The Experts below are selected from a list of 327 Experts worldwide ranked by ideXlab platform
Tarek Chehab - One of the best experts on this subject based on the ideXlab platform.
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Analysis of Ca 2+ -Dependent Weibel–Palade Body Tethering by Live Cell TIRF Microscopy: Involvement of a Munc13-4/S100A10/Annexin A2 Complex
Methods in Molecular Biology, 2019Co-Authors: Nina Criado Santos, Tarek Chehab, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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analysis of ca 2 dependent weibel palade body tethering by live cell tirf microscopy involvement of a munc13 4 s100a10 annexin a2 complex
Methods of Molecular Biology, 2019Co-Authors: Tarek Chehab, Nina Criado Santos, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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A novel Munc13-4/S100A10/Annexin A2 complex promotes Weibel-Palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
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a novel munc13 4 s100a10 annexin a2 complex promotes weibel palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
Kwun-nok Mimi Man - One of the best experts on this subject based on the ideXlab platform.
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A novel Munc13-4/S100A10/Annexin A2 complex promotes Weibel-Palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
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a novel munc13 4 s100a10 annexin a2 complex promotes weibel palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
Volker Gerke - One of the best experts on this subject based on the ideXlab platform.
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Analysis of Ca 2+ -Dependent Weibel–Palade Body Tethering by Live Cell TIRF Microscopy: Involvement of a Munc13-4/S100A10/Annexin A2 Complex
Methods in Molecular Biology, 2019Co-Authors: Nina Criado Santos, Tarek Chehab, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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analysis of ca 2 dependent weibel palade body tethering by live cell tirf microscopy involvement of a munc13 4 s100a10 annexin a2 complex
Methods of Molecular Biology, 2019Co-Authors: Tarek Chehab, Nina Criado Santos, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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Annexins A2 and A8 in endothelial cell exocytosis and the control of vascular homeostasis
Biological chemistry, 2016Co-Authors: Volker GerkeAbstract:Blood Vessel homeostasis is controlled by a variety of regulatory circuits that involve both the Vessel-lining endothelial cells as well as the circulating Blood cells and products thereof. One important feature is the control exerted by endothelial cells through regulated exocytosis of factors affecting Blood coagulation and local inflammatory processes. These factors include two important adhesion proteins: the leukocyte receptor P-selectin and the pro-coagulant von Willebrand factor (VWF) that binds platelets and is involved in the formation of a platelet plug at sites of Blood Vessel Injury. Failure to correctly produce and secrete P-selectin and VWF leads to pathologies such as von Willebrand disease, the most common inherited bleeding disorder. P-selectin and VWF are stored in unique secretory granules, the Weibel-Palade bodies (WPB), that undergo a complex maturation process and are acutely secreted following endothelial stimulation, e.g. in the course of inflammation or following Blood Vessel Injury. Two annexins have been shown to be involved in different aspects of WPB biology: annexin A8 is required for proper WPB maturation and annexin A2 participates in late steps of WPB exocytosis. Thus, by affecting the stimulated release of P-selectin and VWF from endothelial cells, annexins fulfil important functions in the control of vascular homeostasis and could be considered as targets for influencing P-selectin- and VWF-dependent processes/pathologies.
Nina Criado Santos - One of the best experts on this subject based on the ideXlab platform.
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Analysis of Ca 2+ -Dependent Weibel–Palade Body Tethering by Live Cell TIRF Microscopy: Involvement of a Munc13-4/S100A10/Annexin A2 Complex
Methods in Molecular Biology, 2019Co-Authors: Nina Criado Santos, Tarek Chehab, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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analysis of ca 2 dependent weibel palade body tethering by live cell tirf microscopy involvement of a munc13 4 s100a10 annexin a2 complex
Methods of Molecular Biology, 2019Co-Authors: Tarek Chehab, Nina Criado Santos, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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A novel Munc13-4/S100A10/Annexin A2 complex promotes Weibel-Palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
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a novel munc13 4 s100a10 annexin a2 complex promotes weibel palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
Anna Holthenrich - One of the best experts on this subject based on the ideXlab platform.
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Analysis of Ca 2+ -Dependent Weibel–Palade Body Tethering by Live Cell TIRF Microscopy: Involvement of a Munc13-4/S100A10/Annexin A2 Complex
Methods in Molecular Biology, 2019Co-Authors: Nina Criado Santos, Tarek Chehab, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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analysis of ca 2 dependent weibel palade body tethering by live cell tirf microscopy involvement of a munc13 4 s100a10 annexin a2 complex
Methods of Molecular Biology, 2019Co-Authors: Tarek Chehab, Nina Criado Santos, Anna Holthenrich, Volker GerkeAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated, Ca2+-dependent exocytosis of WPBs critically depends on their proper targeting to the plasma membrane, but the mechanism of WPB-plasma membrane tethering prior to fusion is not well characterized. Here we describe a method to visualize and analyze WPB tethering and fusion in living human umbilical vein endothelial cells (HUVEC) by total internal reflection fluorescence (TIRF) microscopy. This method is based on automated object detection and allowed us to identify components of the tethering complex of WPBs and to monitor their dynamics in space and time. An important tethering factor identified by this means was Munc13-4 that was shown to interact with S100A10 residing in a complex with plasma membrane-bound annexin A2.
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A novel Munc13-4/S100A10/Annexin A2 complex promotes Weibel-Palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
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a novel munc13 4 s100a10 annexin a2 complex promotes weibel palade body exocytosis in endothelial cells
Molecular Biology of the Cell, 2017Co-Authors: Tarek Chehab, Ali Reza Nazmi, Nina Criado Santos, Anna Holthenrich, Sophia N. Koerdt, Jennifer Disse, Christian Schuberth, Maaike Neeft, Henriette Koch, Kwun-nok Mimi ManAbstract:Endothelial cells respond to Blood Vessel Injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel-Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB-plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB-plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.