Salivary MMP-8, TIMP-1, and ICTP as markers of advanced periodontitis

Gursoy UK, Könönen E, Pradhan‐Palikhe P, Tervahartiala T, Pussinen PJ, Suominen‐Taipale L, Sorsa T. Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced periodontitis. J Clin Periodontol 2010; 37: 487–493. doi: 10.1111/j.1600‐051X.2010.01563.x. Aim: Salivary matrix metalloproteinase (MMP)‐8 and ‐...

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Published inJournal of clinical periodontology Vol. 37; no. 6; pp. 487 - 493
Main Authors Gursoy, Ulvi Kahraman, Könönen, Eija, Pradhan-Palikhe, Pratikshya, Tervahartiala, Taina, Pussinen, Pirkko J., Suominen-Taipale, Liisa, Sorsa, Timo
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.06.2010
Blackwell
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Online AccessGet full text
ISSN0303-6979
1600-051X
1600-051X
DOI10.1111/j.1600-051X.2010.01563.x

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Abstract Gursoy UK, Könönen E, Pradhan‐Palikhe P, Tervahartiala T, Pussinen PJ, Suominen‐Taipale L, Sorsa T. Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced periodontitis. J Clin Periodontol 2010; 37: 487–493. doi: 10.1111/j.1600‐051X.2010.01563.x. Aim: Salivary matrix metalloproteinase (MMP)‐8 and ‐14, tissue inhibitor of matrix metalloproteinase (TIMP)‐1, and pyridinoline cross‐linked carboxyterminal telopeptide of type I collagen (ICTP) were analysed aiming to detect potential markers of advanced periodontitis in saliva. In addition, we compared two MMP‐8 detection methods, a time‐resolved immunofluorometric assay (IFMA) and an enzyme‐linked immunoassay (ELISA), to differentiate periodontitis subjects from controls. Material and Methods: Concentrations of MMP‐8, MMP‐14, TIMP‐1, and ICTP were analysed from salivary specimens of 165 subjects, including 84 subjects having at least 14 teeth with periodontal pocket (pocket depth 4 mm) and 81 subjects without pocket depth as their controls. Results: Salivary MMP‐8 detection by IFMA differentiated periodontitis subjects from controls more strongly than by ELISA. Salivary MMP‐8, TIMP‐1, and ICTP concentrations were higher in periodontitis subjects than those in controls. When only smokers were included in the analysis these differences were lost. The MMP‐8/TIMP‐1 ratio and the combination of MMP‐8 and ICTP differentiated periodontitis and control groups even in smoker subjects. Conclusion: Salivary MMP‐8, TIMP‐1, ICTP, and especially their ratios and combinations are potential candidates in the detection of advanced periodontitis. Differentiating periodontitis and control subjects with salivary MMP‐8 detection is dependent on the selected techniques.
AbstractList Salivary matrix metalloproteinase (MMP)-8 and -14, tissue inhibitor of matrix metalloproteinase (TIMP)-1, and pyridinoline cross-linked carboxyterminal telopeptide of type I collagen (ICTP) were analysed aiming to detect potential markers of advanced periodontitis in saliva. In addition, we compared two MMP-8 detection methods, a time-resolved immunofluorometric assay (IFMA) and an enzyme-linked immunoassay (ELISA), to differentiate periodontitis subjects from controls.AIMSalivary matrix metalloproteinase (MMP)-8 and -14, tissue inhibitor of matrix metalloproteinase (TIMP)-1, and pyridinoline cross-linked carboxyterminal telopeptide of type I collagen (ICTP) were analysed aiming to detect potential markers of advanced periodontitis in saliva. In addition, we compared two MMP-8 detection methods, a time-resolved immunofluorometric assay (IFMA) and an enzyme-linked immunoassay (ELISA), to differentiate periodontitis subjects from controls.Concentrations of MMP-8, MMP-14, TIMP-1, and ICTP were analysed from salivary specimens of 165 subjects, including 84 subjects having at least 14 teeth with periodontal pocket (pocket depth > or =4 mm) and 81 subjects without pocket depth as their controls.MATERIAL AND METHODSConcentrations of MMP-8, MMP-14, TIMP-1, and ICTP were analysed from salivary specimens of 165 subjects, including 84 subjects having at least 14 teeth with periodontal pocket (pocket depth > or =4 mm) and 81 subjects without pocket depth as their controls.Salivary MMP-8 detection by IFMA differentiated periodontitis subjects from controls more strongly than by ELISA. Salivary MMP-8, TIMP-1, and ICTP concentrations were higher in periodontitis subjects