Podoplanin (PDPN) is a small transmembrane glycoprotein encoded by the T1α gene, initially identified in lymphatic endothelial cells. It plays critical roles in cell migration, adhesion, and signaling, particularly during embryonic development, immune responses, and cancer progression. Structurally, it contains a heavily O-glycosylated extracellular domain that mediates interactions with ligands like CLEC-2 (C-type lectin-like receptor-2) on platelets, influencing thrombosis and metastasis. Notably, podoplanin is a well-established marker of lymphatic endothelium, helping distinguish lymphatic vessels from blood vessels in pathological studies.
Antibodies targeting podoplanin are widely used in research and diagnostics. For example, the D2-40 monoclonal antibody is a gold-standard tool for detecting lymphatic structures in immunohistochemistry, aiding in the diagnosis of vascular tumors and assessing lymphatic invasion in cancers. Beyond lymphatics, podoplanin is overexpressed in various malignancies, including squamous cell carcinoma, glioblastoma, and sarcoma, where it correlates with tumor invasiveness and poor prognosis. Researchers also explore its role in cancer stem cells and epithelial-mesenchymal transition.
Recent studies highlight podoplanin's involvement in inflammatory diseases and fibrosis, expanding its therapeutic relevance. Antibodies against podoplanin are being investigated for targeted therapies, such as antibody-drug conjugates or immune checkpoint modulation. However, challenges remain in understanding its tissue-specific glycosylation patterns and context-dependent functions. Overall, podoplanin antibodies remain indispensable for both basic research and clinical applications, bridging molecular mechanisms with diagnostic and therapeutic innovation.