The Experts below are selected from a list of 6 Experts worldwide ranked by ideXlab platform
Masahiro Maki - One of the best experts on this subject based on the ideXlab platform.
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effects of Calphobindin II annexin vi on procoagulant and anticoagulant activities of cultured endothelial cells
Chemical & Pharmaceutical Bulletin, 1992Co-Authors: Hideo Yoshizaki, Koichi Arai, Yohichi Hashimoto, Masao Ohkuchi, Sohei Tanabe, Akira Murakami, Yasushi Wada, Masahiro MakiAbstract:Effects of human placental Calphobindin II (CPB-II) on the protein C activation and prothrombin activation on the cell surface of cultured calf pulmonary arterial endothelial cells have been investigated. CPB-II inhibited thrombin generation by factor Xa bound to the surface of the cultured endothelial cells in a dose-dependent manner. The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM. CPB-II was found to be ineffective, however, in the protein C activation by thrombin-thrombomodulin (TM) complex on the cell surface. Assay using purified TM revealed that CPB-II was able to exhibit the inhibitory potency for the protein C activation exclusively in the reconstituted system with negatively charged phospholipids. These results suggest that the neutral phospholipids participate in the protein C activation through the thrombin-TM system on the endothelial cell surface. The ability of CPB-II to inhibit procoagulant activity without affecting anticoagulant activity on the cultured endothelial cells is probably related to its potential physiological function, while it is able to exert various degrees of influence upon these activities in blood coagulation by interacting with negatively charged phospholipids in vitro.
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phospholipid binding properties of Calphobindin II annexin vi an anticoagulant protein from human placenta
Chemical & Pharmaceutical Bulletin, 1991Co-Authors: Hideo Yoshizaki, Yoshihiro Shidara, Koichi Arai, Masami Shiratsuchi, Yohichi Hashimoto, Masao Ohkuchi, Masahiro MakiAbstract:Calphobindin-II (CPB-II, annexin VI), is a calcium dependent phospholipid binding protein that can be classified as a member of the annexin family. The phospholipid-binding properties of CPB-II were investigated by measuring the binding constants of [125I]-CPB-II using phospholipid vesicles consisting of 80% phosphatidylcholine and 20% phosphatidylserine. A dissociation constant (Kd) of CPB-II with the phospholipid vesicles was determined to be 0.2 to 0.3 nM in the presence of Ca2+ ranging from 0.3 to 30 mM. The number of CPB-II capable of binding to the phospholipid vesicles at 0.3 mM Ca2+ decreased to about 1/2 in the presence of Ca2+ of more than 1 mM. Prothrombin and factor X were effective in competing with the binding of CPB-II to the phospholipid vesicles, although their affinities were lower by two or three orders of magnitude than that of unlabeled CPB-II at 30 nM Ca2+. Competitive effects of CPB-II, Calphobindin-I (CPB-I, annexin V) and Calphobindin-III (CPB-III, annexin III) on binding of [125I]-CPB-II to phospholipid vesicles, were similarly observed.
Hideo Yoshizaki - One of the best experts on this subject based on the ideXlab platform.
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effects of Calphobindin II annexin vi on procoagulant and anticoagulant activities of cultured endothelial cells
Chemical & Pharmaceutical Bulletin, 1992Co-Authors: Hideo Yoshizaki, Koichi Arai, Yohichi Hashimoto, Masao Ohkuchi, Sohei Tanabe, Akira Murakami, Yasushi Wada, Masahiro MakiAbstract:Effects of human placental Calphobindin II (CPB-II) on the protein C activation and prothrombin activation on the cell surface of cultured calf pulmonary arterial endothelial cells have been investigated. CPB-II inhibited thrombin generation by factor Xa bound to the surface of the cultured endothelial cells in a dose-dependent manner. The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM. CPB-II was found to be ineffective, however, in the protein C activation by thrombin-thrombomodulin (TM) complex on the cell surface. Assay using purified TM revealed that CPB-II was able to exhibit the inhibitory potency for the protein C activation exclusively in the reconstituted system with negatively charged phospholipids. These results suggest that the neutral phospholipids participate in the protein C activation through the thrombin-TM system on the endothelial cell surface. The ability of CPB-II to inhibit procoagulant activity without affecting anticoagulant activity on the cultured endothelial cells is probably related to its potential physiological function, while it is able to exert various degrees of influence upon these activities in blood coagulation by interacting with negatively charged phospholipids in vitro.
