ADAM32 (A Disintegrin and Metalloproteinase 32) is a member of the ADAM family of transmembrane proteins, which are known for their roles in cell adhesion, proteolytic processing, and cell signaling. First identified in the early 2000s, ADAM32 shares structural features common to ADAMs, including a prodomain, metalloproteinase domain, disintegrin domain, cysteine-rich region, and a transmembrane segment. However, unlike many ADAMs with well-characterized protease activity, ADAM32 is predicted to be catalytically inactive due to substitutions in critical residues of its metalloproteinase domain. This suggests non-enzymatic functions, potentially involving cell-cell or cell-matrix interactions through its disintegrin or cysteine-rich domains.
Expression of ADAM32 has been detected in immune-related tissues such as the spleen, thymus, and lymph nodes, as well as in the testis, hinting at possible roles in immune regulation and reproductive biology. Despite its discovery over two decades ago, ADAM32 remains understudied compared to other ADAM family members. Current research focuses on its potential involvement in pathological conditions, including cancer and inflammatory diseases, though mechanistic insights remain limited.
Antibodies targeting ADAM32 are primarily used as research tools to investigate its expression patterns, localization, and interactions. Their development faces challenges due to the protein's structural similarity to other ADAMs and limited knowledge of its physiological ligands. Further studies are needed to clarify ADAM32's biological significance and therapeutic potential.