Matrix Metalloproteinase-9 (MMP-9) Level in Tuberculosis Exposed and Infected Children
American Journal of Health Research
Volume 5, Issue 1, January 2017, Pages: 7-10
Received: Jan. 24, 2016; Accepted: Feb. 4, 2016; Published: Feb. 15, 2017
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Authors
Wildana Azikin, Department of Pediatrics, Medical Faculty of Hasanuddin University, Makassar, South Sulawesi, Indonesia
Amiruddin Laompo, Department of Pediatrics, Medical Faculty of Hasanuddin University, Makassar, South Sulawesi, Indonesia
Husein Albar, Department of Pediatrics, Medical Faculty of Hasanuddin University, Makassar, South Sulawesi, Indonesia
Dasril Daud, Department of Pediatrics, Medical Faculty of Hasanuddin University, Makassar, South Sulawesi, Indonesia
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Abstract
Background: Lung Tuberculosis (TB) is a chronic infectious disease caused by Mycobacterium tuberculosis (M. Tb). Excessive body's immune response to M. Tb will contribute to the host tissue damage. M. Tb infection stimulates gene expression and MMP-9 secretion from monocyte which is infected by M. Tb. M. Tb molecular mechanisms inducing granuloma formation which is the ESAT-6 protein that stimulates the production of matrix metalloproteinase-9 (MMP-9) from epithelial cells near the infected macrophages. Objective: To evaluate the levels of Matrix Metalloproteinase-9 (MMP-9) in children who lived in the same house with a tuberculosis person. Methods: A cross sectional study was conducted at the Lung Health Community Center (BBKPM) Makassar, from May to July 2015. The study population was children aged 3 months to 18 years. Results: Levels of MMP-9 were examined in 55 samples of the study, 29 samples infected with TB (52.7%), and 26 samples exposed to TB (47.3%). There is no significant difference in the levels of MMP-9 and genders, age, nutritional status, status of BCG, as well as the levels of MMP-9 in the group of exposed and infected to TB (p>0.05). Conclusion: There was no significant differences between the levels of MMP-9 in the group of exposed and infected to TB.
Keywords
Matrix Metalloproteinase-9 (MMP-9), Tuberculosis Exposed Children, Tuberculosis Infected Children
To cite this article
Wildana Azikin, Amiruddin Laompo, Husein Albar, Dasril Daud, Matrix Metalloproteinase-9 (MMP-9) Level in Tuberculosis Exposed and Infected Children, American Journal of Health Research. Vol. 5, No. 1, 2017, pp. 7-10. doi: 10.11648/j.ajhr.20170501.12
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Copyright © 2017 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
References
[1]
Rahajoe, N. N., Basir, D., Makmuri, M. S., Kartasasmita, C. B. Pedoman Nasional Tuberkulosis Anak. Edisi Revisi. Jakarta: UKK Respirologi PP Ikatan Dokter Anak Indonesia. 2010.
[2]
World Health Organization. Global tuberculosis report. Available from: URL: http://www.who.int/gtb/publications/globrep. 2013
[3]
Danneberg, A. M. Jr. Roles of Cytotoxic Delayed-Type Hypersensitivity and Macrophage-Activating Cell-Mediated Immunity in the Pathogenesis of Tuberculosis, Immunopathology. 1994.
[4]
Rundhaug, J. E. Matrix metalloproteinase, Angiogenesis and Cancer. Clinicancerres. 9: 551-554. 2003.
[5]
Welgus, H. G., Campbell E. J., Cury, J. D., Eisen, A. Z., Senior, R. M., Wilhelm, S. M., Goldberg, G. I. Neutral Metalloproteinase Produced by Human Mononuclear Phagocytes. Enzyme Profile, Regulation, and Expression during Cellular Development. J. Clin. Invest. The American Society for Clinical Investigation, Inc. 1990.
