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Association of MMP-2 and MMP-9 with clinical outcome of neurocysticercosis

Published online by Cambridge University Press:  04 August 2011

AVANTIKA VERMA ,
KASHI N. PRASAD ,
KISHAN K. NYATI ,
SATYENDRA K. SINGH ,
ALOUKICK K. SINGH ,
VIMAL K. PALIWAL  and
RAKESH K. GUPTA
AVANTIKA VERMA
Affiliation:
Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
KASHI N. PRASAD*
Affiliation:
Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
KISHAN K. NYATI
Affiliation:
Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
SATYENDRA K. SINGH
Affiliation:
Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
ALOUKICK K. SINGH
Affiliation:
Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
VIMAL K. PALIWAL
Affiliation:
Department of Neurology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
RAKESH K. GUPTA
Affiliation:
Department of Radiodiagnosis, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226014, India
*
*Corresponding author: Department of Microbiology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow-226 014, India. Tel: +91 522 2494265. Fax: +91 522 2668100/+91 522 2668017. E-mail: [email protected]
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Summary

Matrix metalloproteinases (MMPs) are the major endopeptidases involved in proteolysis of blood brain barrier (BBB) during central nervous system (CNS) infections. The present study detected serum levels and activities of MMP-2 and MMP-9 in patients with neurocysticercosis (NCC) and their association with symptomatic disease. In total, 68 individuals with NCC (36 symptomatic patients with active seizures and 32 asymptomatic individuals) and 37 healthy controls were enrolled for the study. Serum MMP-2 and MMP-9 levels and their activities were measured by ELISA and gel zymography respectively. Mean serum MMP-2 levels (ng/ml) were higher both in asymptomatic and symptomatic NCC cases compared to healthy controls. However, significantly higher levels of serum MMP-9 (ng/ml) were detected only in symptomatic NCC patients compared to asymptomatic NCC cases and healthy controls. Levels of both MMPs positively correlated with symptomatic NCC. Serum MMP-2 activities were significantly higher in symptomatic and asymptomatic NCC compared to healthy controls whereas serum MMP-9 activity was significantly associated with symptomatic NCC compared to healthy controls and asymptomatic NCC. In conclusion, the elevated level of MMP-9 in serum appears to play an important role in the development of symptoms i.e. active seizures in patients with NCC. However, further studies are needed to elucidate its precise role in disease pathogenesis.

Keywords

neurocysticercosisblood brain barrierMMP-2MMP-9
Type
Research Article
Information
Parasitology , Volume 138 , Issue 11 , September 2011 , pp. 1423 - 1428
Copyright
Copyright © Cambridge University Press 2011

