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Provedor de dados:  Biol. Res.
País:  Chile
Título:  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
Autores:  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
Data:  2008-01-01
Ano:  2008
Palavras-chave:  Tropical spastic paraparesis
Cerebrospinal fluid
SH-SY5Y cells
Retraction
Tau
Phosphorylated-tau forms
Tubulin
Acetyl-tubulin
Resumo:  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 of pT181/total tau was higher in patients than in controls, this being completely different from what is reported in other neurodegenerative diseases. Phosphorylation at T181 was also confirmed by Mass Spectrometry analysis. Western Blotting with monospecific polyclonal antibodies against pS199, pT205, pT231, pS262, pS356, pS396, pS404 and pS422 did not show differences in phosphorylation in these residues between patients and controls. Treating human SH-SY5Y neuroblastoma cells, a well-known in vitro neurite retraction model, with culture supernatant of MT-2 cells (HTLV-I infected cell line that secretes the viral Tax protein) we observed neurite retraction and an increase in tau phosphorylation at T181. A disruption of normal phosphorylation of tau protein in T181 could result in its dysfunction, contributing to axonal damage.
Tipo:  Journal article
Idioma:  Inglês
Identificador:  http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300001
Editor:  Sociedad de Biología de Chile
Formato:  text/html
Fonte:  Biological Research v.41 n.3 2008
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