The Cadherins are a family of transmembrane glycoproteins that mediate homophilic, Ca2+-dependent cell-cell adhesion (1). The cadherin-mediated adhesion provides strong intercellular bonds, which are dependent upon the association of the cadherin carboxyterminal cytoplasmic domain to the central region of β- or γ-catenin and p120 (2). β and γ-catenin bind α-catenin, in turn promote the anchorage of the complex to the actin cytoskeleton. The structural integrity of cardiac cells is maintained by the Ca2+-dependent homophilic cell-cell adhesion of cadherins. N-cadherin is responsible for this adhesion under normal physiological conditions (2). Although it is established that N-cadherin and E-cadherin are crucial for cardiogenesis (3), to date, few studies have addressed the expression and role of these cadherins in adverse cardiac pathology. A study by Kostetskii et al, illustrated that deletion of N-cadherin in the mouse heart leads to dilated cardiomyopathy and impaired cardiac function due to loss of N-cadherin-mediated anchorage of myofibrils at the plasma membrane (4). This study highlights the absolute requirement for N-cadherin in the heart. We hypothesised that cadherins may be dysregulated in the remodelling associated with the hearts of the stroke-prone spontaneously hypertensive (SHRSP) rat and any alteration in expression may contribute to the alteration in the mechanical and electrical activity observed in these hearts. Western blotting of protein homogenates from 12-week old SHRSP animals indicated that similar levels of β, γ-, and α-catenin and T, N and R-cadherin were expressed in the control and SHRSP animals. However, dramatically higher levels of E-cadherin were detected in SHRSP animals compared to controls at 6, 12 and 18 weeks of age. This was confirmed by quantitative Taqman PCR and immunohistochemistry. E-cadherin was located at the intercalated disc of the myocytes in co-localisation with connexin 43. Adenoviral overexpression of E-cadherin in rat H9c2 cells and primary rabbit myocytes resulted in a significant reduction in myocytes cell diameter and breadth. E-cadherin overexpression resulted in re-localisation of β-catenin to the cell surface particularly to cell-to-cell junctions. Subsequent immunohistochemistry of the hearts of WKY and SHRSP animals also revealed increased levels of β-catenin in the intercalated disc in the SHRSP compared to WKY. Therefore, remodelling of the intercalated disc in the hearts of SHRSP animals may contribute to the altered function observed in these animals.