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Registros recuperados: 6
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A 43-kDa protein related to c-Erb A alpha1 is located in the mitochondrial matrix of rat liver Inra
Wrutniak, C.; Cassar-Malek, I.; Marchal, S.; Rascle, A.; Heusser, S.; Keller, J.M.; Fléchon, J.; Dauça, M.; Samarut, J.; Ghysdael, J.; Cabello, G..
Tipo: Journal Article Palavras-chave: RECEPTEUR NUCLEAIRE; ACTIVITE MITOCHONDRIALE; FOIE.
Ano: 1995 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB9600002381054657&uri=/notices/prodinra1/2010/09/
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Characterization of a novel thyroid hormone receptor alpha variant involved in the regulation of myoblast differentiation Inra
Casas, F.; Busson, M.; Grandemange, S.; Seyer, P.; Carazo, A.; Pessemesse, L.; Wrutniak-Cabello, C.; Cabello, G..
The regulation of gene expression by thyroid hormone (T-3) involves binding of the hormone to nuclear receptors [ thyroid hormone receptor (TR)] acting as T-3-dependent transcription factors encoded by TR alpha (NR1A1) and TR beta (NR1A2) genes. Several TR alpha variants have already been characterized, but only some of them display T-3 binding activity. In this study, we have identified another transcript, TR alpha-Delta E6, produced by alternative splicing with microexon 6b instead of exon 6. This splicing leads to the synthesis of a protein devoid of a hinge domain. The TR alpha-Delta E6 transcript is detected in all mouse tissues tested. Although TR alpha-Delta E6 did not bind DNA, its expression induced a TR alpha 1 sequestration in the cytoplasm....
Tipo: Journal Article Palavras-chave: TR ALPHA; MYOBLAST; TRANSCRIPTION; TRIIODOTHYRONINE.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007fe0b10ad&uri=/notices/prodinra1/2007/09/
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Is TR alpha an oncogene ? Overexpression of P43 induces human dermal fibroblast transformation Inra
Wrutniak-Cabello, C.; Grandemange, S.; Seyer, P.; Casas, F.; Cabello, G..
We have previously discovered p43, a truncated form of theTR alpha 1 nuclear receptor synthesized through the use of an internal AUG codon located in the TR alpha 1 transcript. P43 is a T3-dependent mitochondrial transcription factor leading to a stimulation of the organelle activity. We stably overexpressed p43 in human dermal fibroblasts. In parallel to a strong stimulation of mitochondrial activity correlated to an increase in ROS production, p43 overexpression induced strong morphological changes and cell fusion in myotubes-like structures associated with the expression of several muscle-specific genes (Myf5, desmin, connectin, myosin, AchR alpha). In addition, these cells displayed all the in vivo and in vitro features of cell transformation. This...
Tipo: Meeting Paper Palavras-chave: FIBROBLASTE; MITOCHONDRIE MUSCLE-SPECIFIC GENE; ONCOGENE; MITOCHONDRIAL ACTIVITY; ROS PRODUCTION.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007274b8125&uri=/notices/prodinra1/2008/09/
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Leptin downregulates heat shock protein-70 (HSP-70) gene expression in chicken liver and hypothalamus Inra
Figueiredo, D.; Gertler, A.; Cabello, G.; Decuypere, E.; Buyse, J.; Dridi, S..
Heat shock protein (HSP)-70 is expressed in normal and stressed cells but is highly stress-inducible. Although leptin has long been suggested to be involved in the regulation of stress response, its interaction with the HSP-70 gene is still unknown, under both unstressed and stressed conditions. The present study has aimed to investigate the effect of leptin on HSP-70 gene expression in normal chicken liver, hypothalamus, and muscle. Continuous infusion of recombinant chicken leptin (8 mu g/kg per hour) at a constant rate of 3 ml/h for 6 h in 3-week-old broiler chickens significantly (P < 0.05) decreased food intake and HSP-70 mRNA levels in liver and hypothalamus, but not in muscle. In an attempt to discriminate between the effect of leptin and of...
Tipo: Journal Article Palavras-chave: STRESS OXYDATIF; EXPRESSION GENIQUE; LEPTINE LEPTIN; HEAT SHOCK PROTEIN; FASTING; GENDER; OXIDATIVE STRESS; CHICKEN.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20077125ba1&uri=/notices/prodinra1/2008/01/
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Mitochondrial activity regulates myoblast differentiation by control of c-Myc expression Inra
Seyer, P.; Grandemange, S.; Busson, M.; Carazo, A.; Gamaléri, F.; Pessemesse, L.; Casas, F.; Cabello, G.; Wrutniak-Cabello, C..
We have previously shown that mitochondrial activity is an important regulator of myoblast differentiation, partly through processes targeting myogenin expression. Here, we investigated the possible involvement of c-myc in these processes. Inhibition of mitochondrial activity by chloramphenicol abrogated the decrease in c-myc mRNA and protein levels Occurring at the onset of terminal differentiation. Conversely, stimulation of mitochondrial activity by overexpression of the T3 mitochondrial receptor(p43) down-regulated c-myc expression. In addition, c-myc overexpression mimicked the influence of mitochondrial activity inhibition on myoblast differentiation. Moreover, like chloramphenicol, c-myc overexpression strongly inhibited the myogenic influence of...
Tipo: Journal Article Palavras-chave: MYOBLASTE; EXPRESSION GENIQUE; GENE c-Myc; DEVELOPPEMENT MUSCULAIRE CHICK-EMBRYO CELL; THYROID-HORMONE RECEPTOR; MYOGENIC DIFFERENTIATION; PROTEIN-SYNTHESIS; MESSENGER-RNA; RESPIRATION-DEFICIENT; MUSCLE DIFFERENTIATION; DNA.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200728f8a559&uri=/notices/prodinra1/2008/01/
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Myostatin regulation of muscle development: Molecular basis, natural mutations, physiopathological aspects Inra
Joulia-Ekaza, D.; Cabello, G..
Since its identification in 1997, myostatin has been considered as a novel and uniquenegative regulator of muscle growth, as mstn-/- mice display a dramatic and widespreadincrease in skeletal muscle mass. Myostatin also appears to be involved in musclehomeostasis in adults as its expression is regulated during muscle atrophy. Moreover,deletion of the myostatin gene seems to affect adipose tissue mass in addition to skeletalmuscle mass. Natural myostatin gene mutations occur in cattle breeds such as Belgian Blue,exhibiting an obviously increased muscle mass, but also in humans, as has recently beendemonstrated. Here we review these natural mutations and their associated phenotypes aswell as the physiological influence of the alterations in myostatin...
Tipo: Journal Article Palavras-chave: MYOSTATINE; MYOBLASTE; DEVELOPPEMENT MUSCULAIRE; APOPTOSE MYOSTATIN; MECHANISM; MUTATION; PHYSIOPATHOLOGY; MUSCLE DEVELOPMENT; MYOBLAST; GENE MUTATION; MUSCLE PATHOLOGY; CELL THERAPY; CELL SIGNALING.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200765cad115&uri=/notices/prodinra1/2008/01/
Registros recuperados: 6
Primeira ... 1 ... Última
 

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