than those in controls. When only smokers were included in the analysis these differences were lost. The MMP-8/TIMP-1 ratio and the combination of MMP-8 and ICTP differentiated periodontitis and control groups even in smoker subjects.RESULTSSalivary MMP-8 detection by IFMA differentiated periodontitis subjects from controls more strongly than by ELISA. Salivary MMP-8, TIMP-1, and ICTP concentrations were higher in periodontitis subjects than those in controls. When only smokers were included in the analysis these differences were lost. The MMP-8/TIMP-1 ratio and the combination of MMP-8 and ICTP differentiated periodontitis and control groups even in smoker subjects.Salivary MMP-8, TIMP-1, ICTP, and especially their ratios and combinations are potential candidates in the detection of advanced periodontitis. Differentiating periodontitis and control subjects with salivary MMP-8 detection is dependent on the selected techniques.CONCLUSIONSalivary MMP-8, TIMP-1, ICTP, and especially their ratios and combinations are potential candidates in the detection of advanced periodontitis. Differentiating periodontitis and control subjects with salivary MMP-8 detection is dependent on the selected techniques.
Salivary matrix metalloproteinase (MMP)-8 and -14, tissue inhibitor of matrix metalloproteinase (TIMP)-1, and pyridinoline cross-linked carboxyterminal telopeptide of type I collagen (ICTP) were analysed aiming to detect potential markers of advanced periodontitis in saliva. In addition, we compared two MMP-8 detection methods, a time-resolved immunofluorometric assay (IFMA) and an enzyme-linked immunoassay (ELISA), to differentiate periodontitis subjects from controls. Concentrations of MMP-8, MMP-14, TIMP-1, and ICTP were analysed from salivary specimens of 165 subjects, including 84 subjects having at least 14 teeth with periodontal pocket (pocket depth > or =4 mm) and 81 subjects without pocket depth as their controls. Salivary MMP-8 detection by IFMA differentiated periodontitis subjects from controls more strongly than by ELISA. Salivary MMP-8, TIMP-1, and ICTP concentrations were higher in periodontitis subjects than those in controls. When only smokers were included in the analysis these differences were lost. The MMP-8/TIMP-1 ratio and the combination of MMP-8 and ICTP differentiated periodontitis and control groups even in smoker subjects. Salivary MMP-8, TIMP-1, ICTP, and especially their ratios and combinations are potential candidates in the detection of advanced periodontitis. Differentiating periodontitis and control subjects with salivary MMP-8 detection is dependent on the selected techniques.
Gursoy UK, Könönen E, Pradhan‐Palikhe P, Tervahartiala T, Pussinen PJ, Suominen‐Taipale L, Sorsa T. Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced periodontitis. J Clin Periodontol 2010; 37: 487–493. doi: 10.1111/j.1600‐051X.2010.01563.x. Aim: Salivary matrix metalloproteinase (MMP)‐8 and ‐14, tissue inhibitor of matrix metalloproteinase (TIMP)‐1, and pyridinoline cross‐linked carboxyterminal telopeptide of type I collagen (ICTP) were analysed aiming to detect potential markers of advanced periodontitis in saliva. In addition, we compared two MMP‐8 detection methods, a time‐resolved immunofluorometric assay (IFMA) and an enzyme‐linked immunoassay (ELISA), to differentiate periodontitis subjects from controls. Material and Methods: Concentrations of MMP‐8, MMP‐14, TIMP‐1, and ICTP were analysed from salivary specimens of 165 subjects, including 84 subjects having at least 14 teeth with periodontal pocket (pocket depth 4 mm) and 81 subjects without pocket depth as their controls. Results: Salivary MMP‐8 detection by IFMA differentiated periodontitis subjects from controls more strongly than by ELISA. Salivary MMP‐8, TIMP‐1, and ICTP concentrations were higher in periodontitis subjects than those in controls. When only smokers were included in the analysis these differences were lost. The MMP‐8/TIMP‐1 ratio and the combination of MMP‐8 and ICTP differentiated periodontitis and control groups even in smoker subjects. Conclusion: Salivary MMP‐8, TIMP‐1, ICTP, and especially their ratios and combinations are potential candidates in the detection of advanced periodontitis. Differentiating periodontitis and control subjects with salivary MMP‐8 detection is dependent on the selected techniques.
