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VEGF alleviates ALS-CSF induced cytoplasmic accumulations of TDP-43 and FUS/TLS in NSC-34 cells.
Shantanu, Shubham; Vijayalakshmi, K; Shruthi, S; Sagar, B K Chandrasekhar; Sathyaprabha, T N; Nalini, A; Raju, Trichur R; Alladi, Phalguni Anand.
Afiliación
  • Shantanu S; Department of Neurology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Vijayalakshmi K; Department of Neurophysiology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Shruthi S; Department of Neurophysiology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Sagar BKC; Department of Neuropathology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Sathyaprabha TN; Department of Neurophysiology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Nalini A; Department of Neurology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Raju TR; Department of Neurophysiology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India.
  • Alladi PA; Department of Neurophysiology, National Institute of Mental Health and Neuro Sciences, Hosur Road, Bangalore 560 029, India. Electronic address: alladiphalguni@gmail.com.
J Chem Neuroanat ; 81: 48-52, 2017 04.
Article en En | MEDLINE | ID: mdl-28163215
Cytoplasmic mislocalisation and aggregation of TDP-43 and FUS/TLS proteins in spinal motor neurons contribute to the pathogenesis of the highly fatal disorder amyotrophic lateral sclerosis (ALS). We investigated the neuroprotective effect of VEGF on expression of these proteins in the motor neuronal cell line NSC-34 modelled to reminisce sporadic form of ALS. We studied the expression of TDP-43 and FUS/TLS proteins after exposure to ALS-CSF and following VEGF supplementation by quantitative confocal microscopy and electron microscopy. ALS-CSF caused cytoplasmic overexpression of both the proteins and stress-granule formation in the cells. These alterations were alleviated by VEGF supplementation. The related ultrastructural changes like nuclear membrane dysmorphism and p-bodies associated changes were also reversed. However the protein expression did not completely translocate to the nucleus, as some cells continued to show to cytoplasmic mislocalisation. Thus, the present findings indicate that VEGF alleviates TDP43 and FUS pathology by complimenting its role in controlling apoptosis and reversing choline acetyl transferase expression. Hence, VEGF appears to target multiple pathogenic processes in the neurodegenerative cascade of ALS.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoplasma / Proteína FUS de Unión a ARN / Factor A de Crecimiento Endotelial Vascular / Proteínas de Unión al ADN / Esclerosis Amiotrófica Lateral Tipo de estudio: Prognostic_studies Límite: Adult / Female / Humans / Male / Middle aged Idioma: En Revista: J Chem Neuroanat Asunto de la revista: ANATOMIA / NEUROLOGIA / QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: India Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoplasma / Proteína FUS de Unión a ARN / Factor A de Crecimiento Endotelial Vascular / Proteínas de Unión al ADN / Esclerosis Amiotrófica Lateral Tipo de estudio: Prognostic_studies Límite: Adult / Female / Humans / Male / Middle aged Idioma: En Revista: J Chem Neuroanat Asunto de la revista: ANATOMIA / NEUROLOGIA / QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: India Pais de publicación: Países Bajos