Byers P H, Siegel R C, Holbrook K A, Narayanan A S, Bornstein P, Hall J G
N Engl J Med. 1980 Jul 10;303(2):61-5. doi: 10.1056/NEJM198007103030201.
We studied several members of a family with an X-linked form of cutis laxa; the affected males have mild skin laxity, a characteristic facies, skeletal abnormalities, structural abnormalities of the genitourinary tract, and low serum copper levels. The activity of lysyl oxidase, a copper-dependent enzyme involved in cross-link formation in collagen, was decreased in skin-biopsy specimens (13 to 26 per cent of normal) and in culture medium from cells to two affected males (15 to 20 per cent of normal). Immunoreactive lysyl oxidase from skin of both patients was virtually undetectable by immunodiffusion assay. The amounts of lysyl-derived aldehydes (the product formed in collagen and elastin by lysyl oxidase) and of cross-links formed from these products were decreased in dermal fibroblasts in culture. Collagen extractability from these cells was increased in culture. These findings suggest that lysyl oxidase deficiency provides the biochemical basis of the X-linked form of cutis laxa.
我们研究了一个患有X连锁型皮肤松弛症的家族中的几名成员；受影响的男性有轻度皮肤松弛、特征性面容、骨骼异常、泌尿生殖道结构异常以及血清铜水平低。赖氨酰氧化酶是一种参与胶原蛋白交联形成的铜依赖性酶，其活性在皮肤活检标本（为正常水平的13%至26%）以及来自两名受影响男性细胞的培养基中（为正常水平的15%至20%）均降低。通过免疫扩散测定，两名患者皮肤中的免疫反应性赖氨酰氧化酶几乎检测不到。培养的真皮成纤维细胞中，赖氨酰衍生醛（赖氨酰氧化酶在胶原蛋白和弹性蛋白中形成的产物）的量以及由这些产物形成的交联量均减少。这些细胞的胶原蛋白提取率在培养中增加。这些发现表明，赖氨酰氧化酶缺乏为X连锁型皮肤松弛症提供了生化基础。