Author Sorsa, Timo
Könönen, Eija
Pussinen, Pirkko J.
Pradhan-Palikhe, Pratikshya
Tervahartiala, Taina
Gursoy, Ulvi Kahraman
Suominen-Taipale, Liisa
Author_xml – sequence: 1
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– sequence: 7
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  organization: Institute of Dentistry, University of Helsinki, Helsinki, Finland
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Issue 6
Keywords Periodontal disease
TIMP-1
Periodontitis
ICTP
Stomatology
MMP-14
MMP-8
Dentistry
Saliva
Language English
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The authors declare that they have no conflicts of interests.
The present study is a part of the Health 2000 Health Examination survey, organized by National Institute for Health and Welfare of Finland. This study was supported by grants from the Paulo and Yrjo Jahnsson Foundations (for U. K. G.), the Academy of Finland (grant 78443 for E. K. and grant 118391 for P. J. P.), and the Helsinki University Central Hospital Research Foundation. Timo Sorsa is the inventor of US patents 5652227, 5736341, 5866432, and 6143476.
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PublicationTitle Journal of clinical periodontology
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References Ingman, T., Tervahartiala, T., Ding, Y., Tschesche, H., Haerian, A., Kinane, D. F., Konttinen, Y. T. & Sorsa, T. (1996) Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients. Journal of Clinical Periodontology 23, 1127-1132.
Frodge, B. D., Ebersole, J. L., Kryscio, R. J., Thomas, M. V. & Miller, C. S. (2008) Bone remodeling biomarkers of periodontal disease in saliva. Journal of Periodontology 79, 1913-1919.
Miller, C. S., King, C. P. Jr., Langub, M. C., Kryscio, R. J. & Thomas, M. V. (2006) Salivary biomarkers of existing periodontal disease: a cross-sectional study. Journal of American Dental Association 137, 322-329.
Pozo, P., Valenzuela, M A., Melej, C., Zaldivar, M., Puente, J., Martinez, B. & Gamonal, J. (2005) Longitudinal analysis of metalloproteinases, tissue inhibitors of metalloproteinases and clinical parameters in gingival crevicular fluid from periodontitis-affected patients. Journal of Periodontal Research 40, 199-207.
Reynolds, J. J. (1996) Collagenases and tissue inhibitors of metalloproteinases: a functional balance in tissue degradation. Oral Diseases 2, 70-76.
Romanelli, R., Mancini, S., Laschinger, C., Overall, C. M., Sodek, J. & McCulloch, C. A. (1999) Activation of neutrophil collagenase in periodontitis. Infection and Immunity 67, 2319-2326.
Ng, P. Y., Donley, M., Hausmann, E., Hutson, A. D., Rossomando, E. F. & Scannapieco, F. A. (2007) Candidate salivary biomarkers associated with alveolar bone loss: cross-sectional and in vitro studies. FEMS Immunology and Medical Microbiology 49, 252-260.
Könönen, E., Paju, S., Pussinen, P. J., Hyvönen, M., Di Tella, P., Suominen-Taipale, L. & Knuuttila, M. (2007) Population-based study of salivary carriage of periodontal pathogens in adults. Journal of Clinical Microbiology 45, 2446-2451.
Ramseier, C. A., Kinney, J. S., Herr, A. E., Braun, T., Sugai, J. V., Shelburne, C. A., Rayburn, L. A., Tran, H. M., Singh, A. K. & Giannobile, W. V. (2009) Identification of pathogen and host-response markers correlated with periodontal disease. Journal of Periodontology 80, 436-446.
Kiili, M., Cox, S. W., Chen, H. Y., Wahlgren, J., Maisi, P., Eley, B. M., Salo, T. & Sorsa, T. (2002) Collagenase-2 (MMP-8) and collagenase-3 (MMP-13) in adult periodontitis: molecular forms and levels in gingival crevicular fluid and immunolocalisation in gingival tissue. Journal of Clinical Periodontology 29, 224-232.
