Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 463, Issue 3, Pages 292-296Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.05.053
Keywords
Osteomodulin; Collagen fibril; Fibril diameter; Fibril shape; Extracellular matrix; Bone
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Funding
- Japan Society for the Promotion of Science [25249115]
- Great Britain Sasakawa Foundation
- Grants-in-Aid for Scientific Research [25249115] Funding Source: KAKEN
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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. (C) 2015 Elsevier Inc. All rights reserved.
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