[6]
Stuelten CH., Byfield SD., Arany PR., Karpova TS., Stevenson W. G. S., Roberts A. B. Breast cancer cells induce stromal fibroblast to express MMP-9 via secretion of TNF-α and TGF-β. Journal of cell science 118. 2143-2153. 2005.
[7]
Ehlers, S., Schaible, U. E. The granuloma in tuberculosis: dynamics of a host–pathogen collusion. Available at. www.frontiersin.org. 2013.
[8]
Shiryaev SA., Cieplak P., Aleshin AE., Sun Q., Zhu W., Motamedchaboki K., Sloutsky A., Strongin AY. Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis. FEBS Journal, 278: 3277–3286. 2011.
[9]
Yong Li., Wang Y., Liu X. The role of airway epithelial cells in response to mycobacteria infection. Clinical and developmental immunology. 2012.
[10]
Sheen, S., O’Kane, C. M., Chaudhary, K., Tovar, M., Santillan, C., Sosa, J., Caviedes, L., et al. High MMP-9 activity characterises pleural tuberculosis correlating with granuloma formation. Eur Respir J. 2009; 33: 134–141.
[11]
Yurdakul A., Akyurek N., Yilmaz S., Karakaya J., Memis L., Oxturk C. Prognostic impact of matrix metalloproteinases (MMP-9 and MMP-2) and vascular endothelial growth factor expression in non small cell lung cancer. Turk J Med Sci; 42 (2): 281-288. 2012.
[12]
Snitker S., Xie K., Ryan KA., Yu D., Shuldiner AR., Mitchell BD., Gong DW. Correlation of circulating MMP-9 with white blood cell count in humans: Effect of smoking. Divisions of endocrinology. Volume 8 (6). 2013.
[13]
Sundstrom J., Evans JC., Benjamin EJ., Lew D., Larson MG., Sawyer DB., Siwik DA., Colucci WS., Sutherland P., Wilson PW., Vasan RS. Relation of plasma matrix metalloproteinase-9 to clinial cardiovaskular risk factors and echocardiographic left ventrikular measures: 109: 2850-2856). 2004.
[14]
Kilic Z., Ucar B., Ozdemir G., Colak O., Bal C., Ertugrul T. Circulating matrix metalloproteinases and tissue inhibitors of metalloproteinase levels in pediatrics patients with congenital heart disease: relationship to cardiac functions. Anadolu Kardiyol Derg: 14: 531-41. 2014.
[15]
Lee CY., Shim HS., Lee S., Lee JG., Kim DJ., Chung KY. Prognostic effect of matrix metalloproteinase-9 in patients with resected non small cell lung cancer. Journal of cardiothoracic surgery 10; 44. 2015.
[16]
Lacerda L. Faria APD., Fontana V., Moreno H., Sandrim V. Role of MMP-2 and MMP-9 in resistance to drug therapy in patients with resistant hypertension. 2015.
[17]
Olszewska G., M Urban. Elevated matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 1 in obese children and adolescents. 56 (6): 799-805. 2007.
[18]
Jarbrink MQ., Smith DA., Bancroft GJ. Production of matrix metalloproteinases in response to mycobacterial infection. Infection and immunity. Vol 69 no 9. p. 5661-5670. 2001.
[19]
Price NM. Farrar J., Chau T T H., Mai N. T. H. M. Hien T. T., Friedland J. S., Identification of a Matrix-Degrading Phenotype in Human Tuberculosis In Vitro and In Vivo. J Immunol, 166: 4223-4230. 2001.
[20]
Tshesche H., Knauper V., Kramer S., Michaelis J., Oberhoff R., Reinke H. Latent collagenase and gelatinase from human neutrophils and their activation. Matrix Suppl, 1: 245-255. 1992.
[21]
Voraphani N., Khongphatthanayothin A., Srikaew K., Tontulawat P., Poovorawan Y. Matrix Metalloproteinase-9 in children with dengue virus infection. Jpn. J. Infect. Dis, 63: 346-348. 2010.
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