Birkedal-Hansen, H. (1993) Role of matrix metalloproteinases in human periodontal diseases. Journal of Periodontology 64, 474-484.
Syggelos, S. A., Eleftheriou, S. C., Giannopoulou, E., Panagiotopoulos, E. & Aletras, A. J. (2001) Gelatinolytic and collagenolytic activity in periprosthetic tissues from loose hip endoprostheses. Journal of Rheumatology 28, 1319-1329.
Sorsa, T., Hernández, M., Leppilahti, J., Munjal, S., Netuschil, L. & Mäntylä, P. (2010) Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods. Oral Diseases 16, 39-45.
Paju, S., Pussinen, P. J., Suominen-Taipale, L., Hyvönen, M., Knuuttila, M. & Könönen, E. (2009) Detection of multiple pathogenic species in saliva is associated with periodontal infections in adults. Journal of Clinical Microbiology 47, 235-238.
Weiss, S. J. (1989) Tissue destruction by neutrophils. New England Journal of Medicine 9, 365-376.
Sorsa, T., Tjäderhane, L. & Salo, T. (2004) Matrix metalloproteinases (MMPs) in oral diseases. Oral Diseases 10, 311-318.
Hanemaaijer, R., Sorsa, T., Konttinen, Y. T., Ding, Y., Sutinen, M., Visser, H., Van Hinsbergh, V. W., Helaakoski, T., Kainulainen, T., Rönkä, H., Tschesche, H. & Salo, T. (1997) Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. Journal of Biological Chemistry 12, 31504-31509.
Gursoy, U. K., Könönen, E., Uitto, V-J., Pussinen, P., Hyvärinen, K., Suominen-Taipale, L. & Knuuttila, M. (2009) Salivary interleukin-1β concentration and presence of multiple pathogens in periodontitis. Journal of Clinical Periodontology 36, 922-927.
Tatakis, D. N. & Kumar, P. S. (2005) Etiology and pathogenesis of periodontal diseases. Dental Clinics of North America 49, 491-516.
Raitio, A., Tuomas, H., Kokkonen, N., Salo, T., Sorsa, T., Hanemaaijer, R. & Oikarinen, A. (2005) Levels of matrix metalloproteinase-2, -9 and -8 in the skin, serum and saliva of smokers and non-smokers. Archives of Dermatological Research 297, 242-248.
Sorsa, T., Tjäderhane, L., Konttinen, Y. T., Lauhio, A., Salo, T., Lee, H. M., Golub, L. M., Brown, D. L. & Mäntylä, P. (2006) Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Annals of Medicine 38, 306-321.
Mancini, S., Romanelli, R., Laschinger, C. A., Overall, C. M., Sodek, J. & McCulloch, C. A. (1999) Assessment of a novel screening test for neutrophil collagenase activity in the diagnosis of periodontal diseases. Journal of Periodontology 70, 1292-1302.
Tobón-Arroyave, S. I., Jaramillo-González, P. E. & Isaza-Guzmán, D. M. (2008) Correlation between salivary IL-1β levels and periodontal clinical status. Archives of Oral Biology 53, 346-352.
Kibayashi, M., Tanaka, M., Nishida, N., Kuboniwa, M., Kataoka, K., Nagata, H., Nakayama, K., Morimoto, K. & Shizukuishi, S. (2007) Longitudinal study of the association between smoking as a periodontitis risk and salivary biomerkers related to periodontitis. Journal of Periodontology 78, 859-867.
Holopainen, J. M., Moilanen, J. A., Sorsa, T., Kivelä-Rajamäki, M., Tervahartiala, T., Vesaluoma, M. H. & Tervo, T. M. (2003) Activation of matrix metalloproteinase-8 by membrane type 1-MMP and their expression in human tears after photorefractive keratectomy. Investigative Ophthalmology and Visual Science 44, 2550-2556.
Söder, B., Jin, L. J. & Wickholm, S. (2002) Granulocyte elastase, matrix metalloproteinase-8 and prostaglandin E2 in gingival crevicular fluid in matched clinical sites in smokers and non-smokers with persistent periodontitis. Journal of Clinical Periodontology 29, 384-391.
