Melanoma inhibitory activity protein (MIA)

Melanoma inhibitory activity protein (MIA) is a small, secreted, extracellular protein (11-12 kDa) that adopts an SH3 domain-like fold, distinct in being the first secreted protein of its kind[1][2]. It plays a clinically significant role as a biomarker for melanoma, with elevated levels indicating advanced metastatic disease. MIA is involved in modulating cell adhesion by interacting with fibronectin and inhibiting melanoma cell attachment to the extracellular matrix, thus contributing to tumor metastasis[1][2][5]. It is also expressed in cartilage and is implicated in cartilage development. Molecularly, although related to intracellular SH3-domain proteins, MIA is unique in structure and ligand recognition, suggesting specialized extracellular signaling or matrix interaction functions[2][4][5].

Other names

Melanoma-derived growth regulatory proteinCD-RAPMIA1cartilage-derived retinoic acid-sensitive protein

Inhibits cell adhesion to the extracellular matrix by binding fibronectin and competing with integrin binding[1][2]\nInhibits melanoma cell growth in vitro[5]