Rockville, Md. (May 13, 2021)—Researchers from the Oklahoma Medical Research Foundation (OMRF) have found a new way to successfully use a stable isotope of water to learn how fibrosis—scarring or hardening—develops in muscle with age. The new approach revealed a “surprisingly small amount of the collagen in muscle was capable of renewing [itself], and that this got worse with age.”
Scientists coined a new term for this novel method, called “dynamic protein pool,” to indicate what fraction of the proteins (collagen) could renew. In addition, the team found that not accounting for how much collagen was able to renew could lead to the wrong conclusions about how to treat muscle fibrosis.
“Our findings shed light on how fibrosis develops in muscle and, therefore, how to treat it,” said Benjamin Miller, PhD, one of the OMRF scientists conducting the study. “Our new approach can be applied to other fibrotic disease conditions, like liver disease. Since our approach allows us to better understand whether fibrosis results from making too much collagen or from the failure to remove collagen, we can use it to determine what process to target to prevent or treat fibrosis.”
Read the full article, “A novel stable isotope approach demonstrates surprising degree of age-related decline in skeletal muscle collagen proteostasis,” published ahead of print in Function. Contact the APS Communications Office or call 301.634.7314 to schedule an interview with a member of the research team.