Sorsa T, Ingman T, Suomalainen K, Haapasalo M, Konttinen Y T, Lindy O, Saari H, Uitto V J
Department of Periodontology, University of Helsinki, Finland.
Infect Immun. 1992 Nov;60(11):4491-5. doi: 10.1128/iai.60.11.4491-4495.1992.
Activation of latent human fibroblast-type and neutrophil interstitial procollagenases as well as degradation of native type I collagen by supra- and 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 Prevotella intermedia (ATCC 25261), Prevotella buccae (ES 57), Prevotella oris (ATCC 33573), Porphyromonas endodontalis (ES 54b), Actinobacillus actinomycetemcomitans (ATCC 295222), Fusobacterium nucleatum (ATCC 10953), Mitsuokella 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 supra- and 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.
研究了龈上和龈下牙菌斑提取物、牙龈卟啉单胞菌（ATCC 33277）的一种80 kDa类胰蛋白酶、具核梭杆菌（ATCC 29522）的一种95 kDa类糜蛋白酶以及牙周炎中常见分离出的特定细菌种类对人潜伏性成纤维细胞型和中性粒细胞间质前胶原酶的激活作用以及对天然I型胶原的降解作用。所包含的细菌有中间普氏菌（ATCC 25261）、颊普氏菌（ES 57）、口腔普氏菌（ATCC 33573）、牙髓卟啉单胞菌（ES 54b）、伴放线放线杆菌（ATCC 295222）、具核梭杆菌（ATCC 10953）、齿垢密螺旋体（DSM 3688）和缓症链球菌（ATCC 15909）。没有一种细菌能激活潜伏性前胶原酶；然而，发现龈上和龈下牙菌斑提取物（中性盐提取物）以及从潜在牙周病原菌牙龈卟啉单胞菌和具核梭杆菌的细胞提取物中分离出的蛋白酶能激活人潜伏性成纤维细胞型和中性粒细胞间质前胶原酶。与中性粒细胞的间质胶原酶相比，细菌蛋白酶对成纤维细胞型间质胶原酶的激活更有效，而中性粒细胞间质胶原酶更倾向于被氧化剂次氯酸进行非蛋白水解激活。这些蛋白酶不能将金属蛋白酶组织抑制剂（TIMP - 1）复合物转化为活性形式，也不能改变TIMP - 1抑制间质胶原酶的能力。所研究的细菌、牙龈卟啉单胞菌和具核梭杆菌的蛋白酶以及龈上和龈下牙菌斑提取物均未显示出任何显著的胶原溶解活性。然而，这些蛋白酶在被间质胶原酶和明胶酶切割后能降解天然和变性的胶原片段。我们的结果表明，牙周病原菌的蛋白酶可作为人前胶原酶的直接蛋白水解激活剂并降解胶原片段。因此，细菌蛋白酶可能与宿主酶协同参与牙周组织破坏。
