New findings reveal key catalyst that triggers Huntington’s disease

In an exciting breakthrough, scientists have unravelled the long-standing mystery surrounding Huntington’s disease, bringing us closer to a potential treatment that could halt its progression.

The discovery not only offers hope for individuals affected by this debilitating condition but also holds promising implications for other neurodegenerative disorders like Alzheimer’s disease.

On that note, let’s delve into the fascinating findings and their potential impact on our understanding and treatment of Huntington’s disease.

What is Huntington’s disease?

What is this condition? (Image via Freepik/Kjpargeter)

Huntington’s disease is a neurological disorder triggered by a protein known as huntingtin.

Due to a genetic mutation, the HTT protein develops an unusually long strand of repeating amino acids, forming what’s called the polyglutamine (polyQ) stretch.

Typically, this sequence has an average of 17-20 repeats, but in this disease, it often exceeds 40 reps. The number of repetitions correlates with the onset of symptoms like personality changes and movement disorders.

Role of protein misfolding

The mutated form of the HTT protein accumulates in the brain, folding itself into a toxic shape that harms cells. These proteins, known as amyloids, exhibit similar behavior in other neurodegenerative disorders like Alzheimer’s and Parkinson’s diseases.

Amyloid clusters, specifically beta-amyloid in the brain, have been linked to Alzheimer’s disease. Furthermore, the build-up of various amyloid precursors in other parts of the body can lead to a range of conditions referred to as amyloidosis.

Structure reveals protein that triggers Huntington’s disease

Protein unfolding identified (Image via Freepik/Pressfoto)

While scientists have long been aware of the protein misfolding phenomenon, the exact mechanisms behind it remained elusive. However, researchers from the Stowers Institute for Medical Research have made a significant stride towards understanding this process.

Led by Dr Tej Kandola and Dr. Shriram Venkatesan, the team successfully determined the structure of the amyloid nucleus in the HTT protein — a crucial “spark”that initiates the chain reaction of protein misfolding.

Promising path for treatment

A key finding from the study is that the nucleus only forms in isolated proteins. This discovery opens up the possibility of preventing amyloid formation by finding ways to aggregate the proteins together.