Bone Induction in Intramuscular Implants by Demineralized Bone Matrix: Sequential Changes of Collagen Synthesis

Irvin A. Guterman , Thomas E. Boman , Gwo-Jaw Wang , Gary Balian
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引用次数: 14

Abstract

Implantation of rat demineralized bone matrix into intramuscular pouches has beenshown to cause a complex cellular transition of mesenchymal-type cells into well developed mature bone. Demineralized bone matrix was surgically implanted into rat muscle pouches and removed at various intervals between 7 and 28 days. Histological sections of the implants revealed bone formation by endochondral ossification and appositional bone growth. Biochemical analysis of collagen synthesis demonstrated the following: (1) synthesis of type X collagen, a collagen produced by hypertrophic chondrocytes in the growth plate and in fracture callus. (2) Synthesis of a collagenase-sensitive 17k protein which seems to increase in the early stages of bone induction. Pulse chase analysis indicates that 17k is not a degradation product of another protein and appears to be synthesized without a large Mr precursor. The 17k component contains one or more collagenous domains that are partially resistant to proteolysis with pepsin. Our results confirm the appearance of a cartilage intermediate during demineralized bone matrix induced ossification and implicate the existence of proteins which may be useful markers in future studies on matrix mineralization and ossification.

脱矿骨基质诱导肌内植入物成骨:胶原合成的顺序变化
将大鼠脱矿骨基质植入肌内囊可引起间充质型细胞向发育良好的成熟骨的复杂细胞转化。将脱矿骨基质手术植入大鼠肌肉囊内,每隔7 ~ 28天取出一次。种植体的组织学切片显示软骨内成骨和骨生长。胶原合成的生化分析表明:(1)X型胶原的合成,这是一种由生长板和骨折愈伤组织中的肥大软骨细胞产生的胶原。(2)胶原酶敏感蛋白17k的合成,该蛋白似乎在骨诱导的早期阶段增加。脉冲追踪分析表明,17k不是另一种蛋白质的降解产物,似乎在合成时没有一个大的Mr前体。17k成分包含一个或多个胶原结构域,这些结构域部分抵抗胃蛋白酶的蛋白水解。我们的研究结果证实了脱矿化骨基质诱导骨化过程中软骨中间体的出现,并暗示了蛋白质的存在,这可能是未来研究基质矿化和骨化的有用标记。
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