There are currently no new disease-modifying therapies that can change the progression of Parkinson’s disease, but scientists from the University of Colorado and other institutions have conducted research that may improve the treatment of Parkinson’s disease.
The researchers took a deep dive to uncover the characteristics and key roles of the key protein α-synuclein (αSyn, α-synuclein), and found that it may link inflammation to Parkinson’s disease. Alpha-synuclein is mainly expressed in neurons and is often directly associated with the development of neurodegenerative diseases such as Parkinson’s disease and Lewy body dementia. Researchers have revealed a specific mechanism that may interfere with Activation of alpha-synuclein is linked to the function of alpha-synuclein in neurons, making this mechanism promising as a potential trigger for Parkinson’s disease progression.
David Beckham, MD, noted that further understanding of the elicitors that lead to Parkinson’s disease and elucidating how inflammation interacts with proteins found in the disease are critical to developing novel targeted therapies, and based on the findings, we may hope to Altering or intervening in the inflammatory pathways that act as elicitors in diseases can provide certain ideas and research foundations for the development of new treatments.
To investigate the molecular mechanisms underlying α-synuclein-induced immune responses to viral infection in the brain, the researchers used RNA virus infection to “challenge” α-synuclein knockout mice as well as human α-synuclein In dopaminergic neurons in which the nuclear protein was knocked out, it was found that α-synuclein is necessary for neurons to express interferon-stimulated genes (ISGs), and they subsequently found that in any evoked interferon signal Following stimulation (a type of immune response), α-synuclein interacts with signaling proteins in neurons to induce the expression of ISGs.
The study proposes the first definitive mechanism linking inflammation to alpha-synuclein, a specific protein closely linked to the development of Parkinson’s disease. The researchers pointed out that the data in this study confirmed the response of α-synuclein to infection and inflammatory signaling pathways, and suggested that this interaction may play an important role in the development of Parkinson’s disease. The next step is to study Research will determine whether the interaction between interferon and alpha-synuclein induces the formation of toxic forms of misfolded alpha-synuclein (ie, fibrils), which are primarily found in in patients with Parkinson’s disease.
Finally, the researchers say that future studies will need to shed light on the interaction between type 1 interferon signaling and misfolded α-synuclein in neurons to determine whether drugs that inhibit these interactions can inhibit the error. The formation of folded alpha-synuclein, which may help develop a potential disease-modifying treatment.
