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Published in: Journal of Cardiovascular Translational Research 3/2018

Open Access 01-06-2018 | Original Article

Serum MMP-9 Diagnostics, Prognostics, and Activation in Acute Coronary Syndrome and Its Recurrence

Authors: Laura Lahdentausta, Jaakko Leskelä, Alina Winkelmann, Taina Tervahartiala, Timo Sorsa, Erkki Pesonen, Pirkko J. Pussinen

Published in: Journal of Cardiovascular Translational Research | Issue 3/2018

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Abstract

Matrix metalloproteinase (MMP)-9 is crucial in atherosclerotic plaque rupture and tissue remodeling after a cardiac event. The balance between MMP-9 and endogenous inhibitor, tissue inhibitors of matrix metalloproteinase 1 (TIMP-1), is important in acute coronary syndrome (ACS). This is an age- and gender-matched case-control study of ACS (N = 669). Patients (45.7%) were resampled after recovery, and all were followed up for 6 years. The molecular forms of MMP-9 were investigated by gelatin zymography. Diagnostically, MMP-9 and the MMP-9/TIMP-1 molar ratio were associated with ACS (OR 5.81, 95% CI 2.65–12.76, and 4.96, 2.37–10.38). The MMP-9 concentrations decreased 49% during recovery (p < 0.001). The largest decrease of these biomarkers between acute and recovery phase (ΔMMP-9) protected the patients from major adverse cardiac events, especially the non-fatal events. The fatal events were associated with in vitro activatable MMP-9 levels (p = 0.028). Serum MMP-9 and the MMP-9/TIMP-1 molar ratio may be valuable in ACS diagnosis and prognosis. High serum MMP-9 activation potential is associated with poor cardiovascular outcome.
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Literature
1.
go back to reference Ross, R. (1999). Atherosclerosis—an inflammatory disease. The New England Journal of Medicine, 340(2), 115–126.CrossRefPubMed Ross, R. (1999). Atherosclerosis—an inflammatory disease. The New England Journal of Medicine, 340(2), 115–126.CrossRefPubMed
2.
go back to reference Libby, P., Ridker, P. M., Hansson, G. K., & Leducq Transatlantic Network on Atherothrombosis. (2009). Inflammation in atherosclerosis: from pathophysiology to practice. Journal of the American College of Cardiology, 54(23), 2129–2138.CrossRefPubMedPubMedCentral Libby, P., Ridker, P. M., Hansson, G. K., & Leducq Transatlantic Network on Atherothrombosis. (2009). Inflammation in atherosclerosis: from pathophysiology to practice. Journal of the American College of Cardiology, 54(23), 2129–2138.CrossRefPubMedPubMedCentral
3.
go back to reference Packard, R. R., & Libby, P. (2008). Inflammation in atherosclerosis: from vascular biology to biomarker discovery and risk prediction. Clinical Chemistry, 54(1), 24–38.CrossRefPubMed Packard, R. R., & Libby, P. (2008). Inflammation in atherosclerosis: from vascular biology to biomarker discovery and risk prediction. Clinical Chemistry, 54(1), 24–38.CrossRefPubMed
4.
go back to reference Tayebjee, M. H., Lip, G. Y., & MacFadyen, R. J. (2005). Matrix metalloproteinases in coronary artery disease: clinical and therapeutic implications and pathological significance. Current Medicinal Chemistry, 12(8), 917–925.CrossRefPubMed Tayebjee, M. H., Lip, G. Y., & MacFadyen, R. J. (2005). Matrix metalloproteinases in coronary artery disease: clinical and therapeutic implications and pathological significance. Current Medicinal Chemistry, 12(8), 917–925.CrossRefPubMed
5.
go back to reference Van Doren, S. R. (2015). Matrix metalloproteinase interactions with collagen and elastin. Matrix Biology, 44-46, 224–231.CrossRefPubMed Van Doren, S. R. (2015). Matrix metalloproteinase interactions with collagen and elastin. Matrix Biology, 44-46, 224–231.CrossRefPubMed
6.
