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Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau

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dc.contributor Ministerio de Educación y Ciencia (España)
dc.contributor Comunidad de Madrid
dc.contributor Fundación Botín
dc.contributor Fundación Ramón Areces
dc.creator Santa María, Ismael
dc.creator Hernández Pérez, Félix
dc.creator Río, Joaquín del
dc.creator Moreno Muñoz, Francisco José
dc.creator Ávila, Jesús
dc.date 2008-03-31T12:45:19Z
dc.date 2008-03-31T12:45:19Z
dc.date 2007-09-06
dc.date.accessioned 2017-01-31T01:01:23Z
dc.date.available 2017-01-31T01:01:23Z
dc.identifier Mol Neurodegener. 2007; 2: 17
dc.identifier 1750-1326
dc.identifier http://hdl.handle.net/10261/3392
dc.identifier 10.1186/1750-1326-2-17
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3392
dc.description This article is available from: http://www.molecularneurodegeneration.com/content/2/1/17
dc.description Alzheimer's disease (AD) is characterized by the presence of two histopathological hallmarks; the senile plaques, or extracellular deposits mainly composed of amyloid-β peptide (Aβ), and the neurofibrillary tangles, or intraneuronal inclusions composed of hyperphosphorylated tau protein. Since Aβ aggregates are found in the pathological cases, several strategies are under way to develop drugs that interact with Aβ to reduce its assembly. One of them is 3-amino-1-propane sulfonic acid (Tramiprosate, 3-APS, Alzhemed™), that was developed as a sulfated glycosaminoglycan mimetic, that could interact with Aβ peptide, preventing its aggregation. However, little is known about the action of 3-APS on tau protein aggregation. In this work, we have tested the action of 3-APS on cell viability, microtubule network, actin organization and tau aggregation. Our results indicate that 3-APS favours tau aggregation, in tau transfected non-neuronal cells, and in neuronal cells. We also found that 3-APS does not affect the binding of tau to microtubules but may prevent the formation of tau-actin aggregates. We like to emphasize the importance of testing on both types of pathology (amyloid and tau) the potential drugs to be used for AD treatment.
dc.description This work was supported by grants froom Plan Nacional (Ministerio de Educación y Ciencia, Spain), Comunidad de Madrid, Fundación Botin, and by an Institucional Grant of Fundación R. Areces. Also, this work is part to our contribution to CIBER Enfermedades Neurodegenerativas (CIBERNED) (Ministerio de Sanidad y Consumo).
dc.description Peer reviewed
dc.format 700762 bytes
dc.format 425087 bytes
dc.format application/pdf
dc.format application/pdf
dc.language eng
dc.publisher BioMed Central
dc.relation Publisher’s version
dc.rights openAccess
dc.title Tramiprosate, a drug of potential interest for the treatment of Alzheimer's disease, promotes an abnormal aggregation of tau
dc.type Artículo


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