Analysis of angiogenin mutations provides insight into neurodegenerative disease


Angiogenin is a protein that plays a role in stimulating angiogenesis, the process of blood vessel formation. Various mutations in angiogenin have been found to correlate to Parkinson's Disease (PD) and Amyotrophic Lateral Sclerosis (ALS), both of which are neurodegenerative diseases. But the mechanism of angiogenin action is not completely understood.

Now a study of the University of Bath provides insight into the role of angiogenin in PD and ALS. Described in Scientific Reports, the study would help understand the cause of the two diseases and develop novel treatments. The study's senior author is K. Ravi Acharya from the University of Bath Department of Biology and Biochemistry.

ALS is a disease predominantly affecting motor neurons in the brain and spinal cord. These neurons are responsible for controlling the voluntary muscles. The cause of more than 90% of all ALS cases is unknown. PD occurs when the brain fails to produce enough dopamine, a neurotransmitter that is important for transmitting signals between different brain regions. Both ALS and PD affect patients' movement function. Over time, the diseases can lead to weakness, rigidity, cramping, or atrophy of muscles, difficulty with walking, swallowing, and breathing, and even cognitive impairment.

Acharya's team previously has shown that angiogenin is expressed in neurons during neuro-ectodermal differentiation and the protein protects neurons from cell death. Additionally, certain mutations in angiogenin prevent the protein from being transported to the cell nucleus, a process crucial for its normal function.

The focus of the current study is to determine exactly how angiogenin mutations affects the structure and function of the protein. Acharya and colleagues analyzed the three-dimensional structures of eleven new mutant versions of angiogenin implicated in PD and ALS: H13R, K40R, K54R, K60E, Q77P, T80S, R95Q, F100I, V103I, H114R, R121C. By comparing these angiogenin variants with the wide-type angiogenin, the researchers elucidated altered molecular interactions that underpin the abrogated catalytic efficiency or an increase in RNase activity of these angiogenin variants.

The researchers believed that their findings would provide structural and molecular basis in understanding the role of angiogenin mutations in the pathogenesis of PD and ALS.

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