DOI QR코드

DOI QR Code

Changes in Matrix Metalloproteinase and Tissue Inhibitors of Metalloproteinase in Patients with Rotator Cuff Tears

  • Kwon, Oh-Soo (Department of Orthopedic Surgery, The Catholic University of Korea, Daejeon St. Mary's Hospital) ;
  • Kim, Young-Yul (Department of Orthopedic Surgery, The Catholic University of Korea, Daejeon St. Mary's Hospital) ;
  • Ha, Ji Yoon (Department of Orthopedic Surgery, The Catholic University of Korea, Daejeon St. Mary's Hospital) ;
  • Kang, Han Bit (Department of Orthopedic Surgery, The Catholic University of Korea, Daejeon St. Mary's Hospital)
  • Received : 2014.02.25
  • Accepted : 2014.04.30
  • Published : 2014.06.30

Abstract

Background: The purpose of this study was to determine whether in patients with rotator cuff tears a correlation exists between molecular changes and clinical parameters such as age, duration of symptom, range of motion, and tear size. Molecular changes of matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase (TIMP) were assessed by measuring messenger RNA (mRNA) levels of the two proteins. Methods: The rotator cuff tissue from was obtained from the edge of a torn tendon revealed after debridement by a motorized shaver. Using the sample of rotator cuff tissue, the reverse transcription polymerase chain reaction was performed to quantify MMP-2 and TIMP-2 mRNA expression. To determine whether mRNA levels and the clinical variables, such as age, defect size, range of motion (ROM) of shoulder, and duration of symptoms, show any correlation, Spearman's correlation coefficients were used to test for significant differences. Results: There was an inverse correlation between the mRNA levels of MMP-2 and TIMP-2 from the torn rotator cuff tendons regardless of the clinical variables. However, comparison of mRNA levels versus clinical parameters such as age, defect size, range of motion and duration of symptoms revealed a number of findings. We found a significant correlation between age and mRNA levels of MMP-2 from torn cuffs (r = 0.513, p = 0.021). Further, we found a significant correlation between defect size in the full thickness tears and mRNA levels of MMP-2 (r = 0.454, p = 0.045). Conversely, no significant association between mRNA levels of MMP-2 and ROM or duration of symptom was found. Conclusions: Our results suggest that both MMP-2 and TIMP-2 may be involved in the disease process of rotator cuff tears. Although the level of mRNA expression of MMP-2 and TMP-2 remain constant in torn rotator cuffs irrespective of the clinical variables, their levels may be influenced by age and defect size, which could account to change in tendon degradation and the healing process.

Keywords

References

  1. Murrell GA, Walton JR. Diagnosis of rotator cuff tears. Lancet. 2001;357(9258):769-70. https://doi.org/10.1016/S0140-6736(00)04161-1
  2. Cofield RH, Parvizi J, Hoffmeyer PJ, Lanzer WL, Ilstrup DM, Rowland CM. Surgical repair of chronic rotator cuff tears. A prospective long-term study. J Bone Joint Surg Am. 2001;83-A(1):71-7.
  3. Hattrup SJ. Rotator cuff repair: relevance of patient age. J Shoulder Elbow Surg. 1995;4(2):95-100. https://doi.org/10.1016/S1058-2746(05)80061-8
  4. Jensen KL, Williams GR Jr, Russell IJ, Rockwood CA Jr. Rotator cuff tear arthropathy. J Bone Joint Surg Am. 1999;81(9):1312-24.
  5. Tetlow LC, Adlam DJ, Woolley DE. Matrix metalloproteinase and proinflammatory cytokine production by chondrocytes of human osteoarthritic cartilage: associations with degenerative changes. Arthritis Rheum. 2001;44(3):585-94. https://doi.org/10.1002/1529-0131(200103)44:3<585::AID-ANR107>3.0.CO;2-C
  6. Yoshihara Y, Nakamura H, Obata K, et al. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis. Ann Rheum Dis. 2000;59(6):455-61. https://doi.org/10.1136/ard.59.6.455
  7. Dalton S, Cawston TE, Riley GP, Bayley IJ, Hazleman BL. Human shoulder tendon biopsy samples in organ culture produce procollagenase and tissue inhibitor of metalloproteinases. Ann Rheum Dis. 1995;54(7):571-7. https://doi.org/10.1136/ard.54.7.571
  8. Bedi A, Kovacevic D, Hettrich C, et al. The effect of matrix metalloproteinase inhibition on tendon-to-bone healing in a rotator cuff repair model. J Shoulder Elbow Surg. 2010;19(3):384-91. https://doi.org/10.1016/j.jse.2009.07.010
  9. Lo IK, Marchuk LL, Hollinshead R, Hart DA, Frank CB. Matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase mRNA levels are specifically altered in torn rotator cuff tendons. Am J Sports Med. 2004;32(5):1223-9. https://doi.org/10.1177/0363546503262200
  10. Riley GP, Curry V, DeGroot J, et al. Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology. Matrix Biol. 2002;21(2):185-95. https://doi.org/10.1016/S0945-053X(01)00196-2
  11. Lakemeier S, Braun J, Efe T, et al. Expression of matrix metalloproteinases 1, 3, and 9 in differing extents of tendon retraction in the torn rotator cuff. Knee Surg Sports Traumatol Arthrosc. 2011;19(10):1760-5. https://doi.org/10.1007/s00167-010-1367-y
  12. Thornton GM, Shao X, Chung M, et al. Changes in mechanical loading lead to tendonspecific alterations in MMP and TIMP expression: influence of stress deprivation and intermittent cyclic hydrostatic compression on rat supraspinatus and Achilles tendons. Br J Sports Med. 2010;44(10):698-703. https://doi.org/10.1136/bjsm.2008.050575
  13. Choi HR, Kondo S, Hirose K, Ishiguro N, Hasegawa Y, Iwata H. Expression and enzymatic activity of MMP-2 during healing process of the acute supraspinatus tendon tear in rabbits. J Orthop Res. 2002;20(5):927-33. https://doi.org/10.1016/S0736-0266(02)00016-5
  14. Ritty TM, Herzog J. Tendon cells produce gelatinases in response to type I collagen attachment. J Orthop Res. 2003;21(3):442-50. https://doi.org/10.1016/S0736-0266(02)00200-0
  15. Castagna A, Cesari E, Gigante A, Conti M, Garofalo R. Metalloproteases and their inhibitors are altered in both torn and intact rotator cuff tendons. Musculoskelet Surg. 2013;97 Suppl 1:39-47.