骨调节素调节胶原纤维的直径并改变其形状。
Osteomodulin regulates diameter and alters shape of collagen fibrils.
作者信息
Tashima Takumi, Nagatoishi Satoru, Sagara Hiroshi, Ohnuma Shin-Ichi, Tsumoto Kouhei
机构信息
Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan; Department of Bioengineering, School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8654, Japan.
出版信息
Biochem Biophys Res Commun. 2015 Jul 31;463(3):292-6. doi: 10.1016/j.bbrc.2015.05.053. Epub 2015 May 20.
Osteomodulin (OMD) is a member of the small leucine-rich repeat proteoglycan family, which is involved in the organization of the extracellular matrix. OMD is located in bone tissue and is reportedly important for bone mineralization. However, the details of OMD function in bone formation are poorly understood. Using the baculovirus expression system, we produced recombinant human OMD and analyzed its interaction with type I collagen, which is abundant in bone. In this result, OMD directly interacted with purified immobilized collagen and OMD suppressed collagen fibril formation in a turbidity assay. Morphological analysis of collagen in the presence or absence of OMD demonstrated that OMD reduces the diameter and changes the shape of collagen fibrils. We conclude that OMD regulates the extracellular matrix during bone formation.
骨调节素（OMD）是富含亮氨酸的小分子重复序列蛋白聚糖家族的成员，参与细胞外基质的组织。OMD位于骨组织中，据报道对骨矿化很重要。然而，人们对OMD在骨形成中的功能细节了解甚少。我们利用杆状病毒表达系统制备了重组人OMD，并分析了它与骨中丰富的I型胶原的相互作用。结果显示，OMD与纯化的固定化胶原直接相互作用，并且在比浊分析中OMD抑制了胶原纤维的形成。有无OMD存在时对胶原的形态学分析表明，OMD减小了胶原纤维的直径并改变了其形状。我们得出结论，OMD在骨形成过程中调节细胞外基质。
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