ADAM15

Disintegrin and metalloproteinase domain-containing protein 15 is an is_associated_with::enzyme that in humans is encoded by the ADAM15 is_associated_with::gene.

Function
The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I is_associated_with::transmembrane is_associated_with::glycoproteins known to be involved in is_associated_with::cell adhesion and proteolytic is_associated_with::ectodomain processing of is_associated_with::cytokines and is_associated_with::adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a is_associated_with::disintegrin-like domain, as well as an is_associated_with::EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a is_associated_with::phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.

Arthritis
ADAM15 has been associated with a number of diseases, most recently is_associated_with::Rheumatoid Arthritis where it is required for the activation of the FAK and Src pathways to generate apoptosis resistance in response to apoptotic signalling or cell stress. ADAM15 also has an antiapoptotic effect in osteoarthritic is_associated_with::chondrocytes.

Cancer
The precise role of ADAM15 in cancer is still unclear but the metalloprotein has been linked to a number of different cancerous diseases such as is_associated_with::Breast cancer where the expression of the protein is increased in carcinoma in-situ, invasive carcinoma and metastatic breast cancer tissues Additionally, the alternative splice variant forms of ADAM15 have also been correlated with different prognosis in 48 breast cancer patients based upon their expression levels. ADAM15 has also been shown to have a role in is_associated_with::Prostate Cancer again through increased expression in neoplastic and metastatic tissues compared to normal prostate tissues and also through its modulation of epithelial cell- tumour cell interactions.

Interactions
ADAM15 has been shown to interact with:
 * is_associated_with::Grb2,
 * is_associated_with::HCK,
 * is_associated_with::Lck and
 * is_associated_with::SH3GL2, and
 * is_associated_with::SNX9.

The alternatively spliced isoforms have also been shown to exhibit different preferential interactions with proteins containing SH3 domains.