This site has been optimized to work with modern browsers and does not fully support your version of Internet Explorer.

Labelling proteins through the diet gives new insights into how collagen-rich tissues change as we age

A new study, published in eLife, uses advanced tissue analysis technology to show how the incorporation of new proteins changes in bone and cartilage with age.

During ageing, cellular and physiological processes naturally decline and this is a particular problem in collagen-rich tissues such as the articular cartilage and bone, where tissue turnover is low and repair of the tissue is reduced with age. Reduced repair capacity increases the risk of common age-related diseases such as osteoarthritis (OA), non-union after bone fracture, and osteoporosis.

Protein studies have previously indicated levels of protein in a tissue at any given time, but are unable to provide information on how much is being newly synthesised and incorporated into the tissue. A new study, published in ELife,  uses a new methodology that gives researchers the ability to examine protein synthesis in situ, providing details of activity in the tissues under normal physiological conditions at different ages.

The tissues in the cartilage, bone and skin are made up of an extracellular matrix (ECM), which is a dynamic network composed of collagens and proteins, and collectively known as the matrisome.

The research team at the Kennedy Institute of Rheumatology used an in vivo technique called pulsed SILAC labelling in healthy mice to show changes in the synthesis of proteins of the matrisome over three stages of life: during maximum skeletal growth, and at young, and older adulthood.

Read the full story on the Nuffield Department of Orthopaedics, Rheumatology & Musculoskeletal Sciences website

Research Healthcare Innovation Education and Training