Hayakawa, H., Yamashita, K., Ohwaki, K., Sawa, M., Noguchi, T., Iwata, K. & Hayakawa, T. (1994) Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontology diseased subjects. Journal of Periodontal Research 29, 305-308.
Uitto, V-J., Suomalainen, K. & Sorsa, T. (1990) Salivary collagenase. Origin, characteristics and relationship to periodontal health. Journal of Periodontal Research 25, 135-142.
Taba, M. Jr., Kinney, J., Kim, A. S. & Giannobile, W. V. (2005) Diagnostic biomarkers for oral and periodontal diseases. Dental Clinics of North America 49, 551-571.
Teles, R. P., Likhari, V., Socransky, S. S. & Haffajee, A. D. (2009) Salivary cytokine levels in subjects with chronic periodontitis and in periodontally healthy individuals: a cross-sectional study. Journal of Periodontal Research 44, 411-417.
Giannobile, W. V. (1997) Crevicular fluid biomarkers of oral bone loss. Current Opinion in Periodontology 4, 11-20.
Sorsa, T., Uitto, V-J., Suomalainen, K., Vauhkonen, M. & Lindy, S. (1988) Comparison of interstitial collagenases from human gingiva, sulcular fluid and polymorphonuclear leukocytes. Journal of Periodontal Research 23, 386-393.
Scannapieco, F. A., Ng, P. B. Y., Hovey, K., Hausmann, E. & Wactawski-Wende, J. (2007) Salivary biomarkers associated with alveolar bone loss. Annals of the New York Academy of Sciences 1098, 496-497.
Kinney, J. S., Ramseier, C. A. & Giannobile, W. V. (2007) Oral fluid-based biomarkers of alveolar bone loss in periodontitis. Annals of the New York Academy of Sciences 1098, 230-251.
Teles, R. P., Sakellari, D., Teles, F. R. F., Konstantinidis, A., Kent, R., Socransky, S. S. & Haffajee, A. D. (2010) Relationships among gingival crevicular fluid biomarkers, clinical parameters of periodontal disease, and subgingival microbiota. Journal of Periodontology 81, 89-98.
Tuomainen, A. M., Nyyssönen, K., Laukkanen, J. A., Tervahartiala, T., Tuomainen, T. P., Salonen, J. T., Sorsa, T. & Pussinen, P. J. (2007) Serum matrix metalloproteinase-8 concentrations are associated with cardiovascular outcome in men. Arteriosclerosis, Thrombosis, and Vascular Biology 27, 2722-2728.
Lorencini, M., Silva, J. A., De La Hoz, C. L., Carvalho, H. F. & Stach-Machado, D. R. (2009) Changes in MMPs and inflammatory cells in experimental gingivitis. Histology and Histopathology 24, 157-166.
Palcanis, K. G., Larjava, I. K., Wells, B. R., Suggs, K. A., Landis, J. R., Chadwick, D. E. & Jeffcoat, M. K. (1992) Elastase as an indicator of periodontal disease progression. Journal of Periodontology 63, 237-242.
Hyvärinen, K., Laitinen, S., Paju, S., Hakala, A. S., Suominen-Taipale, L., Skurnik, M., Könönen, E. & Pussinen, P. J. (2009) Detection and quantification of five major periodontal pathogens by single copy gene-based real-time PCR. Innate Immunity 15, 195-204.
Knäuper, V., Krämer, S., Reinke, H. & Tschesche, H. (1990) Partial amino acid sequence of human PMN leukocyte procollagenase. Biological Chemistry Hoppe-Seyler 371, 295-304.
Lee, W., Aitken, S., Sodek, J. & McCulloch, C. A. (1995) Evidence of a direct relationship between neutrophil collagenase activity and periodontal tissue destruction in vivo: role of active enzyme in human periodontitis. Journal of Periodontal Research 30, 23-33.
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References_xml – reference: Frodge, B. D., Ebersole, J. L., Kryscio, R. J., Thomas, M. V. & Miller, C. S. (2008) Bone remodeling biomarkers of periodontal disease in saliva. Journal of Periodontology 79, 1913-1919.
