Grant W T, Wang G J, Balian G
J Biol Chem. 1987 Jul 15;262(20):9844-9.
Collagen synthesis in normal connective tissue development and repair is integral to tissue stability. The appearance of a short chain collagen, designated Type X, was studied in experimental fractures created in the chicken humerus. Biosynthetic studies using [14C]proline incorporation coupled with histologic examination of the cartilaginous callus demonstrated that Type X collagen synthesis occurs during endochondral ossification in the fracture callus. Type X synthesis occurred in the areas of cartilaginous callus composed of hypertrophic and degenerative chondrocytes that were associated with increased vascularity and matrix mineralization. Synthesis of short chain collagen was not detected in either skeletal muscle or bone. Two-dimensional peptide mapping of cyanogen bromide and proteolytic fragments derived from fracture callus short chain collagen confirmed the identity of this collagen as Type X. The synthesis of Type X collagen by fracture callus is further evidence supporting its close association with the process of endochondral ossification.
在正常结缔组织发育和修复过程中,胶原蛋白的合成对于组织稳定性至关重要。在鸡肱骨实验性骨折中,对一种名为X型的短链胶原蛋白的出现情况进行了研究。利用[14C]脯氨酸掺入进行的生物合成研究,结合对软骨痂的组织学检查表明,X型胶原蛋白的合成发生在骨折痂的软骨内成骨过程中。X型胶原蛋白的合成发生在由肥大和退变软骨细胞组成的软骨痂区域,这些区域伴有血管增多和基质矿化。在骨骼肌或骨骼中均未检测到短链胶原蛋白的合成。对来自骨折痂短链胶原蛋白的溴化氰和蛋白水解片段进行二维肽图谱分析,证实了这种胶原蛋白为X型。骨折痂合成X型胶原蛋白进一步证明了它与软骨内成骨过程密切相关。