Woodley D T, O'Keefe E J, McDonald J A, Reese M J, Briggaman R A, Gammon W R
J Clin Invest. 1987 Jun;79(6):1826-30. 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.
获得性大疱性表皮松解症患者皮肤和血清中的自身抗体与皮肤基底膜致密层区域内的一种大型基质分子结合。在这些免疫复合物的部位，表皮与真皮分离，在致密层下方形成一个表皮下水疱。自身抗体的靶分子与纤连蛋白紧密相邻，纤连蛋白是一种主要的细胞外基质分子，在皮肤真皮上层中含量丰富。在本报告中，我们展示了纤连蛋白与获得性大疱性表皮松解症抗原的290,000-D链之间的特异性亲和力，并且这种亲和力是由纤连蛋白的明胶/胶原结合结构域（Mr = 60,000）介导的。由于获得性大疱性表皮松解症中的水疱形成通常在没有临床和组织学炎症的情况下发生，纤连蛋白与获得性大疱性表皮松解症抗原之间的键的直接中断可能参与了这种大疱性疾病中发生的表皮-真皮分离的发病机制。