– reference: Kibayashi, M., Tanaka, M., Nishida, N., Kuboniwa, M., Kataoka, K., Nagata, H., Nakayama, K., Morimoto, K. & Shizukuishi, S. (2007) Longitudinal study of the association between smoking as a periodontitis risk and salivary biomerkers related to periodontitis. Journal of Periodontology 78, 859-867.
– reference: Hyvärinen, K., Laitinen, S., Paju, S., Hakala, A. S., Suominen-Taipale, L., Skurnik, M., Könönen, E. & Pussinen, P. J. (2009) Detection and quantification of five major periodontal pathogens by single copy gene-based real-time PCR. Innate Immunity 15, 195-204.
– reference: Kiili, M., Cox, S. W., Chen, H. Y., Wahlgren, J., Maisi, P., Eley, B. M., Salo, T. & Sorsa, T. (2002) Collagenase-2 (MMP-8) and collagenase-3 (MMP-13) in adult periodontitis: molecular forms and levels in gingival crevicular fluid and immunolocalisation in gingival tissue. Journal of Clinical Periodontology 29, 224-232.
– reference: Palcanis, K. G., Larjava, I. K., Wells, B. R., Suggs, K. A., Landis, J. R., Chadwick, D. E. & Jeffcoat, M. K. (1992) Elastase as an indicator of periodontal disease progression. Journal of Periodontology 63, 237-242.
– reference: Sorsa, T., Tjäderhane, L., Konttinen, Y. T., Lauhio, A., Salo, T., Lee, H. M., Golub, L. M., Brown, D. L. & Mäntylä, P. (2006) Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Annals of Medicine 38, 306-321.
– reference: Weiss, S. J. (1989) Tissue destruction by neutrophils. New England Journal of Medicine 9, 365-376.
– reference: Tatakis, D. N. & Kumar, P. S. (2005) Etiology and pathogenesis of periodontal diseases. Dental Clinics of North America 49, 491-516.
– reference: Knäuper, V., Krämer, S., Reinke, H. & Tschesche, H. (1990) Partial amino acid sequence of human PMN leukocyte procollagenase. Biological Chemistry Hoppe-Seyler 371, 295-304.
– reference: Miller, C. S., King, C. P. Jr., Langub, M. C., Kryscio, R. J. & Thomas, M. V. (2006) Salivary biomarkers of existing periodontal disease: a cross-sectional study. Journal of American Dental Association 137, 322-329.
– reference: Paju, S., Pussinen, P. J., Suominen-Taipale, L., Hyvönen, M., Knuuttila, M. & Könönen, E. (2009) Detection of multiple pathogenic species in saliva is associated with periodontal infections in adults. Journal of Clinical Microbiology 47, 235-238.
– reference: Hayakawa, H., Yamashita, K., Ohwaki, K., Sawa, M., Noguchi, T., Iwata, K. & Hayakawa, T. (1994) Collagenase activity and tissue inhibitor of metalloproteinases-1 (TIMP-1) content in human whole saliva from clinically healthy and periodontology diseased subjects. Journal of Periodontal Research 29, 305-308.
– reference: Uitto, V-J., Suomalainen, K. & Sorsa, T. (1990) Salivary collagenase. Origin, characteristics and relationship to periodontal health. Journal of Periodontal Research 25, 135-142.
– reference: Pozo, P., Valenzuela, M A., Melej, C., Zaldivar, M., Puente, J., Martinez, B. & Gamonal, J. (2005) Longitudinal analysis of metalloproteinases, tissue inhibitors of metalloproteinases and clinical parameters in gingival crevicular fluid from periodontitis-affected patients. Journal of Periodontal Research 40, 199-207.
– reference: Birkedal-Hansen, H. (1993) Role of matrix metalloproteinases in human periodontal diseases. Journal of Periodontology 64, 474-484.
– reference: Ng, P. Y., Donley, M., Hausmann, E., Hutson, A. D., Rossomando, E. F. & Scannapieco, F. A. (2007) Candidate salivary biomarkers associated with alveolar bone loss: cross-sectional and in vitro studies. FEMS Immunology and Medical Microbiology 49, 252-260.
– reference: Söder, B., Jin, L. J. & Wickholm, S. (2002) Granulocyte elastase, matrix metalloproteinase-8 and prostaglandin E2 in gingival crevicular fluid in matched clinical sites in smokers and non-smokers with persistent periodontitis. Journal of Clinical Periodontology 29, 384-391.
