Eady R A, Dunnill M G
Department of Cell Pathology, St John's Institute of Dermatology, St. Thomas's Hospital, London, UK.
Arch Dermatol Res. 1994;287(1):2-9. doi: 10.1007/BF00370710.
Recent research into the molecular basis of epidermolysis bullosa has provided a unique insight into a variety of mechanisms in normal cell biology, such as cell-matrix interactions, and has uncovered an excellent model for studies on keratin intermediate filaments. The simplex forms of epidermolysis bullosa are caused by mutations in the genes for the basal epidermal keratins, K5 and K14. Most mutations affect highly conserved parts of the molecules, illustrating their importance in normal keratin filament assembly and integrity. Mutations in corresponding regions of the differentiation-associated keratins, K1 and K10 can also occur in epidermolytic ichthyosis. Both recessive and dominant forms of dystrophic epidermolysis bullosa result from mutations in an anchoring fibril collagen gene, COL7A1. Junctional epidermolysis bullosa is caused by mutations in the genes encoding different chains of the novel laminin isoform, nicein/kalinin, also known as laminin 5, which is associated with the anchoring filament-hemidesmosome complex of the basement membrane zone. These recent findings strengthen the evidence for the role of nicein/kalinin and type VII collagen in adherence and stabilization of the dermo-epidermal junction.
近期对大疱性表皮松解症分子基础的研究,为正常细胞生物学中的多种机制(如细胞与基质的相互作用)提供了独特的见解,还发现了一个研究角蛋白中间丝的绝佳模型。大疱性表皮松解症的单纯型由基底表皮角蛋白K5和K14的基因突变引起。大多数突变影响分子中高度保守的部分,这表明它们在正常角蛋白丝组装和完整性中的重要性。在表皮松解性鱼鳞病中也可发生分化相关角蛋白K1和K10相应区域的突变。营养不良性大疱性表皮松解症的隐性和显性形式均由锚定原纤维胶原蛋白基因COL7A1的突变引起。交界性大疱性表皮松解症由编码新型层粘连蛋白异构体(巢蛋白/卡利宁,也称为层粘连蛋白5)不同链的基因突变引起,该层粘连蛋白与基底膜区的锚定丝-半桥粒复合体相关。这些最新发现进一步证明了巢蛋白/卡利宁和VII型胶原在真皮-表皮连接的黏附与稳定中的作用。