Stanford University: Aging Disrupts Ribosomal Functions in the Body Leading to Many Diseases

As you get older, your cells weaken, and ribosomes which are important organelles in your cells fail in their functions – manufacturing of body proteins – and this hinders the formation of healthy proteins for your cells. Your body proteins become clustered and do not take their normal three-dimensional shape when formed. This makes you prone to several diseases.

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Ribosomes

Ribosomes. Image Credit Felipe Serrano

Ribosomes are cell organelles that serve as the sites for protein manufacture in the cell. You can say they are the protein-manufacturing factory of your cells. After chains of amino acids have been made from ribosomes (through the process known as translation), they fold into a specific protein that has a three-dimensional shape ready for action. Diseases arise when there is a problem with protein folding as a result of the decline in the function of your ribosomes as you get older.

The study

Researchers at Stanford University were the first to carry out a study to determine how aging causes improper folding and clustering of proteins. They carried out the research using these two versions of an older human – yeast, and roundworms. Yes, they knew that clustering of body proteins is causative of many body disorders. What they weren’t quite sure of was how getting old leads to this ‘protein clustering’, and this was the reason for their research.

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They started off the study first by looking into the body’s protein-manufacturing company – ribosomes. They wanted to find out the difference in the function of these ribosomes in an older cell and a younger one. To determine the movement of ribosomes during translation in an older cell, they used the Ribosome Profiling technique. They observed that the ribosomes moved quite slow, and at some points, stood still, causing the ones behind to run into them. This abnormal movement of the ribosomes, as they observed, was the basis of the clustering and improper folding of proteins after translation. This event puts more stress on your cell organelles that clean out your cell – your lysosomes – since at this moment your cell sees these abnormal proteins as foreign bodies and would want to clean them out. However, since millions of proteins are being made by each cell of your body, your lysosomes would have to work twice as hard but still do not clean out every clustered protein completely, leaving about thousands of residue behind. These residues accumulate in your cells causing you to be readily available to diseases like Alzheimer’s and Parkinson’s when they arrive.

The researchers discovered this and something interesting as well that might help improve ribosomal function. They found that mutation in aged yeast that increased its lifespan made its ribosomes function like that of a young yeast’s cell. Further research on this discovery is being carried out, to find out how this can help improve the function of the ribosomes in older humans.

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Your body proteins work well and retain their high solubility in the cell environment when the amino acid chains formed during translation are folded properly. On the contrary, when they do not, they tend to become sticky – sticking to each other and other proteins – resulting in a clog-up of cellular activities and buildup of dangerous residual clusters. Ribosomes function to prevent this abnormal folding of protein units, therefore, problems with ribosomal function affect the formation of healthy body proteins.

Clinical Significance

The knowledge of ribosomes and their essence to healthy protein formation would help scientists and doctors further research better ways to treat age-related diseases.

Conclusion

Age-related diseases have their origin in improper protein folding arising from reduced ribosomal function with age. New research might open up new avenues for their management.

Read Also: Mitochondrial Health Critical in Cancer, Diabetes, and Neurodegenerative Diseases

References

Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis

 

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