Redox regulation, protein S-nitrosylation, and synapse loss in Alzheimer's and related dementias

被引:2
作者
Oh, Chang-ki [1 ,2 ]
Nakamura, Tomohiro [1 ,2 ]
Zhang, Xu [1 ,2 ]
Lipton, Stuart A. [1 ,2 ,3 ]
机构
[1] Scripps Res Inst, Neurodegenerat New Med Ctr, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Dept Mol Med, La Jolla, CA 92037 USA
[3] Univ Calif San Diego, Sch Med, Dept Neurosci, La Jolla, CA 92093 USA
关键词
NITRIC-OXIDE SYNTHASE; UBIQUITIN-PROTEASOME SYSTEM; NMDA RECEPTOR ACTIVATION; NEURONAL CELL-DEATH; OXIDATIVE STRESS; MITOCHONDRIAL DYSFUNCTION; DISULFIDE-ISOMERASE; PARKINSONS-DISEASE; SIGNALING PATHWAY; AMYLOID-BETA;
D O I
10.1016/j.neuron.2024.10.013
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Redox-mediated posttranslational modification, as exemplified by protein S-nitrosylation, modulates protein activity and function in both health and disease. Here, we review recent findings that show how normal aging, infection/inflammation, trauma, environmental toxins, and diseases associated with protein aggregation can each trigger excessive nitrosative stress, resulting in aberrant protein S-nitrosylation and hence dysfunctional protein networks. These redox reactions contribute to the etiology of multiple neurodegenerative disorders as well as systemic diseases. In the CNS, aberrant S-nitrosylation reactions of single proteins or, in many cases, interconnected networks of proteins lead to dysfunctional pathways affecting endoplasmic rescriptional and enzymatic machinery, and mitochondrial metabolism. Aberrant protein S-nitrosylation and transnitrosylation (transfer of nitric oxide [NO]-related species from one protein to another) trigger protein aggregation, neuronal bioenergetic compromise, and microglial phagocytosis, all of which contribute to the synapse loss that underlies cognitive decline in Alzheimer's disease and related dementias.
引用
收藏
页码:3823 / 3850
页数:28
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