Recombinant Human ADAMTS15 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ADAMTS15 also known as A Disintegrin And Metalloproteinase with Thrombospondin motifs 15 is a member of the ADAMTS family of zinc-dependent metalloproteases. It is involved in the degradation of extracellular matrix components especially proteoglycans. This protease has a mass of approximately 110 kDa. Researchers found ADAMTS15 expression mainly in cartilage and testis highlighting its tissue-specific roles. Understanding its mechanical role as a proteoglycanase gives insight into its contribution to tissue remodeling dynamics.

Biological function summary

ADAMTS15 plays a significant role in extracellular matrix organization and turnover. It mediates proteolytic processing of aggrecan and other proteoglycans which are important for structural integrity in tissues like cartilage. It operates independently rather than as part of a complex. The proteolytic function of ADAMTS15 is essential in processes like embryonic development cell migration and angiogenesis emphasizing its influence in maintaining normal physiological functions.

Pathways

ADAMTS15 is implicated in the proteoglycan turnover pathway and the Wnt signaling pathway. Its activities within these pathways contribute to cellular matrix degradation and regulation of cell growth and differentiation. ADAMTS15 associates with other proteins such as aggrecan and collagen that participate in matrix degradation. It shows functional similarities and interactions with other ADAMTS family members like ADAMTS4 and ADAMTS5 which further support its role in matrix dynamics.

Researchers link ADAMTS15 with osteoarthritis and some forms of cancer. In osteoarthritis abnormal activity of ADAMTS15 leads to excessive degradation of cartilage matrix contributing to joint degeneration. Proteins like aggrecan targeted by ADAMTS15 play a role in this disorder. In cancer ADAMTS15 involvement appears in the regulation of tumor microenvironment dynamics and metastasis. Its interaction with structural components of the matrix makes it a potential therapeutic target in both contexts.