-
Categories
-
Pharmaceutical Intermediates
-
Active Pharmaceutical Ingredients
-
Food Additives
- Industrial Coatings
- Agrochemicals
- Dyes and Pigments
- Surfactant
- Flavors and Fragrances
- Chemical Reagents
- Catalyst and Auxiliary
- Natural Products
- Inorganic Chemistry
-
Organic Chemistry
-
Biochemical Engineering
- Analytical Chemistry
-
Cosmetic Ingredient
- Water Treatment Chemical
-
Pharmaceutical Intermediates
Promotion
ECHEMI Mall
Wholesale
Weekly Price
Exhibition
News
-
Trade Service
Prion disease is a rare progressive neurodegenerative disease that affects humans and animals
.
They are related to the formation of prion protein (PrP) aggregates
Their research results were published in the journal "Science Advances" entitled " Endosomal sorting drives the formation of axonal prion protein endoggresomes "
.
Axons are very thin nerve fibers that are responsible for transmitting nerve impulses from one neuron to another
.
Axon loss is an early sign of neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease
In this study, the researchers used mouse brain cells containing mutant PrP and film technology under the microscope to study the initial accumulation of PrP in axons
.
The researchers observed that the mutant PrP produced in somatic cells is surrounded by vesicles that enter axons along orbits called microtubules
The researchers observed that this movement pushes most of the PrP into the axons, where the vesicles containing PrP gather and merge
.
The mutant PrP formed huge aggregates-Dr.
Encalada explained: "We hope these findings will lead to a better understanding of prions and other neurodegenerative diseases, and new strategies to treat them
.
"
The researchers also discovered a complex of key proteins, which is responsible for guiding PrP to axons and causing axon swelling-related aggregation
This discovery gives people hope that protein aggregation diseases in the brain can be prevented or treated by blocking the process of transporting vesicle-encapsulated, aggregation-prone proteins to axons
These findings may lead to the development of new therapies for prion diseases and other neurodegenerative diseases