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	Provedor de dados BJMBR (4) Autor Borecký,J. (1) Cavalheiro,R.A. (1) Christoffolete,M.A. (1) Costa,A.D.T. (1) Faustinoni,V.C. (1) Fortes,F. (1) Jarmuszkiewicz,W. (1) Jezek,P. (1) Moriscot,A.S. (1) Schreiber,A.Z. (1) Sluse,F.E. (1) Vercesi,A.E. (1) Mais... Palavra-chave Uncoupling protein (4) Plant mitochondria (2) Alternative oxidase (1) Candida albicans spheroplasts (1) Chemical modification (1) Electron partitioning (1) Hypercaloric diet (1) Hypothyroidism (1) Mitochondria (1) Mitochondrial membrane potential (1) Mitochondrial swelling (1) Reconstitution (1) Regulation (1) Respiratory chain (1) Thyroid hormone (1) UCP3 (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Info:eu-repo/semantics/other (1) Ano 2004 (2) 2000 (2) País Brazil (4) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Activity and functional interaction of alternative oxidase and uncoupling protein in mitochondria from tomato fruit BJMBR Sluse,F.E.; Jarmuszkiewicz,W.. Cyanide-resistant alternative oxidase (AOX) is not limited to plant mitochondria and is widespread among several types of protists. The uncoupling protein (UCP) is much more widespread than previously believed, not only in tissues of higher animals but also in plants and in an amoeboid protozoan. The redox energy-dissipating pathway (AOX) and the proton electrochemical gradient energy-dissipating pathway (UCP) lead to the same final effect, i.e., a decrease in ATP synthesis and an increase in heat production. Studies with green tomato fruit mitochondria show that both proteins are present simultaneously in the membrane. This raises the question of a specific physiological role for each energy-dissipating system and of a possible functional connection... Tipo: Info:eu-repo/semantics/article Palavras-chave: Plant mitochondria; Alternative oxidase; Uncoupling protein; Regulation; Electron partitioning. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000300002 Hypercaloric cafeteria-like diet induced UCP3 gene expression in skeletal muscle is impaired by hypothyroidism BJMBR Christoffolete,M.A.; Moriscot,A.S.. The uncoupling protein UCP3 belongs to a family of mitochondrial carriers located in the inner mitochondrial membrane of certain cell types. It is expressed almost exclusively at high levels in skeletal muscle and its physiological role has not been fully determined in this tissue. In the present study we have addressed the possible interaction between a hypercaloric diet and thyroid hormone (T3), which are strong stimulators of UCP3 gene expression in skeletal muscle. Male Wistar rats weighing 180 ± 20 g were rendered hypothyroid by thyroidectomy and the addition of methimazole (0.05%; w/v) to drinking water after surgery. The rats were fed a hypercaloric cafeteria diet (68% carbohydrates, 13% protein and 18% lipids) for 10 days and sacrificed by... Tipo: Info:eu-repo/semantics/other Palavras-chave: Thyroid hormone; Hypothyroidism; Hypercaloric diet; Uncoupling protein; UCP3. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000600019 Important amino acid residues of potato plant uncoupling protein (StUCP) BJMBR Jezek,P.; Costa,A.D.T.; Vercesi,A.E.. Chemical modifications were used to identify some of the functionally important amino acid residues of the potato plant uncoupling protein (StUCP). The proton-dependent swelling of potato mitochondria in K+-acetate in the presence of linoleic acid and valinomycin was inhibited by mersalyl (Ki = 5 µM) and other hydrophilic SH reagents such as Thiolyte MB, iodoacetate and 5,5'-dithio-bis-(2-nitrobenzoate), but not by hydrophobic N-ethylmaleimide. This pattern of inhibition by SH reagents was similar to that of brown adipose tissue uncoupling protein (UCP1). As with UCP1, the arginine reagent 2,3-butadione, but not N-ethylmaleimide or other hydrophobic SH reagents, prevented the inhibition of StUCP-mediated transport by ATP in isolated potato mitochondria or... Tipo: Info:eu-repo/semantics/article Palavras-chave: Plant mitochondria; Uncoupling protein; Chemical modification; Mitochondrial swelling; Reconstitution. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001200003 Respiration, oxidative phosphorylation, and uncoupling protein in Candida albicans BJMBR Cavalheiro,R.A.; Fortes,F.; Borecký,J.; Faustinoni,V.C.; Schreiber,A.Z.. The respiration, membrane potential (<FONT FACE=Symbol>Dy</FONT>), and oxidative phosphorylation of mitochondria in situ were determined in spheroplasts obtained from Candida albicans control strain ATCC 90028 by lyticase treatment. Mitochondria in situ were able to phosphorylate externally added ADP (200 µM) in the presence of 0.05% BSA. Mitochondria in situ generated and sustained stable mitochondrial <FONT FACE=Symbol>Dy</FONT> respiring on 5 mM NAD-linked substrates, 5 mM succinate, or 100 µM N,N,N',N'-tetramethyl-p-phenylenediamine dihydrochloride plus 1 mM ascorbate. Rotenone (4 µM) inhibited respiration by 30% and 2 µM antimycin A or myxothiazole and 1 mM cyanide inhibited it by 85%. Cyanide-insensitive respiration was... Tipo: Info:eu-repo/semantics/article Palavras-chave: Candida albicans spheroplasts; Mitochondria; Respiratory chain; Mitochondrial membrane potential; Uncoupling protein. Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004001000003 Registros recuperados: 4 Primeira ... 1 ... Última

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