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2024-11-12 Update From: SLTechnology News&Howtos shulou NAV: SLTechnology News&Howtos > IT Information >
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This article comes from the official account of Wechat: SF Chinese (ID:kexuejiaodian), author: SF
At present, nearly 50 million people worldwide suffer from dementia, of which about 2/3 are Alzheimer's disease. As the population ages, this number will continue to rise. With the current medical level, doctors do not have any effective treatment for Alzheimer's disease, and even with advanced brain imaging technology, it is difficult for doctors to make a 100% accurate diagnosis of Alzheimer's disease. even an autopsy is the only way to diagnose Alzheimer's disease. More worryingly, Alzheimer's disease may also be contagious.
Scientists have long found that if some proteins are misfolded, they will gather and eventually form amyloid plaques visible to the naked eye. This is prion.
This is an MRI image of the human brain. The white area indicated by the arrow in the picture is the location of prion accumulation. (photo Source: Qiu Yufeng) Prions are essentially proteins, first found in mammals, and are often associated with some neurodegenerative diseases, such as mad cow disease and Creutzfeldt-Jakob disease. According to the pathogenic mechanism, prions usually accumulate outside the brain nerve cells and have neurotoxicity, and the defense system in nerve cells has little effect on prions. To make matters worse, although prions are proteins and do not contain any nucleic acid components, they can replicate themselves as well as nucleic acids. This is one of the reasons why it is called a "virus"-viruses replicate themselves and are contagious, as do prions.
We already know that amyloid is a common protein in Alzheimer's disease and may be a key substance that causes Alzheimer's disease. Since prion amyloid plaques are contagious, can we boldly speculate that Alzheimer's disease can also be transmitted?
Is Alzheimer's disease contagious? In fact, scientists have long focused on this point. Researchers found beta-amyloid protein in the brains of eight people who died of Creutzfeldt-Jakob disease-usually found in the brains of people with Alzheimer's disease and similar to prion pathogenicity, according to a 2015 paper in the journal Nature. Moreover, these patients have been treated with auxin injection.
Through the comparative experiment, the researchers speculated that the auxin injection was mixed with β-amyloid protein, and 8 patients were infected by the injection. So, is it possible to say that Alzheimer's disease may be transmitted from one patient to another through beta-amyloid?
Some follow-up studies seem to support this speculation. In 2018, a team at University College London examined eight patients with amyloid angiopathy and found that they had undergone brain surgery in childhood or adolescence, all under the age of 60. It is not very common to have brain diseases caused by amyloid at this age. As a result, the team speculated that early brain surgery led to the transmission of amyloid to them, and that the instruments used in these operations had been used in patients with Alzheimer's disease.
The study supports the idea that Alzheimer's disease may be contagious, pointing out the possibility of iatrogenic transmission of Alzheimer's disease, but rejecting rumors that Alzheimer's disease may be transmitted from person to person. The team analyzed the evidence of "human-to-human" transmission of Alzheimer's disease over the past decade and found no evidence that Alzheimer's disease could be transmitted from person to person.
Cracking the code of protein folding is expected to cure Alzheimer's disease. β-amyloid protein has a prion-like pathogenic mechanism and infectivity, but also because of protein misfolding. Scientists have found that there is a "chaperone network" in cells. A "chaperone network" is a system of "chaperone molecules" that play a role in the folding of proteins and can identify misfolds and solve these "errors".
To that end, a team of researchers led by the University of Massachusetts Amherst edited the "companion network" in cells using gene editing techniques. They found that an enzyme in the endoplasmic reticulum, UGGT, places N-polysaccharides in specific positions of the protein that are misfolded. Experiments show that "chaperone molecules" can recognize N-polysaccharides, so as to determine the position of the wrong fold and correct the error in time.
Pre-amyloid protein is originally a transmembrane protein on the nerve cell membrane. The brains of people with Alzheimer's disease produce enzymes that cut preamyloid into small pieces. Beta amyloid is one of these small fragments, which accumulate outside nerve cells and may cause Alzheimer's disease. The study found the "code" for proteins to maintain their normal form, opening a new door to the treatment of neurodegenerative diseases such as Alzheimer's disease.
References:
Evidence for human transmission of amyloid- β pathology and cerebral amyloid angiopathy | Nature
Potential human transmission of amyloid β pathology: surveillance and risks-The Lancet Neurology
ER chaperones use a protein folding and quality control glyco-code: Molecular Cell
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