Nogami H, Oohira A
Department of Orthopaedic Surgery, Central Hospital, Aichi, Japan.
Clin Orthop Relat Res. 1988 Jul(232):284-91.
The relationship between collagen fibrils and proteoglycans in the bone matrices of three osteogenesis imperfecta (OI) patients was observed ultrastructurally to clarify the mechanism responsible for pronounced bony fragility. Collagen fibrils and noncollagenous components were prepared from the bone matrix of patients with osteogenesis imperfecta and a control sample, respectively. Compared with the control, a 95.2% decrease was found in the number of proteoglycan granules periodically associated with the cross-banding of collagen fibrils in one OI sample from a patient with severe bony fragility. Extractability of collagen fibrils and proteoglycans was high in this sample. However, proteoglycans and collagen fibrils could be reattached in vitro to reproduce the condition observed in the controls. There was no decrease in the number of proteoglycan granules attached to prepared collagen fibrils in a sample from a patient with predominantly bowing deformity of bones. Hypothetically, the separation of proteoglycans from collagen fibrils in OI may be associated with increased bony fragility. In osteogenesis imperfecta patients, the mechanism inducing bowing deformity appears to be different from that inducing fragility.
通过超微结构观察三名成骨不全（OI）患者骨基质中胶原纤维与蛋白聚糖之间的关系，以阐明导致明显骨质脆弱的机制。分别从成骨不全患者的骨基质和对照样本中制备胶原纤维和非胶原成分。与对照相比，在一名患有严重骨质脆弱的OI患者的一个样本中，与胶原纤维交叉带周期性相关的蛋白聚糖颗粒数量减少了95.2%。该样本中胶原纤维和蛋白聚糖的可提取性很高。然而，蛋白聚糖和胶原纤维在体外可以重新附着，以重现对照中观察到的情况。在一名主要表现为骨骼弯曲畸形的患者的样本中，附着在制备的胶原纤维上的蛋白聚糖颗粒数量没有减少。假设，OI中蛋白聚糖与胶原纤维的分离可能与骨质脆弱增加有关。在成骨不全患者中，导致弯曲畸形的机制似乎与导致脆弱的机制不同。
