Specific affinity between fibronectin and the epidermolysis bullosa acquisita antigen.

D T Woodley; E J O'Keefe; J A McDonald; M J Reese; R A Briggaman; W R Gammon

doi:10.1172/JCI113024

Autoantibodies in the skin and sera of patients with epidermolysis bullosa acquisita bind to a large matrix molecule within the lamina densa region of skin basement membrane. At the site of these immune complexes, the epidermis separates from the dermis, which creates a subepidermal blister just below the lamina densa. The target molecule for the autoantibodies is in close apposition to fibronectin, a major extracellular matrix molecule that is abundant in the upper dermis of skin. In this report, we show specific affinity between fibronectin and the 290,000-D chain of the epidermolysis bullosa acquisita antigen, and that this affinity is mediated by the gelatin/collagen-binding domain of fibronectin (Mr = 60,000). Since blistering in epidermolysis bullosa acquisita often occurs in the absence of clinical and histological inflammation, a direct interruption in the fibronectin-epidermolysis bullosa acquisita antigen bond may be involved in the pathogenesis of epidermal-dermal disadherence that occurs in this bullous disease.

Images.

Specific affinity between fibronectin and the epidermolysis bullosa acquisita antigen.

D T Woodley, E J O'Keefe, J A McDonald, M J Reese, R A Briggaman, and W R Gammon

Article tools

Metrics

Go to

Specific affinity between fibronectin and the epidermolysis bullosa acquisita antigen.

D T Woodley, E J O'Keefe, J A McDonald, M J Reese, R A Briggaman, and W R Gammon

Article tools

Metrics

Go to

Sign up for email alerts