Recombinant Human Desmoglein-1 Fc Chimera Protein, CF

Desmoglein-1 is one of three members of the desmoglein subfamily of calcium-dependent cadherin cell adhesion molecules. Together with desmocollins, another subfamily within the cadherin superfamily, the desmoglein isoforms form the adhesive components of desmosomes, the cell-cell adhesive structures that are found in epithelial cells. Human Desmoglein-1 is a type I transmembrane glycoprotein of 1049 amino acid (aa) residues with a 23 aa signal peptide and a 26 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, Desmoglein-1 has R/YAL as the adhesion motif on its amino-terminal cadherin repeat. The cytoplasmic tail of Desmoglein-1 interacts with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the Desmoglein-1 with the intermediate filaments. Desmoglein-1 has been shown to be important in establishing cell-cell adhesion and function in the epidermis. In the autoimmune skin disease pemphigus foliaceus, autoantibodies to Desmoglein-1 can cause the loss of keratinocyte adhesion resulting in blisters.