title: Osteomodulin regulates diameter and alters shape of collagen fibrils.
abstract: 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.
authors.affiliation: Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. Electronic address: 8940109675@mail.ecc.u-tokyo.ac.jp.
authors.forename: Takumi
authors.initials: T
authors.lastname: Tashima
authors.affiliation: 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. Electronic address: nagatoishi@bioeng.t.u-tokyo.ac.jp.
authors.forename: Satoru
authors.initials: S
authors.lastname: Nagatoishi
authors.affiliation: Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. Electronic address: sagara.hiroshi@gmail.com.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Sagara
authors.affiliation: Institute of Ophthalmology, University College London (UCL), 11-43 Bath Street, London EC1V 9EL, UK. Electronic address: s.ohnuma@ucl.ac.uk.
authors.forename: Shin-Ichi
authors.initials: S
authors.lastname: Ohnuma
authors.affiliation: 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; Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. Electronic address: tsumoto@bioeng.t.u-tokyo.ac.jp.
authors.forename: Kouhei
authors.initials: K
authors.lastname: Tsumoto
mesh_terms: D024042:Collagen Type I / Q000378:metabolism* / Q000648:ultrastructure*; D005109:Extracellular Matrix / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011509:Proteoglycans / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D024042:Collagen Type I; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D011994:Recombinant Proteins; C113360:osteoadherin
keywords: Bone; Collagen fibril; Extracellular matrix; Fibril diameter; Fibril shape; Osteomodulin