Halila R, Steinmann B, Peltonen L
Am J Hum Genet. 1986 Aug;39(2):222-31.
The processing of types I and III procollagen was studied in skin fibroblast cultures from type VII A and B of the Ehlers-Danlos syndrome [EDS] and age-matched controls. Synthesis of collagenous proteins was significantly increased in EDS type VII B, and the activities of prolyl-4-hydroxylase and galactosylhydroxylysyl glucosyltransferase were slightly increased in these cell lines, reflecting increased biosynthesis of collagen. The synthesis of collagenous proteins was close to normal in EDS type VII A cells. The synthesis of type III procollagen per cell was increased, as also was the ratio of immunoreactive type III procollagen to total collagen production. The activity of type I procollagen amino-terminal proteinase was decreased in skin fibroblasts of type VII A and normal in those of type VII B relative to cell protein or DNA. Type III amino-terminal proteinase activity was of a level found in normal cells when expressed relative to the protein or DNA, and the release of type III amino-terminal propeptides was nevertheless not disturbed in these EDS type VII cell cultures. The results show that only the conversion of type I procollagen is defective in EDS type VII, and no general defect in procollagen processing can be found in EDS type VII as has been suggested in the case of dermatosparaxis, a connective tissue disorder in animals caused by disturbed procollagen conversion.
在来自埃勒斯-当洛综合征（EDS）VII A型和VII B型以及年龄匹配对照的皮肤成纤维细胞培养物中，研究了I型和III型前胶原的加工过程。VII B型EDS中胶原蛋白质的合成显著增加，这些细胞系中脯氨酰-4-羟化酶和半乳糖基羟赖氨酰葡糖基转移酶的活性略有增加，反映出胶原生物合成增加。VII A型EDS细胞中胶原蛋白质的合成接近正常。每个细胞中III型前胶原的合成增加，免疫反应性III型前胶原与总胶原产生的比率也增加。相对于细胞蛋白质或DNA，VII A型皮肤成纤维细胞中I型前胶原氨基端蛋白酶的活性降低，VII B型则正常。相对于蛋白质或DNA，III型氨基端蛋白酶活性处于正常细胞中的水平，然而在这些VII型EDS细胞培养物中，III型氨基端前肽的释放并未受到干扰。结果表明，在VII型EDS中只有I型前胶原的转化存在缺陷，并且在VII型EDS中未发现如动物中由前胶原转化紊乱引起的结缔组织疾病皮肤松弛症那样的前胶原加工普遍缺陷。
