The Experts below are selected from a list of 723 Experts worldwide ranked by ideXlab platform
Gabriela A Ibanez - One of the best experts on this subject based on the ideXlab platform.
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second order multivariate models for the processing of standard addition synchronous fluorescence ph data application to the analysis of salicylic Acid and its major metabolite in human urine
Talanta, 2014Co-Authors: Ariana P Pagani, Gabriela A IbanezAbstract:Abstract In the present work, we describe the determination of salicylic Acid and its major metabolite, Salicyluric Acid, in spiked human urine samples, using synchronous fluorescence spectra measured in a flow-injection system with a double pH gradient. Because the fluorescent urine background constitutes a potentially interfering signal, it becomes necessary to achieve the second-order advantage. Moreover, due to significant changes in the signal of the analytes in the presence of the urine matrix, mainly for Salicyluric Acid, standard addition was required in order to obtain appropriate quantifications. Several second-order multivariate calibration models were evaluated for this purpose: PARAFAC and MCR-ALS in two different modes, and PLS/RBL.
Ariana P Pagani - One of the best experts on this subject based on the ideXlab platform.
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second order multivariate models for the processing of standard addition synchronous fluorescence ph data application to the analysis of salicylic Acid and its major metabolite in human urine
Talanta, 2014Co-Authors: Ariana P Pagani, Gabriela A IbanezAbstract:Abstract In the present work, we describe the determination of salicylic Acid and its major metabolite, Salicyluric Acid, in spiked human urine samples, using synchronous fluorescence spectra measured in a flow-injection system with a double pH gradient. Because the fluorescent urine background constitutes a potentially interfering signal, it becomes necessary to achieve the second-order advantage. Moreover, due to significant changes in the signal of the analytes in the presence of the urine matrix, mainly for Salicyluric Acid, standard addition was required in order to obtain appropriate quantifications. Several second-order multivariate calibration models were evaluated for this purpose: PARAFAC and MCR-ALS in two different modes, and PLS/RBL.
Robert S. Greenfield - One of the best experts on this subject based on the ideXlab platform.
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Alternative Mechanism of Aspirin in Anti-Thrombotic Therapy: Inhibition of Thrombin Activatable Fibrinolysis Inhibitor
Bulletin of the Korean Chemical Society, 2012Co-Authors: Seong Soo, Robert S. GreenfieldAbstract:The use of aspirin is widely recommended for the prevention of heart attacks owing to its ability to inhibit platelet activation by irreversibly blocking cyclooxygenase 1. However, aspirin also affects the fibrinolytic and hemostatic pathways by mechanisms that are not well understood, causing severe hemorrhagic complications. Here, we investigated the ability of aspirin and aspirin metabolites to inhibit thrombin-activatable fibrinolysis inhibitor (TAFI), the major inhibitor of plasma fibrinolysis. TAFI is activated via proteolytic cleavage by the thrombin-thrombomodulin complex to TAFIa, a carboxypeptidase B-like enzyme. TAFIa modulates fibrinolysis by removing the C-terminal arginine and lysine residues from partially degraded fibrin, which in turn inhibits the binding of plasminogen to fibrin clots. Aspirin and its major metabolites, salicylic Acid, gentisic Acid, and Salicyluric Acid, inhibit TAFIa carboxypeptidase activity. Salicyluric Acid effectively blocks activation of TAFI by thrombin-thrombomodulin; however, salicylates do not inhibit carboxypeptidase N or pancreatic carboxypeptidase B. Aspirin and other salicylates accelerated the dissolution of fibrin clots and reduced thrombus formation in an in vitro model of fibrinolysis. Inhibition of TAFI represents a novel hemostatic mechanism that contributes to aspirin’s therapy-associated antithrombotic activity and hemorrhagic complications.
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Alternative Mechanism of Aspirin in Anti-Thrombotic Therapy: Inhibition of Thrombin Activatable Fibrinolysis Inhibitor
2012Co-Authors: Seong Soo, Robert S. GreenfieldAbstract:The use of aspirin is widely recommended for the prevention of heart attacks owing to its ability to inhibit platelet activation by irreversibly blocking cyclooxygenase 1. However, aspirin also affects the fibrinolytic and hemostatic pathways by mechanisms that are not well understood, causing severe hemorrhagic complications. Here, we investigated the ability of aspirin and aspirin metabolites to inhibit thrombin-activatable fibrinolysis inhibitor (TAFI), the major inhibitor of plasma fibrinolysis. TAFI is activated via proteolytic cleavage by the thrombin-thrombomodulin complex to TAFIa, a carboxypeptidase B-like enzyme. TAFIa modulates fibrinolysis by removing the C-terminal arginine and lysine residues from partially degraded fibrin, which in turn inhibits the binding of plasminogen to fibrin clots. Aspirin and its major metabolites, salicylic Acid, gentisic Acid, and Salicyluric Acid, inhibit TAFIa carboxypeptidase activity. Salicyluric Acid effectively blocks activation of TAFI by thrombin-thrombomodulin; however, salicylates do not inhibit carboxypeptidase N or pancreatic carboxypeptidase B. Aspirin and other salicylates accelerated the dissolution of fibrin clots and reduced thrombus formation in an in vitro model of fibrinolysis. Inhibition of TAFI represents a novel hemostatic mechanism that contributes to aspirin’s therapy-associated antithrombotic activity and hemorrhagic complications. Key Words: Aspirin, Thrombin activatable fibrinolysis inhibitor (TAFI), Fibrinolysi
Seong Soo - One of the best experts on this subject based on the ideXlab platform.
