The Experts below are selected from a list of 18 Experts worldwide ranked by ideXlab platform
Paulo Flavio Silveira - One of the best experts on this subject based on the ideXlab platform.
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Prolyl‚ Cystyl and pyroglutamyl peptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
Peptides, 2007Co-Authors: Leonardo Zambotti-villela, Cristiane Murena-nunes, Simone Cristina Yamasaki, Joyce S. Villarroel, Paulo Flavio SilveiraAbstract:Prolyl, Cystyl and pyroglutamyl peptidases are emerging targets for diabetes and cognitive deficit therapies. The present study is focused on the influence of diabetes mellitus induced by streptozotocin on levels of representative hydrolytic activities of these enzymes in the rat hypothalamus and hippocampus. Streptozotocin-diabetic rats presented about 348 mg glucose/dL blood, and a slightly increased hematocrit and plasma osmolality. The activities of soluble and membrane-bound dipeptidyl-peptidase IV, and soluble Cystyl Aminopeptidase did not differ between diabetic and control rats in both brain areas. Hippocampal soluble prolyl oligopeptidase presented similar activities between diabetic and controls. Increased activities in diabetics were observed for soluble prolyl oligopeptidase (1.78-fold) and membrane-bound Cystyl Aminopeptidase (2.55-fold) in the hypothalamus, and for membrane-bound Cystyl Aminopeptidase (5.14-fold) in the hippocampus. In both brain areas, the activities of membrane-bound and soluble pyroglutamyl Aminopeptidase were slightly lower (
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Cystyl Aminopeptidase activity in the plasma, viscera and brain of the snake Bothrops jararaca.
Comparative biochemistry and physiology. Part A Molecular & integrative physiology, 2005Co-Authors: Rafaela Fadoni Alponti, Leonardo Zambotti-villela, Cristiane Murena-nunes, Camila Eduardo Marinho, Renata Do Amaral Olivo, Paulo Flavio SilveiraAbstract:The relationship between plasma osmolality and Cystyl Aminopeptidase was characterized in the snake Bothrops jararaca and comparisons were made with the emerging picture of this relationship in rats. The profile of Cystyl Aminopeptidase activity under basal conditions was determined in the soluble and membrane-bound forms in visceral organs and in the central nervous system in comparison with that of alanyl Aminopeptidase. The regional localization of Cystyl and alanyl Aminopeptidase activities was studied in the central nervous system. The basal level of plasma Cystyl Aminopeptidase, four- to six-fold higher than in rats, suggests its importance to help regulate circulating levels of neurohypophysial peptides in B. jararaca snake. The osmotic sensitivity of this plasma enzyme, undetectable in male, but about three-fold higher in female snakes than in rats, reveals a sexual dimorphism. In marked contrast to those observed in rats, low levels of soluble and particulate forms in the kidney indicate that Cystyl Aminopeptidase plays a minor metabolizing role at this anatomical location in B. jararaca. Despite of the regional-specific divergence between the levels of rat and snake enzymes, the bilaterally symmetric pattern of the diencephalic distribution of alanyl Aminopeptidase reflects functional homologies between these two distantly related species.
Leonardo Zambotti-villela - One of the best experts on this subject based on the ideXlab platform.
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Prolyl‚ Cystyl and pyroglutamyl peptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
Peptides, 2007Co-Authors: Leonardo Zambotti-villela, Cristiane Murena-nunes, Simone Cristina Yamasaki, Joyce S. Villarroel, Paulo Flavio SilveiraAbstract:Prolyl, Cystyl and pyroglutamyl peptidases are emerging targets for diabetes and cognitive deficit therapies. The present study is focused on the influence of diabetes mellitus induced by streptozotocin on levels of representative hydrolytic activities of these enzymes in the rat hypothalamus and hippocampus. Streptozotocin-diabetic rats presented about 348 mg glucose/dL blood, and a slightly increased hematocrit and plasma osmolality. The activities of soluble and membrane-bound dipeptidyl-peptidase IV, and soluble Cystyl Aminopeptidase did not differ between diabetic and control rats in both brain areas. Hippocampal soluble prolyl oligopeptidase presented similar activities between diabetic and controls. Increased activities in diabetics were observed for soluble prolyl oligopeptidase (1.78-fold) and membrane-bound Cystyl Aminopeptidase (2.55-fold) in the hypothalamus, and for membrane-bound Cystyl Aminopeptidase (5.14-fold) in the hippocampus. In both brain areas, the activities of membrane-bound and soluble pyroglutamyl Aminopeptidase were slightly lower (
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Cystyl Aminopeptidase activity in the plasma, viscera and brain of the snake Bothrops jararaca.
