Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue
Alzheimer’s disease (AD) is a devastating neurodegenerative disorder with no cure and no effective diagnostic criteria. The greatest challenge in effectively treating AD is identifying biomarkers specific for each patient when neurodegenerative processes have not yet begun, an outcome that would all...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-01-01
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| Series: | Brain Sciences |
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| Online Access: | https://www.mdpi.com/2076-3425/11/1/103 |
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| author | Filomena Iannuzzi Vincenza Frisardi Lucio Annunziato Carmela Matrone |
| author_facet | Filomena Iannuzzi Vincenza Frisardi Lucio Annunziato Carmela Matrone |
| author_sort | Filomena Iannuzzi |
| collection | DOAJ |
| description | Alzheimer’s disease (AD) is a devastating neurodegenerative disorder with no cure and no effective diagnostic criteria. The greatest challenge in effectively treating AD is identifying biomarkers specific for each patient when neurodegenerative processes have not yet begun, an outcome that would allow the design of a personalised therapeutic approach for each patient and the monitoring of the therapeutic response during the treatment. We found that the excessive phosphorylation of the amyloid precursor protein (APP) Tyr<sub>682</sub> residue on the APP <sub>682</sub>YENPTY<sub>687</sub> motif precedes amyloid β accumulation and leads to neuronal degeneration in AD neurons. We proved that Fyn tyrosine kinase elicits APP phosphorylation on Tyr<sub>682</sub> residue, and we reported increased levels of APP Tyr<sub>682</sub> and Fyn overactivation in AD neurons. Here, we want to contemplate the possibility of using fibroblasts as tools to assess APP Tyr<sub>682</sub> phosphorylation in AD patients, thus making the changes in APP Tyr<sub>682</sub> phosphorylation levels a potential diagnostic strategy to detect early pathological alterations present in the peripheral cells of AD patients’ AD brains. |
| first_indexed | 2024-03-09T04:51:56Z |
| format | Article |
| id | doaj.art-59246146f9764da9a3547cd7712e6723 |
| institution | Directory Open Access Journal |
| issn | 2076-3425 |
| language | English |
| last_indexed | 2024-03-09T04:51:56Z |
| publishDate | 2021-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Brain Sciences |
| spelling | doaj.art-59246146f9764da9a3547cd7712e67232023-12-03T13:10:14ZengMDPI AGBrain Sciences2076-34252021-01-0111110310.3390/brainsci11010103Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> ResidueFilomena Iannuzzi0Vincenza Frisardi1Lucio Annunziato2Carmela Matrone3Department of Biomedicine, University of Aarhus, Bartholins Allé, 8000 Aarhus, DenmarkGeriatric and Neuro Rehabilitation Department, Clinical Center for Nutrition in the Elderly, AUSL-IRCCS Reggio Emilia, Giovanni Amendola Street, 42122 Reggio Emilia, ItalySDN Research Institute Diagnostics and Nuclear (IRCCS SDN), Gianturco, 80131 Naples, ItalyDivision of Pharmacology, Department of Neuroscience, School of Medicine, University of Naples Federico II, 80131 Naples, ItalyAlzheimer’s disease (AD) is a devastating neurodegenerative disorder with no cure and no effective diagnostic criteria. The greatest challenge in effectively treating AD is identifying biomarkers specific for each patient when neurodegenerative processes have not yet begun, an outcome that would allow the design of a personalised therapeutic approach for each patient and the monitoring of the therapeutic response during the treatment. We found that the excessive phosphorylation of the amyloid precursor protein (APP) Tyr<sub>682</sub> residue on the APP <sub>682</sub>YENPTY<sub>687</sub> motif precedes amyloid β accumulation and leads to neuronal degeneration in AD neurons. We proved that Fyn tyrosine kinase elicits APP phosphorylation on Tyr<sub>682</sub> residue, and we reported increased levels of APP Tyr<sub>682</sub> and Fyn overactivation in AD neurons. Here, we want to contemplate the possibility of using fibroblasts as tools to assess APP Tyr<sub>682</sub> phosphorylation in AD patients, thus making the changes in APP Tyr<sub>682</sub> phosphorylation levels a potential diagnostic strategy to detect early pathological alterations present in the peripheral cells of AD patients’ AD brains.https://www.mdpi.com/2076-3425/11/1/103Alzheimer’s diseaseamyloid precursor proteinTyr682 residueYENPTY motifFyn tyrosine kinaseamyloid beta |
| spellingShingle | Filomena Iannuzzi Vincenza Frisardi Lucio Annunziato Carmela Matrone Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue Brain Sciences Alzheimer’s disease amyloid precursor protein Tyr682 residue YENPTY motif Fyn tyrosine kinase amyloid beta |
| title | Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue |
| title_full | Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue |
| title_fullStr | Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue |
| title_full_unstemmed | Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue |
| title_short | Might Fibroblasts from Patients with Alzheimer’s Disease Reflect the Brain Pathology? A Focus on the Increased Phosphorylation of Amyloid Precursor Protein Tyr<sub>682</sub> Residue |
| title_sort | might fibroblasts from patients with alzheimer s disease reflect the brain pathology a focus on the increased phosphorylation of amyloid precursor protein tyr sub 682 sub residue |
| topic | Alzheimer’s disease amyloid precursor protein Tyr682 residue YENPTY motif Fyn tyrosine kinase amyloid beta |
| url | https://www.mdpi.com/2076-3425/11/1/103 |
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