go back to reference Arpino, V., Brock, M., & Gill, S. E. (2015). The role of TIMPs in regulation of extracellular matrix proteolysis. Matrix Biology, 44-46, 247–254.CrossRefPubMed Arpino, V., Brock, M., & Gill, S. E. (2015). The role of TIMPs in regulation of extracellular matrix proteolysis. Matrix Biology, 44-46, 247–254.CrossRefPubMed
7.
go back to reference Bannikov, G. A., Karelina, T. V., Collier, I. E., Marmer, B. L., & Goldberg, G. I. (2002). Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. The Journal of Biological Chemistry, 277(18), 16022–16027.CrossRefPubMed Bannikov, G. A., Karelina, T. V., Collier, I. E., Marmer, B. L., & Goldberg, G. I. (2002). Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. The Journal of Biological Chemistry, 277(18), 16022–16027.CrossRefPubMed
8.
go back to reference Brew, K., Dinakarpandian, D., & Nagase, H. (2000). Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochimica et Biophysica Acta, 1477(1–2), 267–283.CrossRefPubMed Brew, K., Dinakarpandian, D., & Nagase, H. (2000). Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochimica et Biophysica Acta, 1477(1–2), 267–283.CrossRefPubMed
9.
go back to reference Yabluchanskiy, A., Ma, Y., Iyer, R. P., Hall, M. E., & Lindsey, M. L. (2013). Matrix metalloproteinase-9: many shades of function in cardiovascular disease. Physiology (Bethesda), 28(6), 391–403. Yabluchanskiy, A., Ma, Y., Iyer, R. P., Hall, M. E., & Lindsey, M. L. (2013). Matrix metalloproteinase-9: many shades of function in cardiovascular disease. Physiology (Bethesda), 28(6), 391–403.
10.
go back to reference Grierson, C., Miller, D., LaPan, P., & Brady, J. (2010). Utility of combining MMP-9 enzyme-linked immunosorbent assay and MMP-9 activity assay data to monitor plasma enzyme specific activity. Analytical Biochemistry, 404(2), 232–234.CrossRefPubMed Grierson, C., Miller, D., LaPan, P., & Brady, J. (2010). Utility of combining MMP-9 enzyme-linked immunosorbent assay and MMP-9 activity assay data to monitor plasma enzyme specific activity. Analytical Biochemistry, 404(2), 232–234.CrossRefPubMed
11.
go back to reference Kai, H., Ikeda, H., Yasukawa, H., Kai, M., Seki, Y., Kuwahara, F., Ueno, T., Sugi, K., & Imaizumi, T. (1998). Peripheral blood levels of matrix metalloproteases-2 and -9 are elevated in patients with acute coronary syndromes. Journal of the American College of Cardiology, 32(2), 368–372. Kai, H., Ikeda, H., Yasukawa, H., Kai, M., Seki, Y., Kuwahara, F., Ueno, T., Sugi, K., & Imaizumi, T. (1998). Peripheral blood levels of matrix metalloproteases-2 and -9 are elevated in patients with acute coronary syndromes. Journal of the American College of Cardiology, 32(2), 368–372.
12.
go back to reference Inokubo, Y., Hanada, H., Ishizaka, H., Fukushi, T., Kamada, T., & Okumura, K. (2001). Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome. American Heart Journal, 141(2), 211–217. Inokubo, Y., Hanada, H., Ishizaka, H., Fukushi, T., Kamada, T., & Okumura, K. (2001). Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome. American Heart Journal, 141(2), 211–217.
