HomeThe enzymeTechnologyIngredientsStudiesAbout

ADAMTS5

ADAMTS5 is the main enzyme that cuts aggrecan, the cushioning molecule in cartilage. It is a separate enzyme family from MMP13, which cuts the collagen.

Also called ADAMTS-5, aggrecanase-2, a disintegrin and metalloproteinase with thrombospondin motifs 5.

Its full name is a disintegrin and metalloproteinase with thrombospondin motifs 5 (Rong 2019). It is also called aggrecanase-2.

In 2005, mice whose ADAMTS5 lacked its working part had significantly less cartilage destruction after surgery made the knee unstable, which identified ADAMTS5 as the primary aggrecanase in that model (Glasson 2005). A 2021 review listed senescence, inheritance, inflammation and mechanical stress as drivers of its overactivity, through signalling routes that include RUNX2 and NF-kB (Jiang 2021).

In human cartilage cells it often rises alongside MMP13. Higher glucose, inflammation, oxidative stress and calcium crystals raised both (Jain 2024; Rong 2019). Leptin raised ADAMTS5 at a lower dose than it took to raise MMP13 (Primrose 2023). The body's TIMP inhibitors block several ADAMTS enzymes as well as MMPs (Brew 2010).

Sources

  1. Rong J, Zhu M, Munro J et al. Altered expression of the core circadian clock component PERIOD2 contributes to osteoarthritis-like changes in chondrocyte activity. Chronobiol Int 2019.
  2. Glasson SS, Askew R, Sheppard B et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 2005.
  3. Jiang L, Lin J, Zhao S et al. ADAMTS5 in Osteoarthritis: Biological Functions, Regulatory Network, and Potential Targeting Therapies. Front Mol Biosci 2021.
  4. Jain L, Bolam SM, Monk P et al. Elevated glucose promotes MMP13 and ADAMTS5 production by osteoarthritic chondrocytes under oxygenated but not hypoxic conditions. J Cell Physiol 2024.
  5. Primrose JG, Jain L, Bolam SM et al. Concentration-dependent effects of leptin on osteoarthritis-associated changes in phenotype of human chondrocytes. Connect Tissue Res 2023.
  6. Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 2010.

Related terms

Read next

Last reviewed 3 November 2026Every study cited here is indexed on PubMed. How we read the evidence