A study on dentin proteoglycans as substrates for dentin 59KD protease.

DOI 1 Citations
  • Saito Masahiro
    Department of Restrative Dentistry School of Kanagawa Dental Collage
  • Mukai Yoshiharu
    Department of Restrative Dentistry School of Kanagawa Dental Collage
  • Tomiyama Kiyoshi
    Department of Restrative Dentistry School of Kanagawa Dental Collage
  • Teranaka Toshio
    Department of Restrative Dentistry School of Kanagawa Dental Collage
  • Iwamoto Tsugio
    Department of Restrative Dentistry School of Kanagawa Dental Collage
  • Kubota Takao
    Department of Orthodontics School of Kanagawa Dental Collage
  • Sato Sadao
    Department of Orthodontics School of Kanagawa Dental Collage
  • Suzuki Yoshii
    Department of Orthodontics School of Kanagawa Dental Collage

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  • ５９ＫＤプロテアーゼの基質となる象牙質中のプロテオグリカンに関する研究

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Abstract

We have reported that the dentin 59KD protease (59K P-ase) has MMP-3 (stromelysin)-like activity. The purpose of this study was to extract native dentin proteoglycans (PGs) and to study their degradation by the 59K P-ase. Crude PGs were extracted from the bovine dentin with sequential procedures by using 4M GuHCl (Gl-ext), 0.5MEDTA (E-ext) and 4M GuHCl (G2-ext). Partially purified PGs were obtained from each extract, by DEAE Sephacel, Superose 6 and Reversed phased FPLC. These PGs have apparent molecular weights of Gl-ext: 150-180KD and 300KD, E-ext: 130-150KD, G2-ext: 130-150KD and 180-210KD on SDS/PAGE electrophoresis. The 59K P-ase degraded all of these proteoglycans. It is apparent that the E-ext proteoglycan has several core proteins which were stained blue with Stains-all and these core proteins were cleaved by 59K P-ase. These results demonstrate that the several kinds of different molecular weight mineral binding PGs exist in dentin and 59 K P-ase has MMP-3 like activity, therefore 59 K P-ase may play an important role in the processes of mineralization and maturation of dentin.

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