Galicka Anna, Wolczynski Slawomir, Gindzienski Andrzej
Department of General and Organic Chemistry, Medical Academy, 15-230 Bialystok 8, Poland.
J Pathol. 2002 Feb;196(2):235-7. doi: 10.1002/path.1030.
The expression of type I collagen has been compared in fibroblast and osteoblast cultures of a patient with moderately severe osteogenesis imperfecta (OI) type IV, with respect to control cells. Electrophoretic analysis of type I collagen showed that both OI osteoblasts and fibroblasts synthesized normal chains and chains with delayed migration. However, the osteoblasts contained a higher proportion of abnormal chains than fibroblasts from the proband. Pulse-chase experiments showed that the trimers containing abnormal chains were cleared more rapidly from osteoblasts than fibroblasts. Moreover, the collagen secreted by OI osteoblasts had thermal stability 1 degrees C higher than collagen secreted by OI fibroblasts. These results suggest that the abnormal collagen in osteoblasts may be more resistant to intra- and extracellular degradation and may thus have better survival than in fibroblasts. This finding could have implications for understanding the clinical phenotype of OI.
在一名患有中度严重IV型成骨不全症（OI）患者的成纤维细胞和成骨细胞培养物中，对I型胶原蛋白的表达与对照细胞进行了比较。I型胶原蛋白的电泳分析表明，OI成骨细胞和成纤维细胞均合成正常链和迁移延迟的链。然而，成骨细胞中异常链的比例高于先证者的成纤维细胞。脉冲追踪实验表明，含有异常链的三聚体从成骨细胞中清除的速度比成纤维细胞更快。此外，OI成骨细胞分泌的胶原蛋白的热稳定性比OI成纤维细胞分泌的胶原蛋白高1摄氏度。这些结果表明，成骨细胞中的异常胶原蛋白可能对细胞内和细胞外降解更具抗性，因此可能比成纤维细胞中的胶原蛋白具有更好的存活率。这一发现可能对理解OI的临床表型具有重要意义。
