Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 3
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Role of Integrin-Linked Kinase in Neuronal Cells OAK
Ishii, Toshiaki.
Integrin-linked kinase (ILK) is a focal adhesion serine/threonine protein kinase that binds to the cytoplasmic domain of β1 integrin and has an important role in integrin and growth factor signaling pathways. Clustering of integrins on the cell surface in contact with the extracellular matrix induces focal adhesion that recruits numerous mitogenic signaling proteins other than ILK, such as growth factor receptors, mitogenactivated protein kinase, and small GTP-binding proteins, to integrin receptors and forms signaling centers where adhesive and mitogenic pathways can integrate. ILK is highly expressed in neuronal cells and its enzyme activity is activated by cell adhesion on the extracellular matrix in a phosphatidylinositol 3-kinasedependent manner....
Palavras-chave: Integrin-linked kinase; Neurite; Tau; GSK-3β; Protein kinase B/Akt; P38 MAP kinase; PI3-kinase.
Ano: 2005 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/1458
Imagem não selecionada

Imprime registro no formato completo
Microtubule proteins and their post-translational forms in the cerebrospinal fluid of patients with paraparesis associated with HTLV-I infection and in SH-SY5Y cells: An in vitro model of HTLV-I-induced disease Biol. Res.
MALDONADO,HORACIO; ORTIZ-RIAÑO,EMILIO; KRAUSE,BERNARDO; BARRIGA,ANDRÉS; MEDINA,FERNANDO; PANDO,M ELSA; ALBERTI,CAROLINA; KETTLUN,ANA M; COLLADOS,LUCÍA; GARCÍA,LORENA; CARTIER,LUIS; VALENZUELA,M ANTONIETA.
HTLV-I-associated myelopathy/tropical spastic paraparesis (HAM/TSP) is characterized by axonal degeneration of the corticospinal tracts. The specific requirements for transport of proteins and organelles to the distal part of the long axon are crucial in the corticospinal tracts. Microtubule dysfunction could be involved in this disease, configuring an axonal transport disease. We measured tubulin and its post-translational modified forms (acetylated and tyrosinated) in CSF of patients and controls, as well as tau and its phosphorylated forms. There were no significant differences in the contents of tubulin and acetyl-tubulin between patients and controls; tyrosyl-tubulin was not detected. In HAM/TSP, tau levéis were significantly reduced, while the ratio...
Tipo: Journal article Palavras-chave: Tropical spastic paraparesis; Cerebrospinal fluid; SH-SY5Y cells; Retraction; Tau; Phosphorylated-tau forms; Tubulin; Acetyl-tubulin.
Ano: 2008 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300001
Imagem não selecionada

Imprime registro no formato completo
Changes in tau phosphorylation levels in the hippocampus and frontal cortex following chronic stress BJMBR
Yang,C.; Guo,X.; Wang,G.H.; Wang,H.L.; Liu,Z.C.; Liu,H.; Zhu,Z.X.; Li,Y..
Studies have indicated that early-life or early-onset depression is associated with a 2- to 4-fold increased risk of developing Alzheimers disease (AD). In AD, aggregation of an abnormally phosphorylated form of the tau protein may be a key pathological event. Tau is known to play a major role in promoting microtubule assembly and stabilization, and in maintaining the normal morphology of neurons. Several studies have reported that stress may induce tau phosphorylation. The main aim of the present study was to investigate possible alterations in the tau protein in the hippocampus and frontal cortex of 32 male Sprague-Dawley rats exposed to chronic unpredictable mild stress (CUMS) and then re-exposed to CUMS to mimic depression and the recurrence of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Alzheimers disease; Depression; Tau; Chronic unpredictable mild stress (CUMS); Re-exposure to CUMS; Fluoxetine.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2014000300237
Registros recuperados: 3
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional