia De FranceschiAbstract:Peroxiredoxin 2 (Prx2), the third most abundant cytoplasmic protein in red blood cells (RBCs), is involved in the defense against oxidative stress. Although much is known about Prx2 in healthy RBCs, its role in pathological RBCs remains largely unexplored. Here, we show that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of beta-thalassemia (beta-thal; Hbb(th/th) and Hbb(th3/+) strains). We also demonstrate that the increased expression of Prx2 correlates with the severity of the disease and that the amount of Prx2 bound to the Membrane is markedly reduced in beta-thal mouse RBCs. To explore the impact of oxidative stress on Prx2 Membrane association, we examined Prx2 dimerization and Membrane translocation in murine RBCs exposed to various oxidants (phenylhydrazine, PHZ; diamide; H(2)O(2)). PHZ-treated RBCs, which mimic the Membrane damage in beta-thal RBCs, exhibited a kinetic correlation among Prx2 Membrane Displacement, intracellular methemoglobin levels, and hemichrome Membrane association, suggesting the possible masking of Prx2 docking sites by Membrane-bound hemichromes, providing a possible mechanism for the accumulation of oxidized/dimerized Prx2 in the cytoplasm and the increased Membrane damage in beta-thal RBCs. Thus, reduced access of Prx2 to the Membrane in beta-thal RBCs represents a new factor that could contribute to the oxidative damage characterizing the pathology.
Alex C Wiedenhoeft - One of the best experts on this subject based on the ideXlab platform.
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Original Article Force–Displacement measurements of earlywood bordered pits using a mesomechanical tester
2016Co-Authors: Samuel L Zelinka, Keith J Bourne, John C Hermanson, Samuel V Glass, Adriana Costa, Alex C WiedenhoeftAbstract:The elastic properties of pit Membranes are reported to have important implications in understanding air-seeding phe-nomena in gymnosperms, and pit aspiration plays a large role in wood technological applications such as wood drying and preservative treatment. Here we present force–Displacement measurements for pit Membranes of circular bordered pits, collected on a mesomechanical testing system. The system consists of a quartz microprobe attached to a micro-force sensor that is positioned and advanced with a micromanipulator mounted on an inverted microscope. Membrane Displacement is measured from digital image analysis. Unaspirated pits from earlywood of never-dried wood of Larix and Pinus and aspirated pits from earlywood of dried wood of Larix were tested to generate force– Displacement curves up to the point of Membrane failure. Two failure modes were observed: rupture or tearing of the pit Membrane by the microprobe tip, and the stretching of the pit Membrane until the torus was forced out of the pit chamber through the pit aperture without rupture, a condi-tion we refer to as torus prolapse. Key-words: air seeding; mesomechanical testing; pit mem-brane; torus prolapse; wood preservative treatment
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force Displacement measurements of earlywood bordered pits using a mesomechanical tester
Plant Cell and Environment, 2015Co-Authors: Samuel L Zelinka, Keith J Bourne, John C Hermanson, Samuel V Glass, Adriana Costa, Alex C WiedenhoeftAbstract:The elastic properties of pit Membranes are reported to have important implications in understanding air-seeding phenomena in gymnosperms, and pit aspiration plays a large role in wood technological applications such as wood drying and preservative treatment. Here we present force-Displacement measurements for pit Membranes of circular bordered pits, collected on a mesomechanical testing system. The system consists of a quartz microprobe attached to a microforce sensor that is positioned and advanced with a micromanipulator mounted on an inverted microscope. Membrane Displacement is measured from digital image analysis. Unaspirated pits from earlywood of never-dried wood of Larix and Pinus and aspirated pits from earlywood of dried wood of Larix were tested to generate force-Displacement curves up to the point of Membrane failure. Two failure modes were observed: rupture or tearing of the pit Membrane by the microprobe tip, and the stretching of the pit Membrane until the torus was forced out of the pit chamber through the pit aperture without rupture, a condition we refer to as torus prolapse.
Charles L White - One of the best experts on this subject based on the ideXlab platform.
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nherf1 ebp50 controls morphogenesis of 3d colonic glands by stabilizing pten and ezrin radixin moesin proteins at the apical Membrane
Neoplasia, 2014Co-Authors: Mariamagdalena Georgescu, Gilbert J Cote, Nitin K Agarwal, Charles L WhiteAbstract:Na(+)/H(+) exchanger 3 regulating factor 1/ezrin-radixin-moesin (ERM)-binding phosphoprotein 50 (NHERF1/EBP50), an adaptor molecule that interacts with the ERM-neurofibromatosis type 2 family of cytoskeletal proteins through its ERM-binding region and with phosphatase and tensin homolog (PTEN) and β-catenin through its PDZ domains, has been recently implicated in the progression of various human malignancies, including colorectal cancer (CRC). We report here that NHERF1 controls gland morphogenesis, as demonstrated in three-dimensional (3D) human intestinal glands developing from a single nonpolarized cell. Starting from the early two-cell developmental stage, NHERF1 concentrates at the cellular interface in a central Membrane disc that marks the apical pole delimiting the forming lumen. NHERF1 depletion leads to severe disruption of the apical-basal polarity, with formation of enlarged and distorted cell spheroids devoid of a central lumen. This characteristic and the increased number of mitoses in NHERF1-depleted spheroids, including multipolar ones, mimic high-grade dysplasia lesions observed in CRC progression. NHERF1 ERM-binding or PDZ-domain mutants fail to localize apically and impair gland formation most likely by outcompeting endogenous ligands, with the latter mutant completely aborting gland development. Examination of NHERF1 ligands showed that even if both ezrin and moesin colocalized with NHERF1 at the apical Membrane, moesin but not ezrin depletion disrupted morphogenesis similarly to NHERF1. NHERF1 depletion resulted also in Membrane Displacement of PTEN and nuclear translocation of β-catenin, events contributing to polarity loss and increased proliferation. These findings reveal an essential role of NHERF1 in epithelial morphogenesis and polarity and validate this 3D system for modeling the molecular changes observed in CRC.