13.
go back to reference Derosa, G., D’Angelo, A., Scalise, F., Avanzini, M.A., Tinelli, C., Peros, E., Fogari, E., & Cicero, A.F. (2007). Comparison between metalloproteinases-2 and -9 in healthy subjects, diabetics, and subjects with acute coronary syndrome. Heart and Vessels, 22(6), 361–370. Derosa, G., D’Angelo, A., Scalise, F., Avanzini, M.A., Tinelli, C., Peros, E., Fogari, E., & Cicero, A.F. (2007). Comparison between metalloproteinases-2 and -9 in healthy subjects, diabetics, and subjects with acute coronary syndrome. Heart and Vessels, 22(6), 361–370.
14.
go back to reference Fukuda, D., Shimada, K., Tanaka, A., Kusuyama, T., Yamashita, H., Ehara, S., Nakamura, Y., Kawarabayashi, T., Iida, H., Yoshiyama, M., et al. (2006). Comparison of levels of serum matrix metalloproteinase-9 in patients with acute myocardial infarction versus unstable angina pectoris versus stable angina pectoris. The American Journal of Cardiology, 97(2), 175–180.CrossRefPubMed Fukuda, D., Shimada, K., Tanaka, A., Kusuyama, T., Yamashita, H., Ehara, S., Nakamura, Y., Kawarabayashi, T., Iida, H., Yoshiyama, M., et al. (2006). Comparison of levels of serum matrix metalloproteinase-9 in patients with acute myocardial infarction versus unstable angina pectoris versus stable angina pectoris. The American Journal of Cardiology, 97(2), 175–180.CrossRefPubMed
15.
go back to reference Tan, J., Hua, Q., Gao, J., & Fan Z. X. (2008). Clinical implications of elevated serum interleukin-6, soluble CD40 ligand, metalloproteinase-9, and tissue inhibitor of metalloproteinase-1 in patients with acute ST-segment elevation myocardial infarction. Clinical Cardiology, 31(9), 413–418. https://doi.org/10.1002/clc.20254. Tan, J., Hua, Q., Gao, J., & Fan Z. X. (2008). Clinical implications of elevated serum interleukin-6, soluble CD40 ligand, metalloproteinase-9, and tissue inhibitor of metalloproteinase-1 in patients with acute ST-segment elevation myocardial infarction. Clinical Cardiology, 31(9), 413–418. https://​doi.​org/​10.​1002/​clc.​20254.
16.
go back to reference Blankenberg, S., Rupprecht, H. J., Poirier, O., Bickel, C., Smieja, M., et al. (2003). Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease. Circulation, 107(12), 1579–1585.CrossRefPubMed Blankenberg, S., Rupprecht, H. J., Poirier, O., Bickel, C., Smieja, M., et al. (2003). Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease. Circulation, 107(12), 1579–1585.CrossRefPubMed
17.
go back to reference Pesonen, E., El-Segaier, M., Persson, K., Puolakkainen, M., Sarna, S., Ohlin, H., & Pussinen, P. J. (2009). Infections as a stimulus for coronary occlusion, obstruction, or acute coronary syndromes. Therapeutic Advances in Cardiovascular Disease, 3(6), 447–454.CrossRefPubMed Pesonen, E., El-Segaier, M., Persson, K., Puolakkainen, M., Sarna, S., Ohlin, H., & Pussinen, P. J. (2009). Infections as a stimulus for coronary occlusion, obstruction, or acute coronary syndromes. Therapeutic Advances in Cardiovascular Disease, 3(6), 447–454.CrossRefPubMed
18.
go back to reference Pussinen, P. J., Sarna, S., Puolakkainen, M., Öhlin, H., Sorsa, T., & Pesonen, E. (2013). The balance of serum matrix metalloproteinase-8 and its tissue inhibitor in acute coronary syndrome and its recurrence. International Journal of Cardiology, 167(2), 362–368.CrossRefPubMed Pussinen, P. J., Sarna, S., Puolakkainen, M., Öhlin, H., Sorsa, T., & Pesonen, E. (2013). The balance of serum matrix metalloproteinase-8 and its tissue inhibitor in acute coronary syndrome and its recurrence. International Journal of Cardiology, 167(2), 362–368.CrossRefPubMed
20.
go back to reference Alfakry, H. (2014). Immune and proteolytic events associated with the signs of periodontal and cardiovascular diseases and their treatment. Doctoral dissertation, University of Helsinki. ISBN:978-952-10-9985-4. Alfakry, H. (2014). Immune and proteolytic events associated with the signs of periodontal and cardiovascular diseases and their treatment. Doctoral dissertation, University of Helsinki. ISBN:978-952-10-9985-4.
