Recombinant Human Podoplanin Fc Chimera Protein, CF

Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1-alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family (1-2). Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation (2-3). There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells (4-5), and numerous tumors, including colorectal tumors (3), squamous cell carcinomas (4, 6), testicular seminoma (7), and brain tumors (8-10). One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC-2) (2). Their association is dependent on sialic acid on O-glycans of Podoplanin (2). Through its association with CLEC-2, Podoplanin induces platelet aggregation and tumor metastasis (2). Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth (2).