Osteomodulin regulates diameter and alters shape of collagen fibrils

Biochem Biophys Res Commun. 2015 Jul 31;463(3):292-6. doi: 10.1016/j.bbrc.2015.05.053. Epub 2015 May 20.

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.

Keywords: Bone; Collagen fibril; Extracellular matrix; Fibril diameter; Fibril shape; Osteomodulin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Collagen Type I / metabolism*
  • Collagen Type I / ultrastructure*
  • Extracellular Matrix / metabolism
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Protein Binding
  • Proteoglycans / metabolism*
  • Recombinant Proteins / metabolism

Substances

  • Collagen Type I
  • Extracellular Matrix Proteins
  • Proteoglycans
  • Recombinant Proteins
  • osteoadherin