The Experts below are selected from a list of 10389 Experts worldwide ranked by ideXlab platform
Chikako Ohwada - One of the best experts on this subject based on the ideXlab platform.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & molecular medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & Molecular Medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism. A regulatory pathway that governs cleavage of a cell-surface protein may influence this molecule's contribution to human disease. The protein LR11 is typically embedded in the cell membrane, but its outward-facing portion can be sheared away to yield soluble LR11 (sLR11). Abnormal levels of sLR11 are associated with diverse ailments, including cardiovascular disease and leukemia. Chiaki Nakaseko's team at Chiba University Hospital, Japan, has identified one Mechanism controlling this cleavage. The enzyme ADAM17 mediates release of other cell-surface proteins. Nakaseko and colleagues showed that ADAM17 facilitates sLR11 production in leukemia cell lines. The researchers also identified another protein, CD9, which acts as a potent inhibitor of sLR11 processing. This protein does not appear to be active in leukemia lymph node samples, however, suggesting that cleavage may be modulated by alternate pathways in these patients.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & Molecular Medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:A regulatory pathway that governs cleavage of a cell-surface protein may influence this molecule's contribution to human disease. The protein LR11 is typically embedded in the cell membrane, but its outward-facing portion can be sheared away to yield soluble LR11 (sLR11). Abnormal levels of sLR11 are associated with diverse ailments, including cardiovascular disease and leukemia. Chiaki Nakaseko's team at Chiba University Hospital, Japan, has identified one Mechanism controlling this cleavage. The enzyme ADAM17 mediates release of other cell-surface proteins. Nakaseko and colleagues showed that ADAM17 facilitates sLR11 production in leukemia cell lines. The researchers also identified another protein, CD9, which acts as a potent inhibitor of sLR11 processing. This protein does not appear to be active in leukemia lymph node samples, however, suggesting that cleavage may be modulated by alternate pathways in these patients. LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism.
Christian Poelma - One of the best experts on this subject based on the ideXlab platform.
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Investigation of cavitation and vapor Shedding Mechanisms in a Venturi nozzle
Physics of Fluids, 2020Co-Authors: Maxwell Brunhart, Celia Soteriou, Manolis Gavaises, I.k. Karathanassis, Phoevos Koukouvinis, Saad Jahangir, Christian PoelmaAbstract:Cavitating flow dynamics are investigated in an axisymmetric converging–diverging Venturi nozzle. Computational Fluid Dynamics (CFD) results are compared with those from previous experiments. New analysis performed on the quantitative results from both datasets reveals a coherent trend and shows that the simulations and experiments agree well. The CFD results have confirmed the interpretation of the high-speed images of the Venturi flow, which indicated that there are two vapor Shedding Mechanisms that exist under different running conditions: re-entrant jet and condensation shock. Moreover, they provide further details of the flow Mechanisms that cannot be extracted from the experiments. For the first time with this cavitating Venturi nozzle, the re-entrant jet Shedding Mechanism is reliably achieved in CFD simulations. The condensation shock Shedding Mechanism is also confirmed, and details of the process are presented. These CFD results compare well with the experimental shadowgraphs, space–time plots, and time-averaged reconstructed computed tomography slices of vapor fraction.
Shokichi Tsukamoto - One of the best experts on this subject based on the ideXlab platform.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & molecular medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & Molecular Medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism. A regulatory pathway that governs cleavage of a cell-surface protein may influence this molecule's contribution to human disease. The protein LR11 is typically embedded in the cell membrane, but its outward-facing portion can be sheared away to yield soluble LR11 (sLR11). Abnormal levels of sLR11 are associated with diverse ailments, including cardiovascular disease and leukemia. Chiaki Nakaseko's team at Chiba University Hospital, Japan, has identified one Mechanism controlling this cleavage. The enzyme ADAM17 mediates release of other cell-surface proteins. Nakaseko and colleagues showed that ADAM17 facilitates sLR11 production in leukemia cell lines. The researchers also identified another protein, CD9, which acts as a potent inhibitor of sLR11 processing. This protein does not appear to be active in leukemia lymph node samples, however, suggesting that cleavage may be modulated by alternate pathways in these patients.