21.
go back to reference Nagase, H., & Brew, K. (2003). Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Biochemical Society Symposium, 70, 201–212.CrossRef Nagase, H., & Brew, K. (2003). Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Biochemical Society Symposium, 70, 201–212.CrossRef
22.
go back to reference Sorsa, T., Salo, T., Koivunen, E., Tyynelä, J., Konttinen, Y. T., Bergmann, U., Tuuttila, A., Niemi, E., Teronen, O., Heikkilä, P., Tschesche, H., Leinonen, J., Osman, S., & Stenman, U. H. (1997). Activation of type IV procollagenases by human tumor-associated trypsin-2. The Journal of Biological Chemistry, 272(34), 21067–21074.CrossRefPubMed Sorsa, T., Salo, T., Koivunen, E., Tyynelä, J., Konttinen, Y. T., Bergmann, U., Tuuttila, A., Niemi, E., Teronen, O., Heikkilä, P., Tschesche, H., Leinonen, J., Osman, S., & Stenman, U. H. (1997). Activation of type IV procollagenases by human tumor-associated trypsin-2. The Journal of Biological Chemistry, 272(34), 21067–21074.CrossRefPubMed
23.
go back to reference Kelly, D., Khan, S. Q., Thompson, M., Cockerill, G., Ng, L. L., Samani, N., & Squire, I. B. (2008). Plasma tissue inhibitor of metalloproteinase-1 and matrix metalloproteinase-9: novel indicators of left ventricular remodelling and prognosis after acute myocardial infarction. European Heart Journal, 29(17), 2116–2124.CrossRefPubMedPubMedCentral Kelly, D., Khan, S. Q., Thompson, M., Cockerill, G., Ng, L. L., Samani, N., & Squire, I. B. (2008). Plasma tissue inhibitor of metalloproteinase-1 and matrix metalloproteinase-9: novel indicators of left ventricular remodelling and prognosis after acute myocardial infarction. European Heart Journal, 29(17), 2116–2124.CrossRefPubMedPubMedCentral
24.
go back to reference Hansson, G. (2005). Inflammation, atherosclerosis, and coronary artery disease. The New England Journal of Medicine, 352(16), 1685–1695.CrossRefPubMed Hansson, G. (2005). Inflammation, atherosclerosis, and coronary artery disease. The New England Journal of Medicine, 352(16), 1685–1695.CrossRefPubMed
25.
go back to reference Garvin, P., Nilsson, L., Carstensen, J., Jonasson, L., & Kristenson, M. (2008). Circulating matrix metalloproteinase-9 is associated with cardiovascular risk factors in a middle-aged normal population. PLoS One, 3(3), e1774.CrossRefPubMedPubMedCentral Garvin, P., Nilsson, L., Carstensen, J., Jonasson, L., & Kristenson, M. (2008). Circulating matrix metalloproteinase-9 is associated with cardiovascular risk factors in a middle-aged normal population. PLoS One, 3(3), e1774.CrossRefPubMedPubMedCentral
26.
go back to reference Abdelnaseer, M. M., Nervana, M. E., Esmail, E. H., Kamal, M. M., & Elsawy, E. H. (2017). Matrix metalloproteinase-9 and recovery of acute ischemic stroke. Journal of Stroke and Cerebrovascular Diseases, 26, 733–740.CrossRefPubMed Abdelnaseer, M. M., Nervana, M. E., Esmail, E. H., Kamal, M. M., & Elsawy, E. H. (2017). Matrix metalloproteinase-9 and recovery of acute ischemic stroke. Journal of Stroke and Cerebrovascular Diseases, 26, 733–740.CrossRefPubMed
27.
