ADAM1bfa15(redirected from ADAM Metallopeptidase Domain 15)
ADAM1bfa15An ADAMs family protein encoded by ADAM15 on chromosome 1q21.3, which is expressed on a wide range of cells. It has a zinc-binding metalloprotease domain, an EGF-like domain, and a disintegrin-like domain, through which it interacts with the integrin beta chain. ADAM 15 also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner (and thus may play a role in cell-cell adhesion and cell signalling) and, being collagenolytic, plays a role in wound healing and may be involved in cartilage remodelling. ADAM 15 mediates intraepithelial cell/T-cell interactions and T-cell aggregation, inhibits integrin-mediated cell adhesion and migration of airway smooth muscle cells, cleaves E-cadherin in response to growth factor deprivation, and plays a role in glomerular cell migration. ADAM 15 is involved in sperm epididymal maturation and the acrosome reaction and appears to be involved in sperm-egg binding via its disintegrin domain. It has an RGD tripeptide and thus may be involved in cell-cell interactions with various integrins. ADAM 15 has a cytoplasmic tail that can act as an SH3 domain ligand and interact with endophilin-1 and sorting nexin-9. ADAM 15 may also be involved in intracellular functions, including protein maturation, shedding of CD23, and transactivation of EGF receptors. CRII-7, the rat homolog of ADAM15, is differentially expressed during sciatic nerve regeneration in Schwann cells, endothelial cells of peripheral nerve, and in various neuronal populations in brain and spinal cord.
Abnormal expression ADAM 15 is overexpressed in atherosclerotic lesions, and is involved in pathological neovascularization, and haematologic malignancies—eukaemia, erythroleukaemia (K562), lymphoma, myeloma.