Hui-Chou C S, Lust G
Coll Relat Res. 1982;2(3):245-56. doi: 10.1016/s0174-173x(82)80018-6.
The collagen in the degenerated articular cartilage from dysplastic canine hip joints was characterized as to type by examining cartilage directly and also after labeling cartilage slices with 14C-proline in vitro. Collagen analysis was by sodium dodecylsulfate-polyacrylamide gel electrophoresis of 14C-labeled collagen, and of 14C-peptides which had been cleaved by cyanogen bromide. Amino acid analysis was done on hydrolysates of whole cartilage and of purified collagens to quantify the ratio of hydroxyproline to hydroxylysine. Data revealed that type II collagen was the radiolabeled product synthesized in all samples of degenerated cartilage and was the only collagen detected in biochemical tests in the cartilage of joints with degenerative joint disease as well as in disease free hip joints. Results suggested that chondrocytes in degenerated cartilage of canine joints did not switch their collagen phenotype, but continued to synthesize type II collagen. Cartilage degeneration in joints of dogs with hip dysplasia proceeded without a change in collagen phenotype.
通过直接检查软骨以及在体外将软骨切片用14C - 脯氨酸标记后,对发育异常的犬髋关节退变关节软骨中的胶原蛋白进行类型鉴定。胶原蛋白分析采用对14C标记的胶原蛋白以及经溴化氰裂解后的14C肽进行十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳。对全软骨和纯化胶原蛋白的水解产物进行氨基酸分析,以量化羟脯氨酸与羟赖氨酸的比例。数据显示,II型胶原蛋白是在所有退变软骨样本中合成的放射性标记产物,并且是在患有退行性关节疾病的关节软骨以及无病髋关节软骨的生化检测中检测到的唯一胶原蛋白。结果表明,犬关节退变软骨中的软骨细胞并未改变其胶原蛋白表型,而是继续合成II型胶原蛋白。髋关节发育异常的犬关节软骨退变过程中胶原蛋白表型未发生变化。