Fish protein found to prevent “Parkinson's protein” formation, study shows


23 Apr 2018 --- A common protein found in species of fish, parvalbumin, may prevent the formation of specific protein structures that are closely associated with Parkinson’s disease. The study, conducted at the Chalmers University of Technology, Sweden, shines a light on the link between fish consumption and brain health and expands the healthy reputation of fish beyond the famous omega fatty acids.

One of the hallmarks of Parkinson’s disease is the amyloid formation of a particular human protein called alpha-synuclein. Alpha-synuclein is often referred to as the Parkinson’s protein.

The Chalmers researchers have discovered that parvalbumin can form amyloid structures that bind together with the alpha-synuclein protein. Parvalbumin effectively scavenges the alpha-synuclein proteins, using them for its own purposes, thus preventing them from forming their own potentially harmful amyloids at a later point.

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Pernilla Wittung-Stafshede,
Professor and Head of the Chemical Biology division
at Chalmers and lead author on the study. 

Parvalbumin collects up the 'Parkinson’s protein' and prevents it from aggregating, simply by aggregating itself first, explains Pernilla Wittung-Stafshede, Professor and Head of the Chemical Biology division at Chalmers, and lead author on the study.

The researchers state that with the parvalbumin protein being so highly abundant in certain fish species, increasing the amount of fish in the diet may be a simple way to ward off Parkinson’s disease. Herring, cod, carp, and redfish, including sockeye salmon and red snapper, have particularly high levels of parvalbumin, but it is also common in many other fish species. The levels of parvalbumin can also vary throughout the year:

Fish is normally a lot more nutritious at the end of the summer, because of increased metabolic activity. Levels of parvalbumin are much higher in fish after they have had a lot of sun, so it could be worthwhile increasing consumption during autumn, says Nathalie Scheers, Assistant Professor in the Department of Biology and Biological Engineering, and researcher on the study.

Future potential for other neurodegenerative diseases
The research may hold future promise, in terms of other neurodegenerative diseases.

Alzheimer’s, Amyotrophic lateral sclerosis (ALS) and Huntington’s disease are also caused by specific amyloid structures interfering in the brain. The researchers are therefore keen to research this topic further, to see if the discovery relating to Parkinson’s disease could have implications for other neurodegenerative disorders as well.

Pernilla Wittung-Stafshede stresses the importance of finding ways to combat these neurological conditions in the future, These diseases come with age, and people are living longer and longer. There’s going to be an explosion of these diseases in the future – and the scary part is that we currently have no cures. So we need to follow up on anything that looks promising.

A follow-up study, looking at parvalbumin from another angle, is planned for autumn 2018. Nathalie Scheers, together with Professor Ingrid Undeland, also of Chalmers, will investigate parvalbumin from herring, and its transport in human tissues.

It will be very interesting to study how parvalbumin distributes within human tissues in more depth. There could be some really exciting results.

NutritionInsight has previously reported on efforts to detect treatments for wide-spread neurodegenerative diseases. These efforts include research that revealed the links between the gut microbiome – the population of microorganisms living in the gastrointestinal tract – and brain diseases such as Parkinson's and Alzheimer's. The research expanded on budding research on the gut-brain axis and its potential in providing a promising pathway to cures. 

Furthermore, strengthening the age-old saying, we are what we eat, research has detailed that following a low-fat diet in combination with limited caloric consumption could prevent age-related brain dysfunction. 

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