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phospholipid binding properties of Calphobindin II annexin vi an anticoagulant protein from human placenta
Chemical & Pharmaceutical Bulletin, 1991Co-Authors: Hideo Yoshizaki, Yoshihiro Shidara, Koichi Arai, Masami Shiratsuchi, Yohichi Hashimoto, Masao Ohkuchi, Masahiro MakiAbstract:Calphobindin-II (CPB-II, annexin VI), is a calcium dependent phospholipid binding protein that can be classified as a member of the annexin family. The phospholipid-binding properties of CPB-II were investigated by measuring the binding constants of [125I]-CPB-II using phospholipid vesicles consisting of 80% phosphatidylcholine and 20% phosphatidylserine. A dissociation constant (Kd) of CPB-II with the phospholipid vesicles was determined to be 0.2 to 0.3 nM in the presence of Ca2+ ranging from 0.3 to 30 mM. The number of CPB-II capable of binding to the phospholipid vesicles at 0.3 mM Ca2+ decreased to about 1/2 in the presence of Ca2+ of more than 1 mM. Prothrombin and factor X were effective in competing with the binding of CPB-II to the phospholipid vesicles, although their affinities were lower by two or three orders of magnitude than that of unlabeled CPB-II at 30 nM Ca2+. Competitive effects of CPB-II, Calphobindin-I (CPB-I, annexin V) and Calphobindin-III (CPB-III, annexin III) on binding of [125I]-CPB-II to phospholipid vesicles, were similarly observed.
Koichi Arai - One of the best experts on this subject based on the ideXlab platform.
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effects of Calphobindin II annexin vi on procoagulant and anticoagulant activities of cultured endothelial cells
Chemical & Pharmaceutical Bulletin, 1992Co-Authors: Hideo Yoshizaki, Koichi Arai, Yohichi Hashimoto, Masao Ohkuchi, Sohei Tanabe, Akira Murakami, Yasushi Wada, Masahiro MakiAbstract:Effects of human placental Calphobindin II (CPB-II) on the protein C activation and prothrombin activation on the cell surface of cultured calf pulmonary arterial endothelial cells have been investigated. CPB-II inhibited thrombin generation by factor Xa bound to the surface of the cultured endothelial cells in a dose-dependent manner. The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM. CPB-II was found to be ineffective, however, in the protein C activation by thrombin-thrombomodulin (TM) complex on the cell surface. Assay using purified TM revealed that CPB-II was able to exhibit the inhibitory potency for the protein C activation exclusively in the reconstituted system with negatively charged phospholipids. These results suggest that the neutral phospholipids participate in the protein C activation through the thrombin-TM system on the endothelial cell surface. The ability of CPB-II to inhibit procoagulant activity without affecting anticoagulant activity on the cultured endothelial cells is probably related to its potential physiological function, while it is able to exert various degrees of influence upon these activities in blood coagulation by interacting with negatively charged phospholipids in vitro.
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phospholipid binding properties of Calphobindin II annexin vi an anticoagulant protein from human placenta
Chemical & Pharmaceutical Bulletin, 1991Co-Authors: Hideo Yoshizaki, Yoshihiro Shidara, Koichi Arai, Masami Shiratsuchi, Yohichi Hashimoto, Masao Ohkuchi, Masahiro MakiAbstract:Calphobindin-II (CPB-II, annexin VI), is a calcium dependent phospholipid binding protein that can be classified as a member of the annexin family. The phospholipid-binding properties of CPB-II were investigated by measuring the binding constants of [125I]-CPB-II using phospholipid vesicles consisting of 80% phosphatidylcholine and 20% phosphatidylserine. A dissociation constant (Kd) of CPB-II with the phospholipid vesicles was determined to be 0.2 to 0.3 nM in the presence of Ca2+ ranging from 0.3 to 30 mM. The number of CPB-II capable of binding to the phospholipid vesicles at 0.3 mM Ca2+ decreased to about 1/2 in the presence of Ca2+ of more than 1 mM. Prothrombin and factor X were effective in competing with the binding of CPB-II to the phospholipid vesicles, although their affinities were lower by two or three orders of magnitude than that of unlabeled CPB-II at 30 nM Ca2+. Competitive effects of CPB-II, Calphobindin-I (CPB-I, annexin V) and Calphobindin-III (CPB-III, annexin III) on binding of [125I]-CPB-II to phospholipid vesicles, were similarly observed.
Yohichi Hashimoto - One of the best experts on this subject based on the ideXlab platform.
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effects of Calphobindin II annexin vi on procoagulant and anticoagulant activities of cultured endothelial cells
Chemical & Pharmaceutical Bulletin, 1992Co-Authors: Hideo Yoshizaki, Koichi Arai, Yohichi Hashimoto, Masao Ohkuchi, Sohei Tanabe, Akira Murakami, Yasushi Wada, Masahiro MakiAbstract:Effects of human placental Calphobindin II (CPB-II) on the protein C activation and prothrombin activation on the cell surface of cultured calf pulmonary arterial endothelial cells have been investigated. CPB-II inhibited thrombin generation by factor Xa bound to the surface of the cultured endothelial cells in a dose-dependent manner. The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM. CPB-II was found to be ineffective, however, in the protein C activation by thrombin-thrombomodulin (TM) complex on the cell surface. Assay using purified TM revealed that CPB-II was able to exhibit the inhibitory potency for the protein C activation exclusively in the reconstituted system with negatively charged phospholipids. These results suggest that the neutral phospholipids participate in the protein C activation through the thrombin-TM system on the endothelial cell surface. The ability of CPB-II to inhibit procoagulant activity without affecting anticoagulant activity on the cultured endothelial cells is probably related to its potential physiological function, while it is able to exert various degrees of influence upon these activities in blood coagulation by interacting with negatively charged phospholipids in vitro.