Comparative biochemistry and physiology. Part A Molecular & integrative physiology, 2005Co-Authors: Rafaela Fadoni Alponti, Leonardo Zambotti-villela, Cristiane Murena-nunes, Camila Eduardo Marinho, Renata Do Amaral Olivo, Paulo Flavio SilveiraAbstract:The relationship between plasma osmolality and Cystyl Aminopeptidase was characterized in the snake Bothrops jararaca and comparisons were made with the emerging picture of this relationship in rats. The profile of Cystyl Aminopeptidase activity under basal conditions was determined in the soluble and membrane-bound forms in visceral organs and in the central nervous system in comparison with that of alanyl Aminopeptidase. The regional localization of Cystyl and alanyl Aminopeptidase activities was studied in the central nervous system. The basal level of plasma Cystyl Aminopeptidase, four- to six-fold higher than in rats, suggests its importance to help regulate circulating levels of neurohypophysial peptides in B. jararaca snake. The osmotic sensitivity of this plasma enzyme, undetectable in male, but about three-fold higher in female snakes than in rats, reveals a sexual dimorphism. In marked contrast to those observed in rats, low levels of soluble and particulate forms in the kidney indicate that Cystyl Aminopeptidase plays a minor metabolizing role at this anatomical location in B. jararaca. Despite of the regional-specific divergence between the levels of rat and snake enzymes, the bilaterally symmetric pattern of the diencephalic distribution of alanyl Aminopeptidase reflects functional homologies between these two distantly related species.
Cristiane Murena-nunes - One of the best experts on this subject based on the ideXlab platform.
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Prolyl‚ Cystyl and pyroglutamyl peptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
Peptides, 2007Co-Authors: Leonardo Zambotti-villela, Cristiane Murena-nunes, Simone Cristina Yamasaki, Joyce S. Villarroel, Paulo Flavio SilveiraAbstract:Prolyl, Cystyl and pyroglutamyl peptidases are emerging targets for diabetes and cognitive deficit therapies. The present study is focused on the influence of diabetes mellitus induced by streptozotocin on levels of representative hydrolytic activities of these enzymes in the rat hypothalamus and hippocampus. Streptozotocin-diabetic rats presented about 348 mg glucose/dL blood, and a slightly increased hematocrit and plasma osmolality. The activities of soluble and membrane-bound dipeptidyl-peptidase IV, and soluble Cystyl Aminopeptidase did not differ between diabetic and control rats in both brain areas. Hippocampal soluble prolyl oligopeptidase presented similar activities between diabetic and controls. Increased activities in diabetics were observed for soluble prolyl oligopeptidase (1.78-fold) and membrane-bound Cystyl Aminopeptidase (2.55-fold) in the hypothalamus, and for membrane-bound Cystyl Aminopeptidase (5.14-fold) in the hippocampus. In both brain areas, the activities of membrane-bound and soluble pyroglutamyl Aminopeptidase were slightly lower (
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Cystyl Aminopeptidase activity in the plasma, viscera and brain of the snake Bothrops jararaca.
