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Secretomic changes of amyloid beta peptides on Alzheimer's disease related proteins in differentiated human SH-SY5Y neuroblastoma cells.
Roytrakul, Sittiruk; Jaresitthikunchai, Janthima; Phaonakrop, Narumon; Charoenlappanit, Sawanya; Thaisakun, Siriwan; Kumsri, Nitithorn; Arpornsuwan, Teerakul.
Afiliación
  • Roytrakul S; Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, Thailand.
  • Jaresitthikunchai J; Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, Thailand.
  • Phaonakrop N; Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, Thailand.
  • Charoenlappanit S; Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, Thailand.
  • Thaisakun S; Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, Thailand.
  • Kumsri N; Undergraduate Student of Department of Medical Technology, Faculty of Allied Health Sciences, Thammasat University, Pathumtani, Thailand.
  • Arpornsuwan T; Medical Technology Research and Service Unit, Health Care Service Center, Faculty of Allied Health Sciences, Thammasat University, Pathumthani, Thailand.
PeerJ ; 12: e17732, 2024.
Article en En | MEDLINE | ID: mdl-39035166
ABSTRACT
Alzheimer's disease (AD) is a neurodegenerative disease that causes physical damage to neuronal connections, leading to brain atrophy. This disruption of synaptic connections results in mild to severe cognitive impairments. Unfortunately, no effective treatment is currently known to prevent or reverse the symptoms of AD. The aim of this study was to investigate the effects of three synthetic peptides, i.e., KLVFF, RGKLVFFGR and RIIGL, on an AD in vitro model represented by differentiated SH-SY5Y neuroblastoma cells exposed to retinoic acid (RA) and brain-derived neurotrophic factor (BDNF). The results demonstrated that RIIGL peptide had the least significant cytotoxic activity to normal SH-SY5Y while exerting high cytotoxicity against the differentiated cells. The mechanism of RIIGL peptide in the differentiated SH-SY5Y was investigated based on changes in secretory proteins compared to another two peptides. A total of 380 proteins were identified, and five of them were significantly detected after treatment with RIIGL peptide. These secretory proteins were found to be related to microtubule-associated protein tau (MAPT) and amyloid-beta precursor protein (APP). RIIGL peptide acts on differentiated SH-SY5Y by regulating amyloid-beta formation, neuron apoptotic process, ceramide catabolic process, and oxidative phosphorylation and thus has the potentials to treat AD.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Diferenciación Celular / Péptidos beta-Amiloides / Proteínas tau / Factor Neurotrófico Derivado del Encéfalo / Enfermedad de Alzheimer / Neuroblastoma Límite: Humans Idioma: En Revista: PeerJ Año: 2024 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Diferenciación Celular / Péptidos beta-Amiloides / Proteínas tau / Factor Neurotrófico Derivado del Encéfalo / Enfermedad de Alzheimer / Neuroblastoma Límite: Humans Idioma: En Revista: PeerJ Año: 2024 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Estados Unidos