– reference: Teles, R. P., Likhari, V., Socransky, S. S. & Haffajee, A. D. (2009) Salivary cytokine levels in subjects with chronic periodontitis and in periodontally healthy individuals: a cross-sectional study. Journal of Periodontal Research 44, 411-417.
– reference: Taba, M. Jr., Kinney, J., Kim, A. S. & Giannobile, W. V. (2005) Diagnostic biomarkers for oral and periodontal diseases. Dental Clinics of North America 49, 551-571.
– reference: Scannapieco, F. A., Ng, P. B. Y., Hovey, K., Hausmann, E. & Wactawski-Wende, J. (2007) Salivary biomarkers associated with alveolar bone loss. Annals of the New York Academy of Sciences 1098, 496-497.
– reference: Tuomainen, A. M., Nyyssönen, K., Laukkanen, J. A., Tervahartiala, T., Tuomainen, T. P., Salonen, J. T., Sorsa, T. & Pussinen, P. J. (2007) Serum matrix metalloproteinase-8 concentrations are associated with cardiovascular outcome in men. Arteriosclerosis, Thrombosis, and Vascular Biology 27, 2722-2728.
– reference: Mancini, S., Romanelli, R., Laschinger, C. A., Overall, C. M., Sodek, J. & McCulloch, C. A. (1999) Assessment of a novel screening test for neutrophil collagenase activity in the diagnosis of periodontal diseases. Journal of Periodontology 70, 1292-1302.
– reference: Romanelli, R., Mancini, S., Laschinger, C., Overall, C. M., Sodek, J. & McCulloch, C. A. (1999) Activation of neutrophil collagenase in periodontitis. Infection and Immunity 67, 2319-2326.
– reference: Könönen, E., Paju, S., Pussinen, P. J., Hyvönen, M., Di Tella, P., Suominen-Taipale, L. & Knuuttila, M. (2007) Population-based study of salivary carriage of periodontal pathogens in adults. Journal of Clinical Microbiology 45, 2446-2451.
– reference: Gursoy, U. K., Könönen, E., Uitto, V-J., Pussinen, P., Hyvärinen, K., Suominen-Taipale, L. & Knuuttila, M. (2009) Salivary interleukin-1β concentration and presence of multiple pathogens in periodontitis. Journal of Clinical Periodontology 36, 922-927.
– reference: Hanemaaijer, R., Sorsa, T., Konttinen, Y. T., Ding, Y., Sutinen, M., Visser, H., Van Hinsbergh, V. W., Helaakoski, T., Kainulainen, T., Rönkä, H., Tschesche, H. & Salo, T. (1997) Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. Journal of Biological Chemistry 12, 31504-31509.
– reference: Holopainen, J. M., Moilanen, J. A., Sorsa, T., Kivelä-Rajamäki, M., Tervahartiala, T., Vesaluoma, M. H. & Tervo, T. M. (2003) Activation of matrix metalloproteinase-8 by membrane type 1-MMP and their expression in human tears after photorefractive keratectomy. Investigative Ophthalmology and Visual Science 44, 2550-2556.
– reference: Lee, W., Aitken, S., Sodek, J. & McCulloch, C. A. (1995) Evidence of a direct relationship between neutrophil collagenase activity and periodontal tissue destruction in vivo: role of active enzyme in human periodontitis. Journal of Periodontal Research 30, 23-33.
– reference: Raitio, A., Tuomas, H., Kokkonen, N., Salo, T., Sorsa, T., Hanemaaijer, R. & Oikarinen, A. (2005) Levels of matrix metalloproteinase-2, -9 and -8 in the skin, serum and saliva of smokers and non-smokers. Archives of Dermatological Research 297, 242-248.
– reference: Sorsa, T., Hernández, M., Leppilahti, J., Munjal, S., Netuschil, L. & Mäntylä, P. (2010) Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods. Oral Diseases 16, 39-45.
– reference: Ramseier, C. A., Kinney, J. S., Herr, A. E., Braun, T., Sugai, J. V., Shelburne, C. A., Rayburn, L. A., Tran, H. M., Singh, A. K. & Giannobile, W. V. (2009) Identification of pathogen and host-response markers correlated with periodontal disease. Journal of Periodontology 80, 436-446.
