The main function of the AJC in corneal endothelium is to selectively restrict the flow of water and solutes through the paracellular space, as well as to preserve the polarity of ionic channels including Na
+/K
+ ATPase. The latter function is particularly important, as it is fundamental for the “pump” function of the endothelial layer, the ability to actively transport excessive fluids and electrolytes from corneal stroma toward the anterior chamber.
5 Within the AJC, TJs are established by the homophilic interactions of specific transmembrane proteins such as claudins, occludins, and junction adhesion molecules (JAMs), and further supported by cytoplasmic components, including the adopter protein ZO-1.
6,7 One characteristic of corneal endothelium TJs is their “leakiness,” or relatively high permeability for both fluids and macromolecules.
8 The AJs, which are localized below the TJs, function to stabilize cell-cell connections. The principal adhesion receptors constituting the AJs are “classical” cadherins, a family of transmembrane glycoproteins that bind in a homophilic manner with cadherin molecules on adjacent cells.
9 Inside the cytoplasm, cadherins interact with β-catenin and p120-catenin, among others. β-catenin binds αE-catenin, an adaptor protein known to interact with F-actin. As a consequence, cadherins accumulate actin filaments along the AJs, and in this way control cell shape and contractility. This also occurs in corneal endothelial cells; thick circumferential actin belts demarcate their cell-cell contacts.
6 Among the classical cadherins, N-cadherin is highly expressed in the corneal endothelium.
10 In mouse embryos, it is detected as early as stage E15 when endothelial cells start to differentiate from surrounding mesenchymal cells
10,11 and its expression persists in adult corneas.