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.

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.

Sorsa T, Uitto V-J, Suomalainen K, Turto H and Lindy S: A trypsin-like protease from Bacteroides gingivalis: partial purification and characterization. J Periodont Res 1987; 22: 375-380. Extracts of cell sonicates of Bacteroides gingivalis were shown to contain proteolytic enzymes capable of degrading connective tissue proteins. In this study, neutral proteolytic enzymes, i.e. coilagenase and a trypsin-like protease, were isolated. The trypsin-like protease was readily separated from coliagenase by affinity chromatography on Benzamidine-Sepharose, Proteases were further purified by gel filtration on Sephacryl S-200; apparent molecular weights of 35 kDa and 70 kDa were obtained for a trypsin-like protease and coilagenase, respectively. Further characterization of the potent trypsin-like protease showed that the enzyme was inhibited by serine protease inhibitors phenylmethylsulfonyl fiuoride and benzamidine and by metalloprotease inhibitor EDTA, as well as ascorbic acid. Activation of the enzyme was observed with reducing agents and human serum. The trypsin-like protease was found to be capable of degrading native type IV collagen and denatured type I collagen but not native type I collagen. Thus, we conclude that in addition to coUagenase a potent trypsin-like protease from Bacteroides gingivalis may be involved in the etiopathogenesis of periodontal disease. Since the trypsin-like protease is able to degrade the basement membrane collagen (type IV) in the presence of human serum, this enzyme may be a potent virulence factor of Bacteroides gingivalis in relation to invasiveness and connective tissue destruction.

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