scholarly journals Molecular alterations of protein tau in the cingulate cortex of human brain with Alzheimer’s disease

2020 ◽  
Vol 16 (S2) ◽  
Author(s):  
Ricardo Apatiga‐Perez ◽  
Fidel De la Cruz ◽  
Linda Garcés‐Ramírez ◽  
Mario Hernandes‐Alejandro ◽  
Miguel Ángel Ontiveros‐Torres ◽  
...  
2004 ◽  
Vol 36 (05) ◽  
Author(s):  
L Weller ◽  
F Faltraco ◽  
E Heimberg ◽  
S Teipel ◽  
B Bondy ◽  
...  

2021 ◽  
pp. 1-14
Author(s):  
Pan Liu ◽  
Qian Yang ◽  
Ning Yu ◽  
Yan Cao ◽  
Xue Wang ◽  
...  

Background: Alzheimer’s disease (AD) is one of the most challenging diseases causing an increasing burden worldwide. Although the neuropathologic diagnosis of AD has been established for many years, the metabolic changes in neuropathologic diagnosed AD samples have not been fully investigated. Objective: To elucidate the potential metabolism dysregulation in the postmortem human brain samples assessed by AD related pathological examination. Methods: We performed untargeted and targeted metabolomics in 44 postmortem human brain tissues. The metabolic differences in the hippocampus between AD group and control (NC) group were compared. Results: The results show that a pervasive metabolic dysregulation including phenylalanine metabolism, valine, leucine, and isoleucine biosynthesis, biotin metabolism, and purine metabolism are associated with AD pathology. Targeted metabolomics reveal that phenylalanine, phenylpyruvic acid, and N-acetyl-L-phenylalanine are upregulated in AD samples. In addition, the enzyme IL-4I1 catalyzing transformation from phenylalanine to phenylpyruvic acid is also upregulated in AD samples. Conclusion: There is a pervasive metabolic dysregulation in hippocampus with AD-related pathological changes. Our study suggests that the dysregulation of phenylalanine metabolism in hippocampus may be an important pathogenesis for AD pathology formation.


Genetics ◽  
2003 ◽  
Vol 165 (3) ◽  
pp. 1233-1242
Author(s):  
Joshua M Shulman ◽  
Mel B Feany

Abstract In Alzheimer's disease and related disorders, the microtubule-associated protein Tau is abnormally hyperphosphorylated and aggregated into neurofibrillary tangles. Mutations in the tau gene cause familial frontotemporal dementia. To investigate the molecular mechanisms responsible for Tau-induced neurodegeneration, we conducted a genetic modifier screen in a Drosophila model of tauopathy. Kinases and phosphatases comprised the major class of modifiers recovered, and several candidate Tau kinases were similarly shown to enhance Tau toxicity in vivo. Despite some clinical and pathological similarities among neurodegenerative disorders, a direct comparison of modifiers between different Drosophila disease models revealed that the genetic pathways controlling Tau and polyglutamine toxicity are largely distinct. Our results demonstrate that kinases and phosphatases control Tau-induced neurodegeneration and have important implications for the development of therapies in Alzheimer's disease and related disorders.


2017 ◽  
Vol 13 (7S_Part_2) ◽  
pp. P112-P113
Author(s):  
Joseph Therriault ◽  
Tharick A. Pascoal ◽  
Kok Pin Ng ◽  
Sulantha S. Mathotaarachchi ◽  
Min Su Kang ◽  
...  

2008 ◽  
Vol 4 ◽  
pp. T633-T634
Author(s):  
Ivica Granic ◽  
Csaba Nyakas ◽  
Gabor G. Kovacs ◽  
Paul G.M. Luiten ◽  
Ulrich L.M. Eisel

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