S100 calcium-binding protein A14 (S100A14)

S100 calcium-binding protein A14 (S100A14) is a low-molecular-weight member of the S100 protein family, characterized by EF-hand calcium-binding motifs. Despite being classified in this family, human S100A14 does not bind calcium with significant affinity due to changes in its canonical EF-hand structure. Functionally, S100A14 regulates cell survival and apoptosis through modulation of p53/TP53 levels and impacts cell migration by controlling MMP2, a matrix protease. It interacts with the receptor for advanced glycation end products (RAGE), triggering associated signaling pathways. S100A14 is primarily a cytoplasmic protein expressed in specific tissues, with expression often reduced in cancerous cells and linked to increased metastasis, suggesting a tumor suppressor role. There are no clinically approved drugs specifically targeting S100A14, but its expression may have biomarker potential in cancer settings. The protein is studied for possible roles in cancer and inflammation, but significant challenges remain for therapeutic exploitation due to redundancy and overlap within the S100 protein family.

Other names

S100A14BCMP84S100A15S114Protein S100-A14breast cancer membrane protein 84