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References

REFERENCES

Abraham, M., Shapiro, S., Karni, A., Weiner, H. L. and Miller, A. (2005). Gelatinases (MMP-2 and MMP-9) are preferentially expressed by Th1 vs. Th2 cells. Journal of Neuroimmunology 163, 157–164.CrossRefGoogle ScholarPubMed
Agarwal, S. P., Andreson, M., Durbeej, N. R., Ivars, G. O. and Sorokin, L. M. (2006). Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis. Journal of Experimental Medicine 203, 1007–1019.CrossRefGoogle Scholar
Alvarez, J. I. and Teale, J. M. (2007). Evidence for differential changes of junctional complex proteins in murine neurocysticercosis dependent upon CNS vasculature. Brain Research 1169, 98–111.CrossRefGoogle ScholarPubMed
Alvarez, J. I. and Teale, J. M. (2008). Multiple expression of matrix metalloproteinases in murine neurocysticercosis: implications for leukocyte migration through multiple central nervous system barriers. Brain Research 1214, 145–158.CrossRefGoogle ScholarPubMed
Asahi, M., Wang, X., Mori, T., Sumii, T., Jung, J. C., Moskowitz, M. A., Fini, M. E. and Lo, E. H. (2001). Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood brain barrier and white matter components after cerebral ischemia. Journal of Neuroscience 21, 7724–7732.CrossRefGoogle ScholarPubMed
Avolio, C., Ruggieri, M., Giuliani, F., Liuzzi, G. M., Leante, R., Riccio, P., Livrea, P. and Trojano, M. (2003). Serum MMP-2 and MMP-9 are elevated in different multiple sclerosis subtypes. Journal of Neuroimmunology 136, 46–53.CrossRefGoogle ScholarPubMed
Bar-Or, A., Nuttall, R. K., Duddy, M., Alter, A., Kim, H. J., Ifergan, I., Pennington, C. J., Bourgoin, P., Edwards, D. R. and Yong, V. W. (2003). Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis. Brain 126, 2738–2749.CrossRefGoogle ScholarPubMed
Del Brutto, O. H., Rajshekhar, V., White, A. C. Jr, Tsang, V. C., Nash, T. E., Takayanagui, O. M., Schantz, P. M., Evans, C. A., Flisser, A., Correa, D., Botero, D., Allan, J. C., Sarti, E., Gonzalez, A. E., Gilman, R. H. and Garcia, H. H. (2001). Proposed diagnostic criteria for neurocysticercosis. Neurology 57, 177–183.CrossRefGoogle ScholarPubMed
Fleury, A., Gomez, T., Alvarez, I., Meza, D., Huerta, M., Chavarria, A., Mezo, R. A. C., Lloyd, C., Dessein, A., Preux, P. M., Dumas, M., Larralde, C., Scintto, E. and Fragoso, G. (2003). High prevalence of calcified silent neurocysticercosis in a rural village of Mexico. Neuroepidemiology 22, 139–145.CrossRefGoogle Scholar
Garcia, H. H. and Del Brutto, O. H. (2003). Imaging findings in neurocysticercosis. Acta Tropica 87, 71–78.CrossRefGoogle ScholarPubMed
Garcia, H. H., Del Brutto, O. H., Nash, T. E., White, A. C. Jr, Tsang, V. C. and Gilman, R. H. (2005). New concepts in the diagnosis and management of neurocysticercosis (Taenia solium). American Journal of Tropical Medicine and Hygiene 72, 3–9.CrossRefGoogle ScholarPubMed
Gupta, R. K., Rao, S. B., Jain, R., Pal, R. K., Venkatesh, S. K. and Rathmore, R. K. (2001). Differentiation of calcification from chronic hemorrhage with corrected gradient echo phase imaging. Journal of Computed Assisted Tomography 25, 698–704.CrossRefGoogle ScholarPubMed
Harris, J. E., Vilaseca, M. F., Elkington, P. T. G., Horncastle, D., Graeber, M. B. and Friedland, J. S. (2007). IFNγ synergizes with IL-1β to up-regulate MMP-9 secretion in a cellular model of central nervous system tuberculosis. FASEB Journal 21, 356–365.CrossRefGoogle Scholar
Heuser, K., Hoddevik, E. H., Taubøll, E., Gjerstad, L., Indahl, U., Kaczmarek, L., Berg, P. R., Lien, S., Nagelhus, E. A. and Ottersen, O. P. (2010). Temporal lobe epilepsy and matrix metalloproteinase 9: a tempting relation but negative genetic association. Seizure 19, 335–338.CrossRefGoogle ScholarPubMed
Kim, W. U., Min, S. Y., Cho, M. L., Hong, K. H., Shin, Y. J., Park, S. H. and Cho, C. S. (2005). Elevated matrix metalloproteinase-9 in patients with systemic sclerosis. Arthritis Research & Therapy 7, 71–79.CrossRefGoogle ScholarPubMed
Manicone, A. M. and McGuire, J. K. (2008). Matrix metalloproteinases as modulators of inflammation. Seminars in Cell Developmental Biology 19, 34–41.CrossRefGoogle ScholarPubMed
Piao, M. S., Lee, J. K., Park, C. S., Ryu, H. S., Kim, S. H. and Kim, H. S. (2009). Early activation of matrix metalloproteinase-9 is associated with blood-brain barrier disruption after photothrombotic cerebral ischemia in rats. Acta Neurochirurgica 151, 1649–1653.CrossRefGoogle ScholarPubMed
Prasad, A., Gupta, R. K., Pradhan, S., Tripathi, M., Pandey, C. M., Luthara, C. and Prasad, K. N. (2008). What triggers seizures in neurocysticercosis?- a MRI based study in pig farming community from a district of north India. Parasitology International 55, 166–171.CrossRefGoogle Scholar
Prasad, K. N., Prasad, A., Gupta, R. K., Nath, K., Pradhan, S., Tripathi, M. and Pandey, C. M. (2009). Neurocysticercosis in patients with active epilepsy from the pig farming community of Lucknow district, north India. Transactions of the Royal society of Tropical Medicine & Hygiene 103, 144–150.CrossRefGoogle ScholarPubMed
Sciutto, E., Fragoso, G., Fleury, A., Laclette, J. P., Sotelo, J., Aluja, A., Vargas, L. and Larralde, C. (2000). Taenia solium disease in humans and pigs:an ancient parasitosis disease rooted in developing countries and emerging as a major health problem of global dimensions. Microbes and Infection 2, 1875–1890.CrossRefGoogle Scholar
Strazielle, N., Khuth, S. T., Murat, A., Chalon, A., Giraudon, P., Belin, M. F. and Ghersi-Egea, J. F. (2003). Pro-inflammatory cytokines modulate matrix metalloproteinase secretion and organic anion transport at the blood cerebrospinal fluid barrier. Journal of Neuropathology and Experimental Neurology 62, 1254–1264.CrossRefGoogle ScholarPubMed
Visse, R. and Nagase, H. (2003). Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circulation Research 92, 827–839.CrossRefGoogle ScholarPubMed
Wang, P., Dai, J., Bai, F., Kong, K. F., Wong, S. J., Montgomery, R. R., Madri, J. A. and Fikrig, E. (2008). Matrix metalloproteinase 9 facilitates West Nile Virus entry into the brain. Journal of Virology 82, 8978–8985.CrossRefGoogle ScholarPubMed
Wilczynski, G. M., Konopacki, F. A., Wilczek, E., Lasiecka, Z., Gorlewicz, A., Michaluk, P., Wawrzynski, M., Malinowska, M., Okulski, P., Kolodziej, L. R., Konopka, W., Duniec, K., Mioduszewska, B., Nikolaev, E., Walczak, A., Owczarek, D., Gorecki, D. C., Zuschratter, W., Ottersen, O. P. and Kaczmarek, L. (2008). Important role of matrix metalloproteinase 9 in epileptogenesis. Journal of Cell Biology 180, 1021–1035.CrossRefGoogle ScholarPubMed
Yin, P., Yang, L., Zhou, H. Y. and Sun, R. P. (2011). Matrix metalloproteinase-9 may be a potential therapeutic target in epilepsy. Medical Hypotheses 76, 184–186.CrossRefGoogle ScholarPubMed