Comparative biochemistry and physiology. Part A Molecular & integrative physiology, 2005Co-Authors: Rafaela Fadoni Alponti, Leonardo Zambotti-villela, Cristiane Murena-nunes, Camila Eduardo Marinho, Renata Do Amaral Olivo, Paulo Flavio SilveiraAbstract:The relationship between plasma osmolality and Cystyl Aminopeptidase was characterized in the snake Bothrops jararaca and comparisons were made with the emerging picture of this relationship in rats. The profile of Cystyl Aminopeptidase activity under basal conditions was determined in the soluble and membrane-bound forms in visceral organs and in the central nervous system in comparison with that of alanyl Aminopeptidase. The regional localization of Cystyl and alanyl Aminopeptidase activities was studied in the central nervous system. The basal level of plasma Cystyl Aminopeptidase, four- to six-fold higher than in rats, suggests its importance to help regulate circulating levels of neurohypophysial peptides in B. jararaca snake. The osmotic sensitivity of this plasma enzyme, undetectable in male, but about three-fold higher in female snakes than in rats, reveals a sexual dimorphism. In marked contrast to those observed in rats, low levels of soluble and particulate forms in the kidney indicate that Cystyl Aminopeptidase plays a minor metabolizing role at this anatomical location in B. jararaca. Despite of the regional-specific divergence between the levels of rat and snake enzymes, the bilaterally symmetric pattern of the diencephalic distribution of alanyl Aminopeptidase reflects functional homologies between these two distantly related species.
Simone Cristina Yamasaki - One of the best experts on this subject based on the ideXlab platform.
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Prolyl‚ Cystyl and pyroglutamyl peptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
Peptides, 2007Co-Authors: Leonardo Zambotti-villela, Cristiane Murena-nunes, Simone Cristina Yamasaki, Joyce S. Villarroel, Paulo Flavio SilveiraAbstract:Prolyl, Cystyl and pyroglutamyl peptidases are emerging targets for diabetes and cognitive deficit therapies. The present study is focused on the influence of diabetes mellitus induced by streptozotocin on levels of representative hydrolytic activities of these enzymes in the rat hypothalamus and hippocampus. Streptozotocin-diabetic rats presented about 348 mg glucose/dL blood, and a slightly increased hematocrit and plasma osmolality. The activities of soluble and membrane-bound dipeptidyl-peptidase IV, and soluble Cystyl Aminopeptidase did not differ between diabetic and control rats in both brain areas. Hippocampal soluble prolyl oligopeptidase presented similar activities between diabetic and controls. Increased activities in diabetics were observed for soluble prolyl oligopeptidase (1.78-fold) and membrane-bound Cystyl Aminopeptidase (2.55-fold) in the hypothalamus, and for membrane-bound Cystyl Aminopeptidase (5.14-fold) in the hippocampus. In both brain areas, the activities of membrane-bound and soluble pyroglutamyl Aminopeptidase were slightly lower (
Joyce S. Villarroel - One of the best experts on this subject based on the ideXlab platform.
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Prolyl‚ Cystyl and pyroglutamyl peptidase activities in the hippocampus and hypothalamus of streptozotocin-induced diabetic rats
Peptides, 2007Co-Authors: Leonardo Zambotti-villela, Cristiane Murena-nunes, Simone Cristina Yamasaki, Joyce S. Villarroel, Paulo Flavio SilveiraAbstract:Prolyl, Cystyl and pyroglutamyl peptidases are emerging targets for diabetes and cognitive deficit therapies. The present study is focused on the influence of diabetes mellitus induced by streptozotocin on levels of representative hydrolytic activities of these enzymes in the rat hypothalamus and hippocampus. Streptozotocin-diabetic rats presented about 348 mg glucose/dL blood, and a slightly increased hematocrit and plasma osmolality. The activities of soluble and membrane-bound dipeptidyl-peptidase IV, and soluble Cystyl Aminopeptidase did not differ between diabetic and control rats in both brain areas. Hippocampal soluble prolyl oligopeptidase presented similar activities between diabetic and controls. Increased activities in diabetics were observed for soluble prolyl oligopeptidase (1.78-fold) and membrane-bound Cystyl Aminopeptidase (2.55-fold) in the hypothalamus, and for membrane-bound Cystyl Aminopeptidase (5.14-fold) in the hippocampus. In both brain areas, the activities of membrane-bound and soluble pyroglutamyl Aminopeptidase were slightly lower (