go back to reference Kobayashi, N., Hata, N., Kume, N., Yokoyama, S., Shinada, T., Tomita, K., Kitamura, M., Shirakabe, A., Inami, T., Yamamoto, M., et al. (2011). Matrix metalloproteinase-9 for the earliest stage acute coronary syndrome. Circulation Journal, 75(12), 2853–2861.CrossRefPubMed Kobayashi, N., Hata, N., Kume, N., Yokoyama, S., Shinada, T., Tomita, K., Kitamura, M., Shirakabe, A., Inami, T., Yamamoto, M., et al. (2011). Matrix metalloproteinase-9 for the earliest stage acute coronary syndrome. Circulation Journal, 75(12), 2853–2861.CrossRefPubMed
28.
go back to reference Guzel, S., Serin, O., Guzel, E. C., Buyuk, B., Yilmaz, G., & Güvenen, G. (2013). Interleukin-33, matrixmetalloproteinase-9, and tissue inhibitor of matrix metalloproteinase-1 in myocardial infarction. The Korean Journal of Internal Medicine, 28(2), 165–173.CrossRefPubMedPubMedCentral Guzel, S., Serin, O., Guzel, E. C., Buyuk, B., Yilmaz, G., & Güvenen, G. (2013). Interleukin-33, matrixmetalloproteinase-9, and tissue inhibitor of matrix metalloproteinase-1 in myocardial infarction. The Korean Journal of Internal Medicine, 28(2), 165–173.CrossRefPubMedPubMedCentral
29.
go back to reference Peterson, J. T., Li, H., Dillon, L., & Bryant, J. W. (2000). Evolution of matrix metalloprotease and tissue inhibitor expression during heart failure progression in the infarcted rat. Cardiovascular Research, 46(2), 307–315.CrossRefPubMed Peterson, J. T., Li, H., Dillon, L., & Bryant, J. W. (2000). Evolution of matrix metalloprotease and tissue inhibitor expression during heart failure progression in the infarcted rat. Cardiovascular Research, 46(2), 307–315.CrossRefPubMed
30.
go back to reference Cimmino, G., Ragni, M., Cirillo, P., Petrillo, G., Loffredo, F., Chiariello, M., Gresele, P., Falcinelli, E., & Golino, P. (2013). C-reactive protein induces expression of matrix metalloproteinase-9: a possible link between inflammation and plaque rupture. International Journal of Cardiology, 168(2), 981–986.CrossRefPubMed Cimmino, G., Ragni, M., Cirillo, P., Petrillo, G., Loffredo, F., Chiariello, M., Gresele, P., Falcinelli, E., & Golino, P. (2013). C-reactive protein induces expression of matrix metalloproteinase-9: a possible link between inflammation and plaque rupture. International Journal of Cardiology, 168(2), 981–986.CrossRefPubMed
31.
go back to reference Opstad, T. B., Pettersen, A. A., Weiss, T. W., Akra, S., Øvstebø, R., Arnesen, H., & Seljeflot, I. (2012). Genetic variation, gene-expression and circulating levels of matrix metalloproteinase-9 in patients with stable coronary artery disease. Clinica Chimica Acta, 413(1–2), 113–120.CrossRef Opstad, T. B., Pettersen, A. A., Weiss, T. W., Akra, S., Øvstebø, R., Arnesen, H., & Seljeflot, I. (2012). Genetic variation, gene-expression and circulating levels of matrix metalloproteinase-9 in patients with stable coronary artery disease. Clinica Chimica Acta, 413(1–2), 113–120.CrossRef
32.
go back to reference Li, J., Lu, H., Tao, F., Zhou, H., Feng, G., He, L., & Zhou, L. (2013). Meta-analysis of MMP9-562C/T and the risk of coronary heart disease. Cardiology, 124(1), 53–59.CrossRefPubMed Li, J., Lu, H., Tao, F., Zhou, H., Feng, G., He, L., & Zhou, L. (2013). Meta-analysis of MMP9-562C/T and the risk of coronary heart disease. Cardiology, 124(1), 53–59.CrossRefPubMed
33.
