Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Synovial Fluids of Patients with Temporomandibular Joint Osteoarthritis

Manabu Kanyama, Takuo Kuboki, Shunji Kojima, Takuo Fujisawa, Takako Hattori, Masaharu Takigawa, Atsushi Yamashita

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Aims: Imbalance between matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) may be involved in the breakdown of articular cartilage matrix of the temporomandibular joint (TMJ). Aims: In this study, MMPs, TIMPs, and MMP-1/TIMP-1 complex levels were examined in TMJ synovial fluid samples aspirated from TMJ osteoarthritis (OA) patients (2 males, 8 females; mean age, 29.7 years) and asymptomatic control subjects (2 males, 8 females; mean age, 23.6 years) to determine the likelihood of increased proteolytic activity in the OA joints. Methods: The various types of MMPs and TIMPs were detected by Western blotting with monoclonal antibodies and gelatin zymography. The MMP-1/ TIMP-1 complex level was measured by an enzyme-linked immunosorbent assay kit. All aspirates were first analyzed for total protein content and then individually diluted to make the total protein levels equivalent. Results: The mean MMP-1/TIMP-1 complex concentration in the synovial fluids of the OA patients was 3.92 ± 1.39 ng/mL; this value was significantly lower (P <0.05) than the value from control subjects (5.46 ± 1.32 ng/mL). Matrix metalloproteinase-1 (52 kDa), MMP-3 (57 kDa), TIMP-1 (28 kDa), and TIMP-2 (26 kDa) were detected in all of the normal and the OA samples. However, MMP-1 (28 kDa), MMP-2 (72 kDa), MMP-3 (45 kDa), and MMP-9 (83 kDa) were detected in higher concentration in the OA samples. Conclusion: These findings suggest a strong association between the OA-active joints and the presence of biologically active forms of known tissue degradation enzymes (MMP-1, MMP-3, and MMP-9).

Original languageEnglish
Pages (from-to)20-30
Number of pages11
JournalJournal of Orofacial Pain
Volume14
Issue number1
Publication statusPublished - 2000

Fingerprint

Tissue Inhibitor of Metalloproteinases
Matrix Metalloproteinase 1
Matrix Metalloproteinase Inhibitors
Synovial Fluid
Temporomandibular Joint
Osteoarthritis
Tissue Inhibitor of Metalloproteinase-1
Matrix Metalloproteinase 3
Matrix Metalloproteinase 9
Matrix Metalloproteinases
Joints
Tissue Inhibitor of Metalloproteinase-2
Matrix Metalloproteinase 2
Articular Cartilage
Gelatin
Proteins
Western Blotting
Enzyme-Linked Immunosorbent Assay
Monoclonal Antibodies
Enzymes

Keywords

  • Matrix metalloproteinase
  • Osteoarthritis
  • Synovial fluid
  • Temporomandibular joint
  • Tissue inhibitor of metalloproteinase

ASJC Scopus subject areas

  • Clinical Neurology
  • Dentistry(all)

Cite this

Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Synovial Fluids of Patients with Temporomandibular Joint Osteoarthritis. / Kanyama, Manabu; Kuboki, Takuo; Kojima, Shunji; Fujisawa, Takuo; Hattori, Takako; Takigawa, Masaharu; Yamashita, Atsushi.

In: Journal of Orofacial Pain, Vol. 14, No. 1, 2000, p. 20-30.

Research output: Contribution to journalArticle

@article{7ac8bbd8851549f08ea06d21100bbb1f,
title = "Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Synovial Fluids of Patients with Temporomandibular Joint Osteoarthritis",
abstract = "Aims: Imbalance between matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) may be involved in the breakdown of articular cartilage matrix of the temporomandibular joint (TMJ). Aims: In this study, MMPs, TIMPs, and MMP-1/TIMP-1 complex levels were examined in TMJ synovial fluid samples aspirated from TMJ osteoarthritis (OA) patients (2 males, 8 females; mean age, 29.7 years) and asymptomatic control subjects (2 males, 8 females; mean age, 23.6 years) to determine the likelihood of increased proteolytic activity in the OA joints. Methods: The various types of MMPs and TIMPs were detected by Western blotting with monoclonal antibodies and gelatin zymography. The MMP-1/ TIMP-1 complex level was measured by an enzyme-linked immunosorbent assay kit. All aspirates were first analyzed for total protein content and then individually diluted to make the total protein levels equivalent. Results: The mean MMP-1/TIMP-1 complex concentration in the synovial fluids of the OA patients was 3.92 ± 1.39 ng/mL; this value was significantly lower (P <0.05) than the value from control subjects (5.46 ± 1.32 ng/mL). Matrix metalloproteinase-1 (52 kDa), MMP-3 (57 kDa), TIMP-1 (28 kDa), and TIMP-2 (26 kDa) were detected in all of the normal and the OA samples. However, MMP-1 (28 kDa), MMP-2 (72 kDa), MMP-3 (45 kDa), and MMP-9 (83 kDa) were detected in higher concentration in the OA samples. Conclusion: These findings suggest a strong association between the OA-active joints and the presence of biologically active forms of known tissue degradation enzymes (MMP-1, MMP-3, and MMP-9).",
keywords = "Matrix metalloproteinase, Osteoarthritis, Synovial fluid, Temporomandibular joint, Tissue inhibitor of metalloproteinase",
author = "Manabu Kanyama and Takuo Kuboki and Shunji Kojima and Takuo Fujisawa and Takako Hattori and Masaharu Takigawa and Atsushi Yamashita",
year = "2000",
language = "English",
volume = "14",
pages = "20--30",
journal = "Journal of Orofacial Pain",
issn = "1064-6655",
publisher = "Quintessence Publishing Company",
number = "1",

