Researchers Believe Protein Aggregation Is the Cause Behind a New, Rare Form of Dementia

Neurodegenerative diseases damage the human brain and spinal cord (central nervous system, or CNS), both of which help us think, control our movements, and interpret the environment surrounding us. Over time, neurodegenerative diseases can cause severe cell damage or death. Cell death can lead to dementia and the loss or impairment of at least two crucial CNS functions, such as memory, judgment, critical thinking, decision-making, and the ability to participate in social interactions.

Multiple neurodegenerative diseases cause dementia, including Alzheimer’s disease, Lewy body disorder, and frontal temporal lobar degeneration (FTLD). Recently, researchers have discovered a new form of genetic dementia, and its similarities with the mechanisms of Alzheimer’s disease are striking. Since the two share many attributes, researchers are hopeful that knowledge of a new disease pathway could show treatment potentials for both diseases.

A New Form of Dementia

Researchers at Penn Medicine discovered a new form of dementia via human brain tissue studies from a cadaver donor who had a previously unidentified neurodegenerative disease. They found that the genetic information in the tissue they received displayed a new type of mutation of the gene that produces Valosin-containing protein (VCP). The brain tissue also showed several neurons with holes forming in the middle (vacuoles) and a buildup of tau proteins, leading researchers to name this new form of dementia vacuolar tauopathy (or VT, for short).

The brain of the VT patient displayed similar levels of tau protein buildup in its deteriorating portions as the brain of an Alzheimer’s patient. In both diseases, tau proteins—proteins responsible for maintaining microtubule stability and structural stability in neurons—are overly abundant and misshapen. These protein aggregations are thought to disrupt normal neuron activity and lead to neuronal damage that causes dementia.

Unique Mutation Reveals Insights

Penn researchers examined the VCP and tau proteins independently and arrived at an interesting conclusion—the VCP gene mutation causes an environment within the brain that promotes tau protein aggregation. Researchers now believe that VCP’s function is to identify proteins within an aggregate and separate them, thus dispersing the aggregate. Since the mutation inhibits the production and activity of VCP, the protein’s function within a neuron is also inhibited—thus, the genetic VCP mutation leads to uncontrolled tau protein aggregation.

This newly identified protein aggregation pathway has given researchers a new therapeutic target for both VT and Alzheimer’s. In theory, since inhibited VCP works to enhance protein aggregation, increased VCP may help disperse aggregates. Thus, researchers could one day halt the neuronal deterioration caused by VT and Alzheimer’s by eliminating tau protein aggregates, preventing the onset of dementia.

Future Potential

While the study of VT offers promising implications for new treatments for VT, Alzheimer’s, and other tau protein disorders, the new possibilities unlocked with the study of other rare mutations provide even more hope. Rare genetic mutations and the disorders they cause may reveal disease processes similar to those of other well-known neurodegenerative diseases. Thus, ongoing studies of rare diseases may eventually inspire new therapies that can benefit people suffering from neurodegenerative diseases of all types.

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