go back to reference Vilmi-Kerälä, T., Lauhio, A., Tervahartiala, T., Palomäki, O., Uotila, J., Sorsa, T., & Palomäki, A. (2017). Subclinical inflammation associated with prolonged TIMP-1 upregulation and arterial stiffness after gestational diabetes mellitus: a hospital-based cohort study. Cardiovascular Diabetology, 16(1), 49.CrossRefPubMedPubMedCentral Vilmi-Kerälä, T., Lauhio, A., Tervahartiala, T., Palomäki, O., Uotila, J., Sorsa, T., & Palomäki, A. (2017). Subclinical inflammation associated with prolonged TIMP-1 upregulation and arterial stiffness after gestational diabetes mellitus: a hospital-based cohort study. Cardiovascular Diabetology, 16(1), 49.CrossRefPubMedPubMedCentral
34.
go back to reference Hausenloy, D. J., Garcia-Dorado, D., Bøtker, H. E., Davidson, S. M., Downey, J., Engel, F. B., Jennings, R., et al. (2017). Novel targets and future strategies for acute cardioprotection: Position paper of the European Society of Cardiology Working Group on Cellular Biology of the Heart. Cardiovascular Research, 113(6), 564–585.CrossRefPubMed Hausenloy, D. J., Garcia-Dorado, D., Bøtker, H. E., Davidson, S. M., Downey, J., Engel, F. B., Jennings, R., et al. (2017). Novel targets and future strategies for acute cardioprotection: Position paper of the European Society of Cardiology Working Group on Cellular Biology of the Heart. Cardiovascular Research, 113(6), 564–585.CrossRefPubMed
35.
go back to reference Bencsik, P., Pálóczi, J., Kocsis, G. F., Pipis, J., Belecz, I., Varga, Z. V., Csonka, C., et al. (2014). Moderate inhibition of myocardial matrix metalloproteinase-2 by ilomastat is cardioprotective. Pharmacological Research, 80, 36–42.CrossRefPubMed Bencsik, P., Pálóczi, J., Kocsis, G. F., Pipis, J., Belecz, I., Varga, Z. V., Csonka, C., et al. (2014). Moderate inhibition of myocardial matrix metalloproteinase-2 by ilomastat is cardioprotective. Pharmacological Research, 80, 36–42.CrossRefPubMed
36.
go back to reference Barkho, B. Z., Munoz, A. E., Li, X., et al. (2008). Endogenous matrix metalloproteinase (MMP)-3 and MMP-9 promote the differentiation and migration of adult neural progenitor cells in response to chemokines. Stem Cells, 26, 3139–3149.CrossRefPubMedPubMedCentral Barkho, B. Z., Munoz, A. E., Li, X., et al. (2008). Endogenous matrix metalloproteinase (MMP)-3 and MMP-9 promote the differentiation and migration of adult neural progenitor cells in response to chemokines. Stem Cells, 26, 3139–3149.CrossRefPubMedPubMedCentral
37.
go back to reference Kupai, K., et al. (2010). Matrix metalloproteinase activity assays: importance of zymography. Journal of Pharmacological and Toxicological Methods, 61(2), 205–209.CrossRefPubMed Kupai, K., et al. (2010). Matrix metalloproteinase activity assays: importance of zymography. Journal of Pharmacological and Toxicological Methods, 61(2), 205–209.CrossRefPubMed
38.
go back to reference Kjeldsen, L., Johnsen, A. H., Sengeløv, H., & Borregaard, N. (1993). Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. The Journal of Biological Chemistry, 268(14), 10425–10432.PubMed Kjeldsen, L., Johnsen, A. H., Sengeløv, H., & Borregaard, N. (1993). Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. The Journal of Biological Chemistry, 268(14), 10425–10432.PubMed
39.