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Tetraspanin CD9 modulates ADAM17-mediated Shedding of LR11 in leukocytes
Experimental & Molecular Medicine, 2014Co-Authors: Shokichi Tsukamoto, Masahiro Takeuchi, Takeharu Kawaguchi, Emi Togasaki, Atsuko Yamazaki, Yasumasa Sugita, Tomoya Muto, Shio Sakai, Yusuke Takeda, Chikako OhwadaAbstract:A regulatory pathway that governs cleavage of a cell-surface protein may influence this molecule's contribution to human disease. The protein LR11 is typically embedded in the cell membrane, but its outward-facing portion can be sheared away to yield soluble LR11 (sLR11). Abnormal levels of sLR11 are associated with diverse ailments, including cardiovascular disease and leukemia. Chiaki Nakaseko's team at Chiba University Hospital, Japan, has identified one Mechanism controlling this cleavage. The enzyme ADAM17 mediates release of other cell-surface proteins. Nakaseko and colleagues showed that ADAM17 facilitates sLR11 production in leukemia cell lines. The researchers also identified another protein, CD9, which acts as a potent inhibitor of sLR11 processing. This protein does not appear to be active in leukemia lymph node samples, however, suggesting that cleavage may be modulated by alternate pathways in these patients. LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic Shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A Shedding Mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated Shedding of tumor necrosis factor-α and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the Shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated Shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated Shedding Mechanism.
Maxwell Brunhart - One of the best experts on this subject based on the ideXlab platform.
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Investigation of cavitation and vapor Shedding Mechanisms in a Venturi nozzle
Physics of Fluids, 2020Co-Authors: Maxwell Brunhart, Celia Soteriou, Manolis Gavaises, I.k. Karathanassis, Phoevos Koukouvinis, Saad Jahangir, Christian PoelmaAbstract:Cavitating flow dynamics are investigated in an axisymmetric converging–diverging Venturi nozzle. Computational Fluid Dynamics (CFD) results are compared with those from previous experiments. New analysis performed on the quantitative results from both datasets reveals a coherent trend and shows that the simulations and experiments agree well. The CFD results have confirmed the interpretation of the high-speed images of the Venturi flow, which indicated that there are two vapor Shedding Mechanisms that exist under different running conditions: re-entrant jet and condensation shock. Moreover, they provide further details of the flow Mechanisms that cannot be extracted from the experiments. For the first time with this cavitating Venturi nozzle, the re-entrant jet Shedding Mechanism is reliably achieved in CFD simulations. The condensation shock Shedding Mechanism is also confirmed, and details of the process are presented. These CFD results compare well with the experimental shadowgraphs, space–time plots, and time-averaged reconstructed computed tomography slices of vapor fraction.
J. H. Gerrard - One of the best experts on this subject based on the ideXlab platform.
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Vorticity measurements in the near wake of a circular cylinder at low Reynolds numbers
Journal of Fluid Mechanics, 1993Co-Authors: R. B. Green, J. H. GerrardAbstract:The technique of the particle streak method has been applied to the study of bluff-body wakes at low Reynolds number. Vorticity and shear stress were measured to an accuracy of 15–20%. The vortex Shedding cycles at Reynolds number of 73 and 226 are shown and the differences between the two are highlighted. Quantitative descriptions of the previously described vortex splitting phenomenon in the near wake are made, which leads to a description of the vortex Shedding Mechanism at low Reynolds number. The definition of low-Reynolds-number formation region length is examined. The strength of shed vortices obtained from integration of the vorticity is compared with directly measured vortex strengths and with the results of two-dimensional numerical analysis.
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AN OPTICAL INTERFEROMETRIC STUDY OF THE WAKE OF A BLUFF BODY
Journal of Fluid Mechanics, 1991Co-Authors: R. B. Green, J. H. GerrardAbstract:A Fizeau optical interferometer has been used to visualize the wake behind a circular cylinder at low Reynolds numbers Re. As well as showing the vortex Shedding Mechanism and developement of the far wake in a new light, the shed vortex strength and age were derived from the results. The vortex velocity distributions, at downstream distances of 5 to 16 diameters, were found to be those of convected Oseen vortices
