Cadherin-13, also known as T-Cadherin and H‑Cadherin, is a GPI-anchored protein belonging to the Cadherin superfamily of calcium-dependent adhesion molecules. Cadherins are involved in multiple processes including embryonic development, cell migration, and maintenance of epithelial integrity (1, 2). Following removal of its C‑terminal propeptide, Cadherin-13 is expressed on the cell surface both with and without its N-terminal propeptide in species of approximately 120 kDa and 100 kDa, respectively (3, 4). Mouse Cadherin-13 contains five tandem Cadherin repeats and shares 95% and 98% aa sequence identity with human and rat Cadherin-13, respectively (5). It is most highly expressed in the circulatory and nervous systems, particularly on cardiac myocytes, vascular endothelial and smooth muscle cells, and neurons and astrocytes in the brain (3, 4, 6 - 9). Cadherin-13 exerts a negative influence on neurite extension, and it is down‑regulated in neurons upon NGF stimulation (10, 11). Homotypic Cadherin-13 interactions promote intercellular adhesion which can be inhibited by its binding to LDL (12). Cadherin-13 also mediates the cardioprotective effects of Adiponectin by directly binding Adiponectin (selectively the hexameric and HMW forms) and trapping it on vascular endothelial cells and cardiomyocytes (6 ‑ 8). The role of Cadherin-13 in the vasculature is complex. When expressed on vascular endothelial cells it promotes angiogenesis, but when expressed on stromal cells it inhibits neovascularization (13, 14). Its down‑regulation on breast carcinoma cells and up‑regulation on the vasculature of various tumors limits tumor cell proliferation and angiogenesis but also enhances tumor progression (4, 8, 15).