go back to reference Roy, R., Louis, G., Loughlin, K. R., Wiederschain, D., Kilroy, S. M., Lamb, C. C., Zurakowski, D., & Moses, M. A. (2008). Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clinical Cancer Research, 14(20), 6610–6617.CrossRefPubMedPubMedCentral Roy, R., Louis, G., Loughlin, K. R., Wiederschain, D., Kilroy, S. M., Lamb, C. C., Zurakowski, D., & Moses, M. A. (2008). Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clinical Cancer Research, 14(20), 6610–6617.CrossRefPubMedPubMedCentral
40.
go back to reference Van Wart, H. E., & Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proceedings of the National Academy of Sciences of the United States of America, 87(14), 5578–5582.CrossRefPubMedPubMedCentral Van Wart, H. E., & Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proceedings of the National Academy of Sciences of the United States of America, 87(14), 5578–5582.CrossRefPubMedPubMedCentral
41.
go back to reference Ikeda, M., Maekawa, R., Tanaka, H., Matsumoto, M., Takeda, Y., Tamura, Y., Nemori, R., & Yoshioka, T. (2000). Inhibition of gelatinolytic activity in tumor tissues by synthetic matrix metalloproteinase inhibitor: application of film in situ zymography. Clinical Cancer Research, 6(8), 3290–3296.PubMed Ikeda, M., Maekawa, R., Tanaka, H., Matsumoto, M., Takeda, Y., Tamura, Y., Nemori, R., & Yoshioka, T. (2000). Inhibition of gelatinolytic activity in tumor tissues by synthetic matrix metalloproteinase inhibitor: application of film in situ zymography. Clinical Cancer Research, 6(8), 3290–3296.PubMed
42.
go back to reference DeCoux, A., Lindsey, M. L., Villarreal, F., Garcia, R. A., & Schulz, R. (2014). Myocardial matrix metalloproteinase-2: inside out and upside down. Journal of Molecular and Cellular Cardiology, 77, 64–72.CrossRefPubMed DeCoux, A., Lindsey, M. L., Villarreal, F., Garcia, R. A., & Schulz, R. (2014). Myocardial matrix metalloproteinase-2: inside out and upside down. Journal of Molecular and Cellular Cardiology, 77, 64–72.CrossRefPubMed
43.
go back to reference Jacob-Ferreira, A. L., Kondo, M. Y., Baral, P. K., James, M. N., Holt, A., Fan, X., & Schulz, R. (2013). Phosphorylation status of 72 kDa MMP-2 determines its structure and activity in response to peroxynitrite. PLoS One, 8(8), e71794.CrossRefPubMedPubMedCentral Jacob-Ferreira, A. L., Kondo, M. Y., Baral, P. K., James, M. N., Holt, A., Fan, X., & Schulz, R. (2013). Phosphorylation status of 72 kDa MMP-2 determines its structure and activity in response to peroxynitrite. PLoS One, 8(8), e71794.CrossRefPubMedPubMedCentral
44.
go back to reference Bencsik, P., Sasi, V., Kiss, K., Kupai, K., Kolossváry, M., Maurovich-Horvat, P., Csont, T., Ungi, I., Merkely, B., & Ferdinandy, P. (2015). Serum lipids and cardiac function correlate with nitrotyrosine and MMP activity in coronary artery disease patients. European Journal of Clinical Investigation, 45(7), 692–701.CrossRefPubMed Bencsik, P., Sasi, V., Kiss, K., Kupai, K., Kolossváry, M., Maurovich-Horvat, P., Csont, T., Ungi, I., Merkely, B., & Ferdinandy, P. (2015). Serum lipids and cardiac function correlate with nitrotyrosine and MMP activity in coronary artery disease patients. European Journal of Clinical Investigation, 45(7), 692–701.CrossRefPubMed
45.
