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The role of matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1) Expression in pelvic organ prolapse: A literature review

  • Amilah Anis ,
  • Eighty Mardiyan Kurniawati ,
  • Gatut Hardianto ,
  • Tri Hastono Setyohadi ,

Abstract

Link of Video Abstract: https://youtu.be/Zv9b2Zj96yk

 

Menopause is a physiological process as women get older. Urogenital syndrome, sexual difficulties, and pelvic organ prolapse (POP) are all common complaints among postmenopausal women, and these conditions can negatively impact their quality of life. There are still many unknowns regarding the pathophysiology and mechanisms of POP. Pelvic organ prolapse has been linked to the equilibrium of the extracellular matrix (ECM), which is controlled by matrix metalloproteinases and tissue inhibitors of metalloproteinases. Menopausal women experience a variety of symptoms due to hormonal changes, from urinary tract disturbance, vaginal atrophy, vaginal shortening, up to genital prolapse. Due to the collagen's diminished contractility, POP happens. Matrix metalloproteinase is responsible for breaking down collagen, but TIMP prevents MMP from doing its job. In women with POP caused by the breakdown of the collagen network, MMP-9 exhibits the greatest rise. In order to preserve the health of fibroblasts and collagen in postmenopausal women, increased expression of MMP-9 and decreased expression of TIMP-1 are necessary, which results in a decreased incidence of POP. The expression of MMP-9 in prolapse patients was significantly higher than control patients. In addition, TIMP-1 expression levels were significantly decreased in prolapse patients. Damage to the ECM's equilibrium is caused by increased MMP-9 expression and decreased expression of timp-1, which leads to clinical signs of pelvic organ prolapse.