– reference: Reynolds, J. J. (1996) Collagenases and tissue inhibitors of metalloproteinases: a functional balance in tissue degradation. Oral Diseases 2, 70-76.
– reference: Ingman, T., Tervahartiala, T., Ding, Y., Tschesche, H., Haerian, A., Kinane, D. F., Konttinen, Y. T. & Sorsa, T. (1996) Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients. Journal of Clinical Periodontology 23, 1127-1132.
– reference: Kinney, J. S., Ramseier, C. A. & Giannobile, W. V. (2007) Oral fluid-based biomarkers of alveolar bone loss in periodontitis. Annals of the New York Academy of Sciences 1098, 230-251.
– reference: Sorsa, T., Uitto, V-J., Suomalainen, K., Vauhkonen, M. & Lindy, S. (1988) Comparison of interstitial collagenases from human gingiva, sulcular fluid and polymorphonuclear leukocytes. Journal of Periodontal Research 23, 386-393.
– reference: Tobón-Arroyave, S. I., Jaramillo-González, P. E. & Isaza-Guzmán, D. M. (2008) Correlation between salivary IL-1β levels and periodontal clinical status. Archives of Oral Biology 53, 346-352.
– reference: Giannobile, W. V. (1997) Crevicular fluid biomarkers of oral bone loss. Current Opinion in Periodontology 4, 11-20.
– reference: Lorencini, M., Silva, J. A., De La Hoz, C. L., Carvalho, H. F. & Stach-Machado, D. R. (2009) Changes in MMPs and inflammatory cells in experimental gingivitis. Histology and Histopathology 24, 157-166.
– reference: Sorsa, T., Tjäderhane, L. & Salo, T. (2004) Matrix metalloproteinases (MMPs) in oral diseases. Oral Diseases 10, 311-318.
– reference: Syggelos, S. A., Eleftheriou, S. C., Giannopoulou, E., Panagiotopoulos, E. & Aletras, A. J. (2001) Gelatinolytic and collagenolytic activity in periprosthetic tissues from loose hip endoprostheses. Journal of Rheumatology 28, 1319-1329.
– reference: Teles, R. P., Sakellari, D., Teles, F. R. F., Konstantinidis, A., Kent, R., Socransky, S. S. & Haffajee, A. D. (2010) Relationships among gingival crevicular fluid biomarkers, clinical parameters of periodontal disease, and subgingival microbiota. Journal of Periodontology 81, 89-98.
– volume: 2
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Snippet Gursoy UK, Könönen E, Pradhan‐Palikhe P, Tervahartiala T, Pussinen PJ, Suominen‐Taipale L, Sorsa T. Salivary MMP‐8, TIMP‐1, and ICTP as markers of advanced...
Salivary matrix metalloproteinase (MMP)-8 and -14, tissue inhibitor of matrix metalloproteinase (TIMP)-1, and pyridinoline cross-linked carboxyterminal...
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StartPage 487
SubjectTerms Adult
Area Under Curve
Biological and medical sciences
Biomarkers - analysis
Collagen Type I
Enzyme-Linked Immunosorbent Assay
Facial bones, jaws, teeth, parodontium: diseases, semeiology
Female
Fluoroimmunoassay
Gingival Hemorrhage - classification
Humans
ICTP
Male
Matrix Metalloproteinase 14 - analysis
Matrix Metalloproteinase 8 - analysis
Medical sciences
Middle Aged
MMP-14
MMP-8
Non tumoral diseases
Otorhinolaryngology. Stomatology
Peptide Fragments - analysis
Peptides
Periodontal Index
Periodontal Pocket - classification
Periodontitis - diagnosis
Procollagen - analysis
ROC Curve
saliva
Saliva - chemistry
Saliva - enzymology
Smoking
TIMP-1
Tissue Inhibitor of Metalloproteinase-1 - analysis
Title Salivary MMP-8, TIMP-1, and ICTP as markers of advanced periodontitis
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https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1600-051X.2010.01563.x
https://www.ncbi.nlm.nih.gov/pubmed/20507371
https://www.proquest.com/docview/733109842
Volume 37
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