Macromolecular organization of chicken type X collagen in vitro.
Macromolecular organization of chicken type X collagen in vitro.
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DOI：
10.1083/jcb.114.3.597
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发表时间：
1991-08
期刊：
影响因子：
--
通讯作者：
Grant ME
中科院分区：
文献类型：
--
作者：
Kwan AP;Cummings CE;Chapman JA;Grant ME
用免疫电子显微镜初步研究了原代培养的鸡肥大软骨细胞基质中X型胶原的大分子结构。在肥大的软骨细胞形成的基质中，X型胶原被观察到组装成一种基质样结构。用纯化的鸡X型胶原蛋白和旋转阴影EM在分子水平上研究了其自组装过程。结果表明，在34℃的中性条件下，X型胶原分子通过其羧基末端球状结构域迅速结合成多聚体，形成具有中心结节的羧基末端结构域和向外辐射的三螺旋结构。延长孵化时间导致相邻多聚体团簇中并列的三螺旋结构域侧向缔合形成规则的六方晶格。这种延伸的晶格可能在软骨基质的改变中发挥重要作用，以应对软骨内骨形成中发生的后续事件。
The macromolecular structure of type X collagen in the matrices of primary cultures of chick hypertrophic chondrocytes was initially investigated using immunoelectron microscopy. Type X collagen was observed to assemble into a matlike structure with-in the matrix elaborated by hypertrophic chondrocytes. The process of self assembly was investigated at the molecular level using purified chick type X collagen and rotary-shadowing EM. It was shown that under neutral conditions at 34 degrees C, individual type X collagen molecules associate rapidly into multimeric clusters via their carboxy-terminal globular domains forming structures with a central nodule of carboxy- terminal domains and the triple helices radiating outwards. Prolonged incubation resulted in the formation of a regular hexagonal lattice by lateral association of the juxtaposed triple-helical domains from adjacent multimeric clusters. This extended lattice may play an important role in modifying the cartilage matrix for subsequent events occurring in endochondral bone formation.