On the High Collagen-Affinity Proteins in Bone and Their Characterisitics

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  • Murakami Koji
    Graduate School of Science and Engineering, Aoyama Gakuin University
  • Sai Tomoaki
    Department of Orthopaedic Surgery, The Jikei University School of Medicine
  • Hamamoto Yoko
    Department of Nursing, National College of Nursing
  • Ito Hisashi
    Graduate School of Science and Engineering, Aoyama Gakuin University
  • Yonemoto Kyozo
    Graduate School of Health Sciences, Tokyo Metropolitan University of Health Sciences
  • Kasai Hisataka
    Graduate School of Health Sciences, Tokyo Metropolitan University of Health Sciences:Graduate School of Applied Chemistry and Chemical Engineering, Kogakuin University

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  • 骨形成に関与するコラーゲン高親和性タンパク質の精製とその特徴づけ
  • ホネ ケイセイ ニ カンヨ スル コラーゲン コウシンワセイ タンパクシツ ノ セイセイ ト ソノ トクチョウズケ

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Abstract

Calcium deposition on the major collagen matrices occurs in the process of bone formation and is delicately controlled by a number of noncollagenous proteins. We intend to search for new acidic bone proteins which have a high affinity for collagen and to apply the new proteins to a possible rehabilitation method for bone regeneration. We have detected a trace of acidic proteins with high affinity for collagen in the acetic acid extract of bovine femoral cortical bone. In this report, we adopted acetic acid-decalcification method to search for the new proteins and compared it with various other decalcification methods. The acidic proteins in the acetate-soluble fraction were partially purified from an excess amount of collagen after digestion using bacterial collagenase. Several acidic proteins and cross-linked N-telopeptide of type I collagen were detected in the fraction. The acidic proteins, which are rich in Asp or Glu, were similar to acidic noncollagenous proteins such as osteopontin or BSP in amino acid compositions, but did not agree with them in N-terminal sequences. These results suggest that the acidic proteins are different from the already-known noncollagenous proteins.

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