Muscles rid themselves of worn-out proteins through exercise

Muscles rid themselves of worn-out proteins through exercise

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The self-cleaning of the muscles

Physical activity cleanses the muscles through a newly discovered mechanism. Researchers from Copenhagen showed how worn-out proteins are labeled during physical activity and then disposed of. According to the research team, this mechanism partly explains why sport is so beneficial for health.

Scientists at the University of Copenhagen deciphered the cleaning effect of physical activity on the muscle. A protein called ubiquitin plays a key role in this because it labels worn proteins that are subsequently broken down. The research work was recently presented in the "FASEB Journal".

Exercise keeps the muscles healthy

Researchers at the Faculty of Nutrition, Exercise and Sport at the University of Copenhagen have shown that physical activity cleanses the muscles by labeling worn proteins with ubiquitin, which breaks them down. This prevents the accumulation of damaged proteins and helps to keep the muscles healthy.

Numerous health benefits from sport

It is well known that physical activity has many health benefits. It is also not new that sport is fundamental to building and maintaining muscles. Since muscles convert a large part of the carbohydrates, they also play an important role in regulating the metabolism.

The puzzle of healthy sport

Even though the many benefits of sport on health are known, it is still not fully understood how these positive effects come about. The Danish-Australian research team is now one step closer to deciphering this puzzle.

Cleaning the muscles for maintenance

Maintaining muscle function is essential for human health. This is achieved by breaking down proteins, i.e. the building blocks of the muscles, when they wear out and eliminating them in a kind of cleaning process. The disposed proteins are then replaced by fresh ones.

In experiments on people riding bicycles, the researchers were able to document that the level of the protein ubiquitin is significantly increased after just ten minutes of activity. The increase was followed by a removal of worn proteins. This in turn paved the way for the enrichment of new proteins.

Muscle recycling

"Ubiquitin itself is a small protein," explains Professor Erik Richter from the research team. It attaches to the amino acid lysine on worn proteins, whereupon the protein is transported to a proteasome, a structure that engulfs proteins and processes them into amino acids. These amino acids can then be reused in the synthesis of new proteins. As such, ubiquitin contributes to a very sustainable circulation of the body's proteins.

New knowledge about the circulation of the muscles

Although extensive knowledge has accumulated on how muscles regulate the formation of new proteins during physical training, much less is known about how muscle contractions and training serve to significantly clean worn proteins, the researchers conclude. "The important role of ubiquitin in cleaning up worn proteins in connection with muscle activity has not been fully appreciated," adds Professor Bente Kiens from the project team. "Now we know that physical activity increases the ubiquitin labeling of worn proteins."

Use it or loose it

"Basically, the mechanism explains part of the reason why physical activity is healthy," adds Professor Jørgen Wojtaszewski. The muscles themselves initiate processes that keep them healthy and functional - provided they are used. (vb)

Author and source information

This text corresponds to the specifications of the medical literature, medical guidelines and current studies and has been checked by medical doctors.

Graduate editor (FH) Volker Blasek


  • Benjamin L. Parker Bente Kiens Jørgen F. P. Wojtaszewski, u.a .: Quantification of exercise ‐ regulated ubiquitin signaling in human skeletal muscle identifies protein modification cross talk via NEDDylation; in: FASEB Journal, 2020,
  • University of Copenhagen: The death marker protein cleans up your muscles after exercise (published: 28.05.2020),

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