van der Sluijs J A, Pruys J E
Department of Orthopaedics, Academic Hospital of the Free University, Amsterdam, The Netherlands.
J Pediatr Orthop B. 1999 Oct;8(4):261-3.
In 21 clubfeet (17 children) of different types (idiopathic, spina bifida, syndromal), the authors analyzed modifications and crosslinks in collagen and their possible relations with clinical stiffness of clubfoot deformity, as measured by the Dimeglio/Bensahel method. In a biopsy of the capsule of the ankle joint, the number of hydroxylysine residues (mean +/- standard deviation; 27.1 +/- 3.4) and the number of pyridinium crosslinks per collagen molecule (0.41 +/- 0.12) were normal. This indicates normal processing of collagen molecules and normal alignment of collagen molecules within fibrils despite the variety of clubfeet, and even in scar tissue.
在21例不同类型（特发性、脊柱裂、综合征性）的马蹄内翻足（17名儿童）中，作者分析了胶原蛋白的修饰和交联情况，以及它们与马蹄内翻足畸形临床僵硬程度的可能关系（采用Dimeglio/Bensahel方法测量）。在踝关节囊活检中，羟赖氨酸残基数量（平均值±标准差；27.1±3.4）和每个胶原蛋白分子的吡啶交联数量（0.41±0.12）均正常。这表明尽管马蹄内翻足类型多样，甚至在瘢痕组织中，胶原蛋白分子的加工过程正常，且胶原蛋白分子在原纤维内排列正常。
