Alpha-parvin (PARVA)

Alpha-parvin is an actin-binding adaptor protein that localizes to focal adhesions and interfaces with the integrin-linked kinase (ILK)/PINCH complex (IPP complex), connecting integrin signaling to the actin cytoskeleton[2][8]. It contains calponin homology domains, mediates cell–extracellular matrix adhesion, and regulates cell spreading, motility, and survival[1][3][7]. PARVA interacts directly with ILK, paxillin, and F-actin, influencing focal adhesion turnover, lamellipodia formation, and cytoskeletal architecture[1][2]. It is essential for embryonic cardiovascular development and angiogenesis, and aberrant expression promotes cancer invasion, metastasis, and angiogenesis across various tumor types[1][3][7]. Alpha-parvin is considered a therapeutic target in fields such as oncology and vascular biology due to its role in cancer progression and blood vessel integrity, but as of now, no direct drugs modulate PARVA clinically[1][3][7].

Other names

Alpha-parvinPARVAMXRA2FLJ12254FLJ10793ActopaxinCH-ILKBPCalponin-like integrin-linked kinase-binding proteinMatrix-remodeling-associated protein 2

Not applicable for approved drugs or clinical candidates—PARVA is mechanistically modulated through protein–protein interactions, such as with ILK and paxillin, affecting focal adhesion dynamics