Statins are among the most widely used medicines in the world. For decades, doctors have prescribed them to lower cholesterol levels and reduce the risk of heart attacks and strokes.
These drugs have helped save millions of lives by preventing dangerous blockages in blood vessels and protecting people from serious heart disease.
High cholesterol is a major risk factor for cardiovascular disease. When too much cholesterol builds up in the blood, it can form plaques inside arteries.
Over time, these plaques can narrow or block blood vessels, increasing the risk of heart attacks and strokes. Statins work by reducing the amount of cholesterol produced by the liver, helping keep blood vessels healthier and lowering the chance of life-threatening events.
Despite their benefits, statins are not perfect. Many people who take them experience muscle-related side effects. Some develop muscle aches, soreness, weakness, or unusual tiredness.
In rare cases, the muscle damage can become severe enough to cause a serious condition known as rhabdomyolysis, which can lead to kidney failure and other complications.
Scientists have known about these side effects for years, but the exact reason they happen has remained unclear. Now, researchers from the University of British Columbia and the University of Wisconsin–Madison believe they have found an important piece of the puzzle.
Their study, published in the journal Nature Communications, reveals how statins may directly affect a key protein inside muscle cells. The discovery could eventually help researchers develop a new generation of statins that continue to protect the heart while causing fewer muscle problems.
To make the discovery, the research team used an advanced imaging technology called cryo-electron microscopy.
This technique allows scientists to create extremely detailed images of biological structures, including proteins, at nearly atomic-level resolution. By freezing samples and examining them with powerful electron microscopes, researchers can see how molecules interact inside the body in remarkable detail.
The scientists focused on a protein known as RyR1. This protein plays a crucial role in muscle function because it controls the release of calcium inside muscle cells. Calcium acts as an important signal that tells muscles when to contract and relax. Under normal conditions, the RyR1 channel opens only when needed and then closes again.
The researchers discovered that statins can interfere with this normal process.
According to the study, statin molecules can attach directly to the RyR1 protein and change its behavior. Instead of opening and closing normally, the channel remains open for longer periods. This allows calcium to leak continuously from internal storage areas within muscle cells.
Lead author Dr. Steven Molinarolo explained that the team was able to observe exactly how statins bind to the protein. Their images showed that the leaking calcium may be responsible for the muscle damage, weakness, and pain that some patients experience while taking these medications.
Calcium is essential for healthy muscle function, but too much calcium in the wrong place can be harmful. When calcium leaks continuously, it can place stress on muscle cells and eventually damage them. This may explain why some people develop muscle aches or weakness after starting statin therapy.
The team paid particular attention to atorvastatin, one of the most commonly prescribed statins worldwide. However, the researchers believe their findings may apply to several other statin drugs as well.
One of the most surprising discoveries was how the statin molecules interact with the RyR1 channel. The researchers found that three statin molecules appear to work together. The first statin molecule attaches to the protein when the channel is closed, making it more likely to open.
Then two additional statin molecules move into position and help force the channel fully open. This chain of events creates the calcium leak that can damage muscle tissue.
Senior researcher Dr. Filip Van Petegem said the findings provide scientists with valuable information for designing better medications. By understanding exactly how statins interact with muscle proteins, drug developers may be able to modify the structure of future statins.
The goal would be to preserve their cholesterol-lowering benefits while preventing them from triggering calcium leaks in muscle cells.
Such improvements could have a major impact on public health. More than 200 million people around the world take statins. Although severe muscle damage is rare, mild muscle symptoms are relatively common. These side effects often lead some patients to stop taking their medication, which may increase their risk of heart attacks and strokes.
A safer statin could help more people continue their treatment without discomfort. This would allow patients to receive the cardiovascular protection they need while maintaining a better quality of life.
The study also highlights the growing importance of modern imaging technologies such as cryo-electron microscopy. These tools allow researchers to observe biological processes that were once impossible to see.
By understanding how medicines interact with proteins at the smallest levels, scientists can identify hidden problems and design more effective treatments.
Dr. Van Petegem believes this discovery is an important step toward making statins even better. Statins have been a foundation of heart disease prevention for decades, and researchers hope that future versions will offer the same powerful protection with fewer side effects.
For millions of people who depend on statins to protect their hearts, the findings provide hope that safer and more comfortable treatments may one day become available.
If you care about muscle, please read studies about factors that can cause muscle weakness in older people, and scientists find a way to reverse high blood sugar and muscle loss.
For more health information, please see recent studies about an easy, cheap way to maintain muscles, and results showing these vegetables essential for your muscle strength.
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