Human A Disintegrin And Metalloprotease 12 (ADAM12) Protein

Background

ADAM12, also known as ADAM metallopeptidase domain 12, is another member of the ADAM (a disintegrin and metalloproteinase) family of proteins. Like ADAM10, it is a type I transmembrane glycoprotein encoded by the ADAM12 gene. ADAM12 is known to be involved in various biological processes, including cell adhesion, migration, proliferation, proteolysis, and signaling. It has been implicated in several pathological conditions, including cancer, inflammation, and developmental disorders. ADAM12 is its involved in extracellular matrix (ECM) remodeling. It can cleave ECM components such as fibronectin and type IV collagen, thereby facilitating tissue remodeling processes like wound healing and tissue repair. Additionally, ADAM12 has been shown to interact with integrins, which are cell surface receptors involved in cell adhesion and signaling, further implicating its role in cell-ECM interactions. ADAM 12, a metalloprotease that binds insulin growth factor binding protein-3 (IGFBP-3), appears to be an effective early Down syndrome marker. Decreased levels of ADAM 12 may be detected in cases of trisomy 21. In cancer, ADAM12 expression levels have been found to be dysregulated in various tumor types, and its overexpression has been associated with tumor progression, invasion, and metastasis. It can promote cancer cell migration and invasion by cleaving ECM components, modulating cell adhesion, and facilitating epithelial-to-mesenchymal transition (EMT), a process implicated in cancer metastasis.