Journal of Oral and Maxillofacial Surgery
Volume 67, Issue 1 , Pages 105-113, January 2009

Analysis of the Collagen I and Fibronectin of Temporomandibular Joint Synovial Fluid and Discs

  • Joseph R. Natiella, DDS

      Affiliations

    • Professor Emeritus, Department of Oral Diagnostic Sciences, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY
  • ,
  • Lindsay Burch

      Affiliations

    • Student, Daemen College, Amherst, NY
  • ,
  • Kristin M. Fries

      Affiliations

    • Associate Professor, Daemen College, Amherst, NY
  • ,
  • L. George Upton, DDS, MS

      Affiliations

    • Professor, Department of Oral and Maxillofacial Surgery, and Surgical Director, TMD/Orofacial Pain Clinic, University of Michigan, Ann Arbor, MI
  • ,
  • Laura E. Edsberg, PhD

      Affiliations

    • Director, Center for Wound Healing Research, Natural & Health Sciences Research Center, and Associate Professor, Daemen College, Amherst, NY
    • Corresponding Author InformationAddress correspondence and reprint requests to Dr Edsberg: Center for Wound Healing Research, Natural & Health Sciences Research Center, Daemen College, 4380 Main St, Amherst, NY 14226

Purpose

The objective of this study was to investigate the content of synovial fluid aspirates and temporomandibular joint (TMJ) disc tissue for collagen I and total fibronectin in patients with closed lock. Fibronectin contains dual properties of assisting with wound healing and inducing cartilage degradation. Native fibronectin has been shown to assist with wound repair, whereas particular fibronectin fragments may degrade cartilage. In addition, collagen I is the major supporting protein of the TMJ disc and will degrade as osteoarthritis progresses. Fibronectin or collagen I expression in human TMJ synovial aspirates and disc tissue may indicate the proteins' involvement in closed lock. The hypothesis of this study is that TMJ discs and serum of patients with closed lock will contain an increased amount of fibronectin and decreased amount of collagen I.

Materials and Methods

We analyzed a total of 8 diseased TMJ discs and 4 diseased synovial fluid aspirates. For our control samples, we assessed 5 synovial samples from healthy patients and control skin samples. Using an enzyme-linked immunosorbent assay allowed us to measure the total amount of fibronectin and collagen I in synovial aspirates. Furthermore, we used light microscopy to assess TMJ disc histology and collagen architecture in control skin samples. Lastly, using fluorescent staining, we examined fibronectin and collagen I expression in TMJ discs. We compared the fluorescent staining and light microscopy results of both proteins within each disc to confirm fibronectin and collagen I expression.

Results

Disc specimens with advanced morphologic pathology showed significant labeling for fibronectin in 3 of 3 cases and for collagen I in 4 of 4 cases. There was no considerable difference in detection of either fibronectin or collagen I in TMJ synovial aspirates from patients with advanced disc pathology compared with controls.

Conclusions

The levels of fibronectin and collagen I in the TMJ disc and synovial fluid may be influenced by the stage of disease. The results did not provide a clear understanding of fibronectin and collagen I involvement with tissue repair in closed-lock cases. Detection of fibronectin fragments may provide more meaningful results.

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PII: S0278-2391(08)01468-7

doi:10.1016/j.joms.2008.08.029

Journal of Oral and Maxillofacial Surgery
Volume 67, Issue 1 , Pages 105-113, January 2009