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
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 dysfunc...
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| Lenguaje: | English |
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Sociedad de Biología de Chile
2008
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oai:scielo:S0716-976020080003000012009-04-23Microtubule 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 diseaseMALDONADO,HORACIOORTIZ-RIAÑO,EMILIOKRAUSE,BERNARDOBARRIGA,ANDRÉSMEDINA,FERNANDOPANDO,M ELSAALBERTI,CAROLINAKETTLUN,ANA MCOLLADOS,LUCÍAGARCÍA,LORENACARTIER,LUISVALENZUELA,M ANTONIETA Tropical spastic paraparesis cerebrospinal fluid SH-SY5Y cells retraction tau phosphorylated-tau forms tubulin acetyl-tubulin 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.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.41 n.3 20082008-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300001en10.4067/S0716-97602008000300001 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
Tropical spastic paraparesis cerebrospinal fluid SH-SY5Y cells retraction tau phosphorylated-tau forms tubulin acetyl-tubulin |
| spellingShingle |
Tropical spastic paraparesis cerebrospinal fluid SH-SY5Y cells retraction tau phosphorylated-tau forms tubulin acetyl-tubulin 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 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 |
| description |
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. |
| author |
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 |
| author_facet |
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 |
| author_sort |
MALDONADO,HORACIO |
| title |
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 |
| title_short |
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 |
| title_full |
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 |
| title_fullStr |
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 |
| title_full_unstemmed |
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 |
| title_sort |
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 |
| publisher |
Sociedad de Biología de Chile |
| publishDate |
2008 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000300001 |
| work_keys_str_mv |
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