Periodontitis and peri-implantitis tissue levels of Treponema denticola-CTLP and its MMP-8 activating ability

• Published in: Acta histochemica Vol. 123; no. 6; p. 151767
• Main Authors: Petain, Sami, Kasnak, Gökhan, Firatli, Erhan, Tervahartiala, Taina, Gürsoy, Ulvi K., Sorsa, Timo
• Format: Journal Article
• Language: English
• Published: Germany Elsevier GmbH 01-09-2021
• Subjects: Adult; Bacterial Proteins - metabolism; Chymases - metabolism; collagenase-2; Enzyme Activation; Female; Humans; Male; Matrix Metalloproteinase 8 - metabolism; Medicin och hälsovetenskap; Middle Aged; MMP-8; Peri-implantitis; Peri-Implantitis - enzymology; Peri-Implantitis - microbiology; Periodontitis; Periodontitis - enzymology; Periodontitis - microbiology; Td-CTLP; Treponema denticola; Treponema denticola - enzymology; Treponemal Infections - enzymology; Treponemal Infections - microbiology; Treponema denticola; Peri-implantitis; MMP-8; collagenase-2; Td-CTLP; Periodontitis
• ISSN: 0065-1281; 1618-0372; 1618-0372
• DOI: 10.1016/j.acthis.2021.151767

Chymotrypsin-like-proteinase of Treponema denticola (Td-CTLP) can stimulate the protein expression and activation of matrix metalloproteinase (MMP)-8 (or collagenase-2), a potent tissue destructive enzyme from gingival cells in vitro. The aims of this study were 1) to demonstrate the proMMP-8 (or latent MMP-8) activation by Td-CTLP in vitro and 2) to detect Td-CTLP and MMP-8 protein levels in the tissue samples of peri-implantitis and periodontitis patients.
proMMP-8 activation by Td-CTLP was analyzed by immunoblots. Tissue specimens were collected from 38 systemically healthy and non-smoking patients; 14 of whom had moderate to severe periodontitis, 10 of whom were suffering from peri-implantitis, and finally 14 of whom showed no sign of periodontal inflammation nor radiological bone decay (control group). The immune-expression levels of MMP-8 and Td-CTLP in the epithelium and the connective tissue were analyzed immunohistochemically. A pixel color-intensity analyze was performed with ImageJ software (version 1.46c; Rasband WS, National Institutes of Health, Bethesda, MD, USA) to obtain a comparable numeral score for each patient’s epithelium and connective tissue MMP-8 and Td-CTLP enzyme level.
Td-CTLP activated proMMP-8 in vitro by converting the 70−75 kDa proMMP-8 to 65 kDa active MMP-8. Also, lower molecular size 25−50 kDa parts of MMP-8 were formed. There was no statistically significant difference between the study groups in terms of their MMP-8 and Td-CTLP levels in the epithelium or in the connective tissue.
Regarding the limits of this study, it can thus be said that the Td-CTLP enzyme can activate the host proMMP-8 enzyme. Tissue protein levels of MMP-8 and Td-CTLP do not seem to be changed in peri-implantitis and in periodontitis.