Alzheimer’s disease patients how to prolong life? “Power plants” mitochondria to hide the answer

alzheimer’s disease (AD) denied the right to human natural aging, in the process of destination to press the fast forward button. Cognitive problems, memory function worsening gradually lost, these have greatly affected the group’s health and daily life. International association of alzheimer’s disease, according to the current more than 47 million people worldwide suffer from alzheimer’s disease, and the future will be more severe situation.

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and the disease difficult is that its molecular mechanisms and effective treatment method has still poorly understood. Alzheimer’s disease as a process of neurodegenerative diseases, the scientific community is recognized as a main characteristic is & beta; – amyloid protein in the brain, now a lot of experimental research is mainly focused on eliminating the brain & beta; – amyloid protein aggregation.

however, lausanne, Switzerland, the federal institute of technology, energy metabolism, director of the laboratory, one of the pioneers in the field of nuclear receptor signal transduction Johan Auwerx professor and his colleagues tried to from another path to indirect control & beta; – amyloid protein aggregation.

team the latest research results on December 7th in the morning, published in the international academic journal “Nature” (Nature), is put forward to improve mitochondrial protein steady-state & beta on alzheimer’s disease, etc; – amyloid protein disease is good, can reduce & beta; – starch protein aggregation. Research team believes that perhaps for the treatment of alzheimer’s disease provides a new target, extend the service life of patients with alzheimer’s disease can be a potential way.

Auwerx people think, such as alzheimer’s disease is a complex, many factors lead to disease. In addition to & beta; – amyloid protein aggregation, mitochondrial dysfunction after has proved to be one of the common pathological features. The abnormal mitochondria mainly includes the mitochondrial respiratory chain and activity and mitochondrial morphology change, etc.

it is important to note that mitochondria play a normal physiology function support requires a lot of protein, its premise protein is a set of strict quality control system. Two major control way is not folded proteins reaction (UPRmt) and mitochondria autophagy. But the pathogenesis of alzheimer’s disease and mitochondrial protein correlation between steady state, there is still not very clear.

the team through the experimental results show that in c. elegans and human & beta; – amyloid protein aggregation will induce mitochondrial protein folding reaction and mitochondrial autophagy. Although the molecular mechanism of the induced is unclear, but the experiment group according to the results of the study speculated that this involves the function of the basic, conservative process. And they folded protein, for example, reaction related to mitochondrial protein transport in & beta; – toxicity of amyloid protein was destroyed under pressure. The team on the analysis of the alzheimer’s patients also showed that the mitochondrial protein function is inhibited.

the team also put forward evidence that mitochondria in & beta; – an obvious effect in the pathogenesis of amyloid protein disease. C. elegans, for example, in the stress state of mitochondrial function to maintain and not folded proteins reaction is mainly composed of mitochondria and related atfs – 1 the activation of transcription factors, the team through the atfs – 1 consumption to reduce the steady-state makes mitochondria GMC101 c. elegans deterioration of disease characteristics. Instead, by not folding proteins reaction and mitochondria autophagy both ways to improve the steady state will reduce mitochondrial proteins gathered themselves together, and the restoration of c. elegans comfort and slow disease progression, and eventually to prolong life.

in the same way, the team also found in the anthropogenic neurons SH – SY5Y, mitochondrial translation inhibitors DOX and vitamin B3 a derivatives, niacinamide RNA NR can reduce & beta; – amyloid protein aggregation. DOX, NR can induce mitochondrial protein folding reactions and mitochondrial autophagy.

APPSwe/PSEN1dE9NR with alzheimer’s mice, NR therapy has been shown to reduce amyloid plaques in the brain to form, and can improve memory in mice.

are presented in the paper, the research data show that the toxicity of protein such as alzheimer’s disease, improve mitochondrial function and the steady-state might reduce the formation of harmful protein aggregation.

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