Parkinson’s disease progression: a mutated version of the α-synuclein protein moves through the brain’s lymphatic system, known as the glymphatic system, before aggregating.
The mutated α-synuclein protein propagates through the glymphatic system before forming clumps.
Fluorescent α-synuclein appeared in distant brain areas just two weeks post-injection, showing early propagation
Fibrils of α-synuclein only formed 12 months post-injection, highlighting the delay between propagation and aggregation.
The fibrils are transmitted from neurons to neurons, but it remains unclear whether monomers act in the same way.
A mutated version of a protein called α-synuclein propagates to various cerebral regions through the lymphatic system and then aggregates.
Fluorescent α-synuclein was detected in remote regions two weeks after injection, indicating an early spreading of mutant α-synuclein in the brain. α-synuclein participates in neurotransmission.
However, in some neurodegenerative diseases including Parkinson’s disease, α-synuclein changes shape and forms pathological clumps.
Fluorescent α-synuclein was found in the glymphatic system, which is the lymphatic system of the brain.
The glymphatic system is involved in draining and renewing fluid from the brain and eliminating toxins, but it could also distribute toxic substances throughout the brain.
Fluorescent α-synuclein was found in the matrix surrounding neurons and in the cytosol of neurons. This finding suggested that fluorescent α-synuclein was taken up by the extracellular matrix and, subsequently, by neurons.
Thus, prion-like protein propagation is considered a common pathogenic mechanism in neurodegenerative diseases.