References

  1. Soares CN. Depression and menopause: an update on current knowledge and clinical management for this critical window. Medical Clinics of North America. 2019;103(4):651–67.
  2. Pribakti B. Uroginekologi Dan Disfungsi Dasar Panggul. Kalimantan: PT Grafika Wangi. 2020; Available from: https://repo-dosen.ulm.ac.id/bitstream/handle/123456789/20415/Uroginekologi%20dan%20Disfungsi%20Dasar%20Panggul.pdf?sequence=1
  3. Gandhi J, Chen A, Dagur G, Suh Y, Smith N, Cali B, Khan SA. Genitourinary syndrome of menopause : an overview of clinical manifestations, pathophysiology, etiology, evaluation, and management. American Journal of Obstetrics and Gynecology. 2016;215(6):704–11.
  4. Zhou L, Liang Q, Li Y, Cao Y, Li J, Yang J, Liu Y. Collagenase-I decorated co-delivery micelles potentiate extracellular matrix degradation and hepatic stellate cell targeting for liver fibrosis therapy. Acta Biomaterialia. 2022;152(20):235–54.
  5. Lim NH, Meinjohanns E, Meldal M, Bou-Gharios G, Nagase H. Invivo imaging of MMP-13 activity in the murine destabilised medial meniscus surgical model of osteoarthritis. Osteoarthritis and Cartilage. 2014;22(6):862–8.
  6. Siddique SA. Vaginal anatomy and physiology. Journal of Pelvic Medicine and Surgery. 2003;9(6):263–72.
  7. Maynard RL, Downes N. Anatomy and histology of the laboratory rat in toxicology and biomedical research. Anatomy and Histology of the Laboratory Rat in Toxicology and Biomedical Research. 2019; 1–359. Available from: https://doi.org/10.1016/C2016-0-02030-2
  8. Buy JN, Ghossain M. Embryology, anatomy, and histology of the vagina. Gynecological Imaging. 2013; 685–9. Available from: https://doi.org/10.1007/978-3-642-31012-6_29
  9. Kular JK, Basu S, Sharma RI. The extracellular matrix: Structure, composition, age-related differences, tools for analysis and applications for tissue engineering. Journal of Tissue Engineering. 2014;5:204173141455711.
  10. Kusindarta DL, Wihadmadyatami H. The role of extracellular matrix in tissue regeneration. tissue regeneration. InTech. 2018. Available from: http://dx.doi.org/10.5772/intechopen.75728
  11. Baumann L, Bernstein EF, Weiss A S, Bates D, Humphrey S, Silberberg M, Daniels R. Clinical relevance of elastin in the structure and function of skin. Aesthetic Surgery Journal Open Forum. 2021;3(3):1–8.
  12. Shoulders MD, Raines RT. Collagen structure and stability. Annual Review of Biochemistry. 2009;78:929–58.
  13. Baud S, Duca L, Bochicchio, B, Brassart B, Belloy N, Pepe A, et al. Elastin peptides in aging and pathological conditions. Biomolecular Concepts. 2013;4(1):65–76.
  14. Schmelzer CEH, Hedtke T, Heinz A. Unique molecular networks: Formation and role of elastin cross-links. IUBMB Life. 2019;72(5):842–54.
  15. Alberts B, Bray D, Hopkin K, Johnson A, Lewis J, Raff M, et al. Essential Cell Biology. Third Ed. New York: Garland Science. 2010; 401.
  16. Halade GV, Jin YF, Lindsey ML. Matrix metalloproteinase (MMP)-9: a proximal biomarker for cardiac remodeling and a distal biomarker for inflammation. Pharmacology & Therapeutics. 2013;139(1):32–40.
  17. Michaluk P, Kaczmarek L. Matrix metalloproteinase-9 in glutamate-dependent adult brain function and dysfunction. Cell Death and Differentiation. 2007;14(7):1255–8.
  18. Gardner J, Ghorpade A. Tissue inhibitor of metalloproteinase (TIMP)-1: the TIMPed balance of matrix metalloproteinases in the central nervous system. Journal of Neuroscience Research. 2003;74(6):801–6.
  19. Zucker S, Hymowitz M, Conner C, DeClerck Y, Cao J. TIMP-2 is released as an intact molecule following binding to MT1-MMP on the cell surface. Experimental Cell Research. 2004;293(1):164–74.
  20. Galasso O, Familiari F, Gori MD, Gasparini G. Recent findings on the role of gelatinases (matrix metalloproteinase-2 and -9) in osteoarthritis. Advances in Orthopedics. 2012;2012:834208.
  21. Priyatini T, Santoso BI, Irianta T, Herqutanto, Siregar N, Harahap A, et al. Profile of matrix metalloproteinase activity, markers of collagen and elastin degradation and remodeling during pregnancy, delivery, and puerperium in pelvic organ prolapse 3 months after childbirth. Bali Med J. 2023;12(1):255-60.
  22. Santoso DPJ, Purwara BH, Achmad ED. Correlation between the expression of matrix metalloproteinase 9 and the expression of tissue inhibitor of metalloproteinase-1 of uterosacral ligament in uterine prolapse. Obstet Gynecol Sci. 2022;65(1):46-51.
  23. Wang X, Li Y, Chen J, Guo X, Guan H, Li C. Differential expression profiling of matrix metalloproteinases and tissue inhibitors of metalloproteinases in females with or without pelvic organ prolapse. Mol Med Rep. 2014;10(4):2004-8.
  24. Hu Y, Wu R, Li H, Gu Y, Wei W. Expression and significance of metalloproteinase and collagen in vaginal wall tissues of patients with pelvic organ prolapse. Ann Clin Lab Sci. 2017;47(6):698-705.

How to Cite

Anis, A., Kurniawati, E. M., Hardianto, G., & Setyohadi, T. H. (2023). The role of matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1) Expression in pelvic organ prolapse: A literature review. Bali Medical Journal, 12(3), 2729–2734. https://doi.org/10.15562/bmj.v12i3.4785

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Amilah Anis
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Eighty Mardiyan Kurniawati
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Gatut Hardianto
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Tri Hastono Setyohadi
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