}

TY - JOUR

T1 - Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Synovial Fluids of Patients with Temporomandibular Joint Osteoarthritis

AU - Kanyama, Manabu

AU - Kuboki, Takuo

AU - Kojima, Shunji

AU - Fujisawa, Takuo

AU - Hattori, Takako

AU - Takigawa, Masaharu

AU - Yamashita, Atsushi

PY - 2000

Y1 - 2000

N2 - Aims: Imbalance between matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) may be involved in the breakdown of articular cartilage matrix of the temporomandibular joint (TMJ). Aims: In this study, MMPs, TIMPs, and MMP-1/TIMP-1 complex levels were examined in TMJ synovial fluid samples aspirated from TMJ osteoarthritis (OA) patients (2 males, 8 females; mean age, 29.7 years) and asymptomatic control subjects (2 males, 8 females; mean age, 23.6 years) to determine the likelihood of increased proteolytic activity in the OA joints. Methods: The various types of MMPs and TIMPs were detected by Western blotting with monoclonal antibodies and gelatin zymography. The MMP-1/ TIMP-1 complex level was measured by an enzyme-linked immunosorbent assay kit. All aspirates were first analyzed for total protein content and then individually diluted to make the total protein levels equivalent. Results: The mean MMP-1/TIMP-1 complex concentration in the synovial fluids of the OA patients was 3.92 ± 1.39 ng/mL; this value was significantly lower (P <0.05) than the value from control subjects (5.46 ± 1.32 ng/mL). Matrix metalloproteinase-1 (52 kDa), MMP-3 (57 kDa), TIMP-1 (28 kDa), and TIMP-2 (26 kDa) were detected in all of the normal and the OA samples. However, MMP-1 (28 kDa), MMP-2 (72 kDa), MMP-3 (45 kDa), and MMP-9 (83 kDa) were detected in higher concentration in the OA samples. Conclusion: These findings suggest a strong association between the OA-active joints and the presence of biologically active forms of known tissue degradation enzymes (MMP-1, MMP-3, and MMP-9).

AB - Aims: Imbalance between matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) may be involved in the breakdown of articular cartilage matrix of the temporomandibular joint (TMJ). Aims: In this study, MMPs, TIMPs, and MMP-1/TIMP-1 complex levels were examined in TMJ synovial fluid samples aspirated from TMJ osteoarthritis (OA) patients (2 males, 8 females; mean age, 29.7 years) and asymptomatic control subjects (2 males, 8 females; mean age, 23.6 years) to determine the likelihood of increased proteolytic activity in the OA joints. Methods: The various types of MMPs and TIMPs were detected by Western blotting with monoclonal antibodies and gelatin zymography. The MMP-1/ TIMP-1 complex level was measured by an enzyme-linked immunosorbent assay kit. All aspirates were first analyzed for total protein content and then individually diluted to make the total protein levels equivalent. Results: The mean MMP-1/TIMP-1 complex concentration in the synovial fluids of the OA patients was 3.92 ± 1.39 ng/mL; this value was significantly lower (P <0.05) than the value from control subjects (5.46 ± 1.32 ng/mL). Matrix metalloproteinase-1 (52 kDa), MMP-3 (57 kDa), TIMP-1 (28 kDa), and TIMP-2 (26 kDa) were detected in all of the normal and the OA samples. However, MMP-1 (28 kDa), MMP-2 (72 kDa), MMP-3 (45 kDa), and MMP-9 (83 kDa) were detected in higher concentration in the OA samples. Conclusion: These findings suggest a strong association between the OA-active joints and the presence of biologically active forms of known tissue degradation enzymes (MMP-1, MMP-3, and MMP-9).

KW - Matrix metalloproteinase

KW - Osteoarthritis

KW - Synovial fluid

KW - Temporomandibular joint

KW - Tissue inhibitor of metalloproteinase

UR - http://www.scopus.com/inward/record.url?scp=0034572272&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034572272&partnerID=8YFLogxK

M3 - Article

VL - 14

SP - 20

EP - 30

JO - Journal of Orofacial Pain

JF - Journal of Orofacial Pain

SN - 1064-6655

IS - 1

ER -