go back to reference Marx, N., Froehlich, J., Siam, L., Ittner, J., Wierse, G., Schmidt, A., Scharnagl, H., Hombach, V., & Koenig, W. (2003). Antidiabetic PPAR gamma-activator rosiglitazone reduces MMP-9 serum levels in type 2 diabetic patients with coronary artery disease. Arteriosclerosis, Thrombosis, and Vascular Biology, 23(2), 283–288.CrossRefPubMed Marx, N., Froehlich, J., Siam, L., Ittner, J., Wierse, G., Schmidt, A., Scharnagl, H., Hombach, V., & Koenig, W. (2003). Antidiabetic PPAR gamma-activator rosiglitazone reduces MMP-9 serum levels in type 2 diabetic patients with coronary artery disease. Arteriosclerosis, Thrombosis, and Vascular Biology, 23(2), 283–288.CrossRefPubMed
46.
go back to reference Andrade, V. L., Petruceli, E., Belo, V. A., Andrade-Fernandes, C. M., Caetano Russi, C. V., Bosco, A. A., Tanus-Santos, J. E., & Sandrim, V. C. (2012). Evaluation of plasmatic MMP-8, MMP-9, TIMP-1 and MPO levels in obese and lean women. Clinical Biochemistry, 45(6), 412–415.CrossRefPubMed Andrade, V. L., Petruceli, E., Belo, V. A., Andrade-Fernandes, C. M., Caetano Russi, C. V., Bosco, A. A., Tanus-Santos, J. E., & Sandrim, V. C. (2012). Evaluation of plasmatic MMP-8, MMP-9, TIMP-1 and MPO levels in obese and lean women. Clinical Biochemistry, 45(6), 412–415.CrossRefPubMed
47.
go back to reference Hopps, E., Lo Presti, R., Montana, M., Noto, D., Averna, M. R., & Caimi, G. (2013). Gelatinases and their tissue inhibitors in a group of subjects with metabolic syndrome. Journal of Investigative Medicine, 61(6), 978–983.CrossRefPubMed Hopps, E., Lo Presti, R., Montana, M., Noto, D., Averna, M. R., & Caimi, G. (2013). Gelatinases and their tissue inhibitors in a group of subjects with metabolic syndrome. Journal of Investigative Medicine, 61(6), 978–983.CrossRefPubMed
48.
go back to reference Andrade, V. L., do Valle, I. B., & Sandrim, V. C. (2013). Simvastatin therapy decreases MMP-9 levels in obese women. Journal of Clinical Pharmacology, 53(10), 1072–1077.CrossRefPubMed Andrade, V. L., do Valle, I. B., & Sandrim, V. C. (2013). Simvastatin therapy decreases MMP-9 levels in obese women. Journal of Clinical Pharmacology, 53(10), 1072–1077.CrossRefPubMed
49.
go back to reference Ferretti, G., Bacchetti, T., Banach, M., Simental-Mendía, L. E., & Sahebkar, A. (2016). Impact of statin therapy on plasma MMP-3, MMP-9, and TIMP-1 concentrations. Angiology, 68, 850–862.CrossRef Ferretti, G., Bacchetti, T., Banach, M., Simental-Mendía, L. E., & Sahebkar, A. (2016). Impact of statin therapy on plasma MMP-3, MMP-9, and TIMP-1 concentrations. Angiology, 68, 850–862.CrossRef
Metadata
Title
Serum MMP-9 Diagnostics, Prognostics, and Activation in Acute Coronary Syndrome and Its Recurrence
Authors
Laura Lahdentausta
Jaakko Leskelä
Alina Winkelmann
Taina Tervahartiala
Timo Sorsa
Erkki Pesonen
Pirkko J. Pussinen
Publication date
01-06-2018
Publisher
Springer US
Published in
Journal of Cardiovascular Translational Research / Issue 3/2018
Print ISSN: 1937-5387
Electronic ISSN: 1937-5395
DOI
https://doi.org/10.1007/s12265-018-9789-x

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