Messenger ribonucleic acid expression of 16 matrix metalloproteinases in bone-implant interface tissues of loose

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I Takei1, M Takagi, S Santavirta

  • 1Department of Orthopedic Surgery, Yamagata University School of Medicine, 2-2-2 Iida-Nishi, Yamagata 990-9585, Japan. isaotake@hospital.sakata.yamogata.jp

Journal of Biomedical Materials Research
|October 18, 2000
PubMed

Insights

Matrix metalloproteinases (MMPs) contribute to artificial hip joint loosening. This study analyzed 16 MMPs, finding elevated levels of specific MMPs in loose joints, suggesting their role in prosthetic failure.

Area of Science:

  • Biomedical Engineering
  • Orthopedic Surgery
  • Molecular Biology

Background:

  • Aseptic loosening of artificial hip joints is a significant clinical problem.
  • Matrix metalloproteinases (MMPs) are implicated in prosthetic loosening.
  • The mRNA expression of many MMPs in this context remains uncharacterized.

Purpose of the Study:

  • To investigate the mRNA expression patterns of 16 different MMPs in aseptic loose artificial hip joints.
  • To identify specific MMPs locally produced and contributing to prosthetic loosening.
  • To understand the role of MMPs in periprosthetic tissue remodeling and osteolysis.

Main Methods:

  • Analysis of synovium-like interface tissues from 18 aseptic loose hip joints and 6 normal controls.
  • RNA extraction using the acid guanidinium-thiocyanate-phenol-chloroform method.
  • Semiquantitative reverse transcription-polymerase chain reaction (RT-PCR) to analyze MMP mRNA expression.

Main Results:

  • Elevated mRNA expression of MMP-1, MMP-9, MMP-10, MMP-12, and MMP-13 was observed in loose joints.
  • Moderate expression of MMP-2, MMP-7, MMP-8, MMP-11, and several membrane-type MMPs (MMP-14 to MMP-17, MMP-19) was detected.
  • Lower expression of MMP-3 and minimal significance of MMP-20 were noted.

Conclusions:

  • A wide range of MMPs are locally expressed in aseptic loose artificial hip joints.
  • Specific MMPs, particularly those with elevated expression, likely contribute to prosthetic loosening.
  • These MMPs may drive osteolysis and tissue remodeling through extracellular matrix degradation.

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