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phospholipid binding properties of Calphobindin II annexin vi an anticoagulant protein from human placenta
Chemical & Pharmaceutical Bulletin, 1991Co-Authors: Hideo Yoshizaki, Yoshihiro Shidara, Koichi Arai, Masami Shiratsuchi, Yohichi Hashimoto, Masao Ohkuchi, Masahiro MakiAbstract:Calphobindin-II (CPB-II, annexin VI), is a calcium dependent phospholipid binding protein that can be classified as a member of the annexin family. The phospholipid-binding properties of CPB-II were investigated by measuring the binding constants of [125I]-CPB-II using phospholipid vesicles consisting of 80% phosphatidylcholine and 20% phosphatidylserine. A dissociation constant (Kd) of CPB-II with the phospholipid vesicles was determined to be 0.2 to 0.3 nM in the presence of Ca2+ ranging from 0.3 to 30 mM. The number of CPB-II capable of binding to the phospholipid vesicles at 0.3 mM Ca2+ decreased to about 1/2 in the presence of Ca2+ of more than 1 mM. Prothrombin and factor X were effective in competing with the binding of CPB-II to the phospholipid vesicles, although their affinities were lower by two or three orders of magnitude than that of unlabeled CPB-II at 30 nM Ca2+. Competitive effects of CPB-II, Calphobindin-I (CPB-I, annexin V) and Calphobindin-III (CPB-III, annexin III) on binding of [125I]-CPB-II to phospholipid vesicles, were similarly observed.
Masao Ohkuchi - One of the best experts on this subject based on the ideXlab platform.
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effects of Calphobindin II annexin vi on procoagulant and anticoagulant activities of cultured endothelial cells
Chemical & Pharmaceutical Bulletin, 1992Co-Authors: Hideo Yoshizaki, Koichi Arai, Yohichi Hashimoto, Masao Ohkuchi, Sohei Tanabe, Akira Murakami, Yasushi Wada, Masahiro MakiAbstract:Effects of human placental Calphobindin II (CPB-II) on the protein C activation and prothrombin activation on the cell surface of cultured calf pulmonary arterial endothelial cells have been investigated. CPB-II inhibited thrombin generation by factor Xa bound to the surface of the cultured endothelial cells in a dose-dependent manner. The amount (IC50) of CPB-II causing the inhibition at 50% was estimated to be approximately 10 nM. CPB-II was found to be ineffective, however, in the protein C activation by thrombin-thrombomodulin (TM) complex on the cell surface. Assay using purified TM revealed that CPB-II was able to exhibit the inhibitory potency for the protein C activation exclusively in the reconstituted system with negatively charged phospholipids. These results suggest that the neutral phospholipids participate in the protein C activation through the thrombin-TM system on the endothelial cell surface. The ability of CPB-II to inhibit procoagulant activity without affecting anticoagulant activity on the cultured endothelial cells is probably related to its potential physiological function, while it is able to exert various degrees of influence upon these activities in blood coagulation by interacting with negatively charged phospholipids in vitro.
-
phospholipid binding properties of Calphobindin II annexin vi an anticoagulant protein from human placenta
Chemical & Pharmaceutical Bulletin, 1991Co-Authors: Hideo Yoshizaki, Yoshihiro Shidara, Koichi Arai, Masami Shiratsuchi, Yohichi Hashimoto, Masao Ohkuchi, Masahiro MakiAbstract:Calphobindin-II (CPB-II, annexin VI), is a calcium dependent phospholipid binding protein that can be classified as a member of the annexin family. The phospholipid-binding properties of CPB-II were investigated by measuring the binding constants of [125I]-CPB-II using phospholipid vesicles consisting of 80% phosphatidylcholine and 20% phosphatidylserine. A dissociation constant (Kd) of CPB-II with the phospholipid vesicles was determined to be 0.2 to 0.3 nM in the presence of Ca2+ ranging from 0.3 to 30 mM. The number of CPB-II capable of binding to the phospholipid vesicles at 0.3 mM Ca2+ decreased to about 1/2 in the presence of Ca2+ of more than 1 mM. Prothrombin and factor X were effective in competing with the binding of CPB-II to the phospholipid vesicles, although their affinities were lower by two or three orders of magnitude than that of unlabeled CPB-II at 30 nM Ca2+. Competitive effects of CPB-II, Calphobindin-I (CPB-I, annexin V) and Calphobindin-III (CPB-III, annexin III) on binding of [125I]-CPB-II to phospholipid vesicles, were similarly observed.
