Nuytinck L, Narcisi P, Nicholls A, Renard J P, Pope F M, De Paepe A
Centre for Medical Genetics, University of Gent, Belgium.
J Med Genet. 1992 Jun;29(6):375-80. doi: 10.1136/jmg.29.6.375.
The clinical and biochemical observations in a patient with a mild form of Ehlers-Danlos syndrome (EDS) type IV are described. The patient's skin fibroblasts produced markedly diminished amounts of type III collagen. SDS-polyacrylamide gel electrophoresis of collagens produced by cells obtained from other, non-cutaneous tissues showed two forms of collagen alpha 1(III) chains, a normal and a slow migrating, mutant form. Further analysis confirmed that the type III collagen molecules containing mutant alpha chains which were overmodified had a lower thermal stability and were poorly secreted into the extracellular medium. The protein defect was mapped by in situ cyanogen bromide digestion and was located in alpha 1(III) CB9, the C-terminal peptide of the collagen triple helix. This study shows that non-cutaneous connective tissues can be a useful source for the study of type III collagen defects in patients with EDS type IV.
本文描述了一名患有轻度IV型埃勒斯-当洛综合征（EDS）患者的临床和生化观察结果。患者的皮肤成纤维细胞产生的III型胶原蛋白量明显减少。对取自其他非皮肤组织的细胞所产生的胶原蛋白进行十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示，存在两种形式的胶原蛋白α1(III)链，一种正常，另一种迁移缓慢的突变形式。进一步分析证实，含有过度修饰的突变α链的III型胶原蛋白分子热稳定性较低，且分泌到细胞外介质中的量很少。通过原位溴化氰消化对蛋白质缺陷进行定位，结果表明该缺陷位于胶原蛋白三螺旋的C末端肽α1(III)CB9中。本研究表明，非皮肤结缔组织可作为研究IV型EDS患者III型胶原蛋白缺陷的有用来源。
