Sorsa T, Uitto V-J, Suomalainen K, Vauhkonen M, Lindy S.: Comparison of interstitial coliagenases from human gingiva, sulcular fluid and polymorphonuclear leukocytes. J Periodont Res 1988: 23: 386-393. Mammalian coliagenases (EC 3.4,24,7) have been suggested as playing an essential role in the initiation of the collagen degradation in periodontal diseases. Two distinct types of interstitial coliagenases have been characterized in vertebrate tissues. These enzymes, the fibrobiast-and the neutrophil-type coliagenases,, differ in molecular weight and antigenic properties, as well as substrate specificity and mechanism of activation. In order to determine the cellular origin and mode of action of coliagenase in periodontal tissue, we studied the molecular size, the substrate specificity and the activation of coliagenases partially purified from inflamed human gingival extracts, sulcular fluid, gingival expiant culture medium and polymorphonuclear leukocytes (PMN). Types I, II and III collagens used as substrates were purifted from bovine tendon, cartilage and amnion membrane, respectively. Apparent molecular weights of 70-75 k were obtained for gingival extract, sulcular fluid and PMN coliagenases and 45 k for gingival expiant culture collagenase by gel filtration technique. The gingival extract and sulcular fiuid coliagenases as well as PMN collagenase could be activated by gold thioglucose and gold thiomalate; no activation of gingival expiant culture collagenase was noted. The gingival extract collagenase. sulcular fluid collagenase and PMN collagenase degraded preferentially types I and 11 collagens relative to type-Ill collagen. In contrast, gingival expiant culture coliagenase degraded preferentially types I and III collagens relative to type-II collagen. The results indicate that collagenase in extracts of inflamed human gingiva and in sulcular fluid during inflammation is mostly derived from PMN cells. On the other hand, collagenase produced by gingival explants in culture is probably synthesized by fibrobiasts.

Persistently elevated GCF MMP-8 concentrations may indicate sites at risk, as well as patients with poor response to conventional periodontal treatment (e.g. SRP). MMP-8 testing may be useful as an adjunct to traditional periodontal diagnostic methods during the maintenance phase.

Activation of latent human fibroblast-type and neutrophil interstitial procollagenases as well as degradation of native type I collagen by supraand subgingival dental plaque extracts, an 80-kDa trypsinlike protease from Porphyromas gingivalis (ATCC 33277), a 95-kDa chymotrypsinlike protease from Treponema denticola (ATCC 29522), and selected bacterial species commonly isolated in periodontitis was studied. The bacteria included were PrevotelUa intermedia (ATCC 25261), PrevoteUla buccae (ES 57), PrevoteUa oris (ATCC 33573), Porphyromonas endodontalis (ES 54b), Actinobacillus actinomycetemcomitans (ATCC 295222), Fusobacterium nukeatum (ATCC 10953), Mitsuokela dentalis (DSM 3688), and Streptococcus mitis (ATCC 15909). None of the bacteria activated latent procollagenases; however, both sub-and supragingival dental plaque extracts (neutral salt extraction) and proteases isolated from cell extracts from potentially periodontopathogenic bacteria P. gingivalis and T. denticola were found to activate latent human fibroblast-type and neutrophil interstitial procollagenases. The fibroblast-type interstitial collagenase was more efficiently activated by bacterial proteases than the neutrophil counterpart, which instead preferred nonproteolytic activation by the oxidative agent hypochlorous acid. The proteases were not able to convert collagenase tissue inhibitor of metalloproteinase (TIMP-1) complexes into active form or to change the ability of TIMP-1 to inhibit interstitial collagenase. None of the studied bacteria, proteases from P. gingivalis and T. denticola, or extracts of supraand subgingival dental plaque showed any significant collagenolytic activity. However, the proteases degraded native and denatured collagen fragments after cleavage by interstitial collagenase and gelatinase. Our results indicate that proteases from periodontopathogenic bacteria can act as direct proteolytic activators of human procollagenases and degrade collagen fragments. Thus, in concert with host enzymes the bacterial proteases may participate in periodontal tissue destruction.

BackgroundInflammatory processes are considered to participate in the development of cardiovascular disease (CVD). Statins have been used successfully in the prevention and treatment of coronary heart disease. Chronic periodontitis has been suggested to contribute to CVD. The aim of this study was to examine the association of statin use and clinical markers of chronic periodontitis.MethodsPeriodontal probing pocket depth (PPD) values were collected from dental records of 100 consecutive adult patients referred to a university dental clinic for treatment of advanced chronic periodontitis. A novel index, Periodontal Inflammatory Burden Index (PIBI), was derived from the PPD values to estimate systemic effects of periodontitis.ResultsPeriodontitis patients taking statins had a 37% lower number of pathological periodontal pockets than those without statin medication (P = 0.00043). PIBI, which combines and unifies the data on PPD, was 40% smaller in statin using patients than in patients without statin (P = 0.00069). PIBI of subjects on simvastatin and atorvastatin both differed significantly from patients without statin and were on the same level. The subjects' number of teeth had no effect on the resultsConclusionPatients on statin medication exhibit fewer signs of periodontal inflammatory injury than subjects without the statin regimen. PIBI provides a tool for monitoring inflammatory load of chronic periodontitis. The apparent beneficial effects of statins may in part be mediated by their pleiotropic anti-inflammatory effect on periodontal tissue.