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Alternative Mechanism of Aspirin in Anti-Thrombotic Therapy: Inhibition of Thrombin Activatable Fibrinolysis Inhibitor
Bulletin of the Korean Chemical Society, 2012Co-Authors: Seong Soo, Robert S. GreenfieldAbstract:The use of aspirin is widely recommended for the prevention of heart attacks owing to its ability to inhibit platelet activation by irreversibly blocking cyclooxygenase 1. However, aspirin also affects the fibrinolytic and hemostatic pathways by mechanisms that are not well understood, causing severe hemorrhagic complications. Here, we investigated the ability of aspirin and aspirin metabolites to inhibit thrombin-activatable fibrinolysis inhibitor (TAFI), the major inhibitor of plasma fibrinolysis. TAFI is activated via proteolytic cleavage by the thrombin-thrombomodulin complex to TAFIa, a carboxypeptidase B-like enzyme. TAFIa modulates fibrinolysis by removing the C-terminal arginine and lysine residues from partially degraded fibrin, which in turn inhibits the binding of plasminogen to fibrin clots. Aspirin and its major metabolites, salicylic Acid, gentisic Acid, and Salicyluric Acid, inhibit TAFIa carboxypeptidase activity. Salicyluric Acid effectively blocks activation of TAFI by thrombin-thrombomodulin; however, salicylates do not inhibit carboxypeptidase N or pancreatic carboxypeptidase B. Aspirin and other salicylates accelerated the dissolution of fibrin clots and reduced thrombus formation in an in vitro model of fibrinolysis. Inhibition of TAFI represents a novel hemostatic mechanism that contributes to aspirin’s therapy-associated antithrombotic activity and hemorrhagic complications.
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Alternative Mechanism of Aspirin in Anti-Thrombotic Therapy: Inhibition of Thrombin Activatable Fibrinolysis Inhibitor
2012Co-Authors: Seong Soo, Robert S. GreenfieldAbstract:The use of aspirin is widely recommended for the prevention of heart attacks owing to its ability to inhibit platelet activation by irreversibly blocking cyclooxygenase 1. However, aspirin also affects the fibrinolytic and hemostatic pathways by mechanisms that are not well understood, causing severe hemorrhagic complications. Here, we investigated the ability of aspirin and aspirin metabolites to inhibit thrombin-activatable fibrinolysis inhibitor (TAFI), the major inhibitor of plasma fibrinolysis. TAFI is activated via proteolytic cleavage by the thrombin-thrombomodulin complex to TAFIa, a carboxypeptidase B-like enzyme. TAFIa modulates fibrinolysis by removing the C-terminal arginine and lysine residues from partially degraded fibrin, which in turn inhibits the binding of plasminogen to fibrin clots. Aspirin and its major metabolites, salicylic Acid, gentisic Acid, and Salicyluric Acid, inhibit TAFIa carboxypeptidase activity. Salicyluric Acid effectively blocks activation of TAFI by thrombin-thrombomodulin; however, salicylates do not inhibit carboxypeptidase N or pancreatic carboxypeptidase B. Aspirin and other salicylates accelerated the dissolution of fibrin clots and reduced thrombus formation in an in vitro model of fibrinolysis. Inhibition of TAFI represents a novel hemostatic mechanism that contributes to aspirin’s therapy-associated antithrombotic activity and hemorrhagic complications. Key Words: Aspirin, Thrombin activatable fibrinolysis inhibitor (TAFI), Fibrinolysi
N. W. Davies - One of the best experts on this subject based on the ideXlab platform.
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Does Excretion of Secondary Metabolites Always Involve a Measurable Metabolic Cost? Fate of Plant Antifeedant Salicin in Common Brushtail Possum, Trichosurus vulpecula
Journal of Chemical Ecology, 2001Co-Authors: S. Mclean, G. J. Pass, W. J. Foley, S. Brandon, N. W. DaviesAbstract:Salicin was administered orally to six brushtail possums by incorporation in food for six days at three dose levels (0.05, 0.5, and 1.5% wet weight), giving mean ± SD daily intakes of 0.31 ± 0.09, 2.76 ± 0.75, and 6.04 ± 1.12 mmol salicin. Metabolites were identified by mass spectrometry and assayed by HPLC. Salicyl alcohol glucuronide accounted for 56–64% of urinary metabolites over the three doses, Salicyluric Acid 15–26%, salicin 10–18%, and there were smaller amounts of free (2–4%) and conjugated (0–6%) salicylic Acid. β,2-Dihydroxyphenylpropionic Acid was a minor metabolite. The hydrolysis of dietary salicin enabled reconjugation of its aglycone, salicyl alcohol, with a more polar sugar, glucuronic Acid, thus enhancing its renal excretion and resulting in little net loss of substrates for conjugation and a low measurable metabolic cost of excretion.
