Ulvi K Gürsoy1, Eija Könönen1,2, Taina Tervahartiala3, Mervi Gürsoy1, Jari Pitkänen3, Paula Torvi3, Anna Liisa Suominen4,5,6, Pirkko Pussinen3, Timo Sorsa3,7. 1. Periodontology, Institute of Dentistry, University of Turku, Turku, Finland. 2. Welfare Division, Oral Health Care, Turku, Finland. 3. Department of Oral and Maxillofacial Disease, Helsinki University Hospital, University of Helsinki, Helsinki, Finland. 4. Institute of Dentistry, University of Eastern Finland, Kuopio, Finland. 5. Health Monitoring Unit, National Institute for Health and Welfare, Helsinki, Finland. 6. Department of Oral and Maxillofacial Diseases, Kuopio University Hospital, Kuopio, Finland. 7. Periodontology, Department of Dental Medicine, Karolinska Institutet, Huddinge, Sweden.
Abstract
AIM: To investigate the molecular forms of salivary matrix metalloproteinase (MMP)-8 in relation to periodontitis. MATERIALS AND METHODS: Molecular forms, degree of activation and fragmentation of neutrophilic and mesenchymal-type MMP-8 isoforms were analysed from salivary samples of 81 subjects with generalized periodontitis, 63 subjects with localized periodontitis and 79 subjects without pocket teeth, by using western-immunoblots with computer quantitation. In addition, human recombinant proMMP-8 was in vitro activated by Treponema denticola chymotrypsin-like protease (Td-CTLP), sodium hypochlorite (NaOCl, 1 mM, oxidant) or amino phenyl mercuric acetate (APMA, 1 mM). RESULTS: In saliva of periodontitis-affected individuals, MMP-8 is found in multiple forms, that is, complexes, active and pro-forms of neutrophilic and mesenchymal-type MMP-8, and especially 20-27 kDa fragments. The quantity of these fragments was elevated in both localized and generalized forms of periodontitis. Moreover, the tested activators (Td-CTLP, NaOCl and APMA) activated inactive proMMP-8, resulting in fragments of 20-27 kDa, in vitro, and salivary concentrations of T. denticola correlated significantly with salivary levels of fragmented MMP-8. CONCLUSION: The present results indicate that during the development and progression of periodontitis, MMP-8 appears as activated and fragmented, and treponemal proteases most likely play role in this cascade.
AIM: To investigate the molecular forms of salivary matrix metalloproteinase (MMP)-8 in relation to periodontitis. MATERIALS AND METHODS: Molecular forms, degree of activation and fragmentation of neutrophilic and mesenchymal-type MMP-8 isoforms were analysed from salivary samples of 81 subjects with generalized periodontitis, 63 subjects with localized periodontitis and 79 subjects without pocket teeth, by using western-immunoblots with computer quantitation. In addition, human recombinant proMMP-8 was in vitro activated by Treponema denticola chymotrypsin-like protease (Td-CTLP), sodium hypochlorite (NaOCl, 1 mM, oxidant) or amino phenyl mercuric acetate (APMA, 1 mM). RESULTS: In saliva of periodontitis-affected individuals, MMP-8 is found in multiple forms, that is, complexes, active and pro-forms of neutrophilic and mesenchymal-type MMP-8, and especially 20-27 kDa fragments. The quantity of these fragments was elevated in both localized and generalized forms of periodontitis. Moreover, the tested activators (Td-CTLP, NaOCl and APMA) activated inactive proMMP-8, resulting in fragments of 20-27 kDa, in vitro, and salivary concentrations of T. denticola correlated significantly with salivary levels of fragmented MMP-8. CONCLUSION: The present results indicate that during the development and progression of periodontitis, MMP-8 appears as activated and fragmented, and treponemal proteases most likely play role in this cascade.
Authors: Jemima Ho; Giorgio Camilli; James S Griffiths; Jonathan P Richardson; Nessim Kichik; Julian R Naglik Journal: Immunology Date: 2020-09-13 Impact factor: 7.397
Authors: Panagiota Katsiki; Kamran Nazmi; Bruno G Loos; Marja L Laine; Kim Schaap; Esen Hepdenizli; Floris J Bikker; Henk S Brand; Enno C I Veerman; Elena A Nicu Journal: J Clin Periodontol Date: 2021-06-20 Impact factor: 8.728