Activation of latent collagenase by microbial plaque

Robertson, Paul B.; Cobb, Charles M.; Taylor, Robert E.; Fullmer, Harold M.

doi:10.1111/j.1600-0765.1974.tb00657.x

Cited by 34 publications

(14 citation statements)

References 12 publications

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“…Considerable emphasis has been placed on the role of ver-tebrate collagenases elaborated by host celis commcm to the periodontium. Indeed, vertebrate collagenases similar to the enzyme originally described by Gross and Lapiere (15>62) have been demonstrated in human gingival explants (Fullmer 1970, Robertson et al 1974, alveolar bone (Fullmer & Lazarus 1969), polymorphcmuciear leukocytes (Lazarus et al 1968), macrophages (Wahl et al 1974, and fibroblasts (Hook, Hook & Brown 1974). The present study is consistent •with previous reports that certain members of the oral microflora also elaborate collagenase which may contribute to periodontal connective tissue degradation.…”

Section: Discussionmentioning

confidence: 77%

Collagenolytic activity associated with Bacteroides species and Actinobacillus actinomycetemcomitans

Robertson

Lantz

Marucha

et al. 1982

J of Periodontal Research

178

120

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Collagenolytic activity was assessed in a variety of microorganisms with particular emphasis on members of the indigenous oral flora. Organisms were grown in complete and peptide depleted basal anaerobic broth. Cell sonicates and media preparations were assayed for collagenolytic activity using 14C‐labelled collagen in solution and as fibrils. Assay reaction products were evaluated by acrylamide gel electrophoresis. All tested species of Bacteroides, including B. gingivalis, B, melaninogenicus ss. melaninogenicus and intermedius, B. capillus, B. oris, B. thetaiotaomicron, and B. fragilis produced collagenase which was primarily associated with the cell fraction. Collagenolytic activity was also observed in both media and cell sonicates of Actinobacillus actinomycetemcomitans, Strain 511. The Bacteroides and Actinobacillus enzymes were heat labile, inhibited by EDTA and human serum. Enzyme activity appeared to be enhanced when these organisms were grown in peptide depleted medium. Collagenase production by tested species of Bacteroides and A. actinomycetemcomitans (511) was unique among other members of the oral microflora including species of Fusobacterium, Actinomyces, Capnocylophaga, and Selenomonas, which did not demonstrate collagenolytic activity under the same cultural conditions.

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Section: Discussionmentioning

confidence: 77%

Collagenolytic activity associated with Bacteroides species and Actinobacillus actinomycetemcomitans

Robertson

Lantz

Marucha

et al. 1982

J of Periodontal Research

178

120

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“…Plaque has been shown to contain several types of proteolytic enzymes, and the proteolytic activity increases with increasing amounts of plaque (Soder 1972). Bacterial plaque enzyme extraet has been shown to be capable of hydrolyzing periodontal collagen (Makinen & Paunio 1966) and to activate latent collagenase (Robertson et al 1974, Uitto & Raeste 1978.…”

Section: Bacterial Proteasesmentioning

confidence: 99%

“…According to the latter author, the main sources of collagenase in periodontal tissues are fibroblasts, polymorphonuclear leukocytes (PMNs), macrophages, epithelial cells, and even endothelial cells. Collagenase has been shown to be released from the cells in a latent form and to be activated by a brief exposure to trypsin (Birkedal-Hansen et al 1975), a number of other proteolytic enzymes (Birkedal-Hansen 1980), or by bacterial plaque (Robertson et al 1974). High levels of collagenase have been found in gingival tissue in periodontitis (Fullmer et al 1969, Geiger & Harper 1980.…”

mentioning

confidence: 99%

Proteases and their inhibitors in chronic inflammatory periodontal disease

Sandholm

1986

J Clinic Periodontology

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This article reviews the current knowledge of the sources, function and interactions of proteolytic enzymes and their inhibitors in chronic inflammatory periodontal disease. Proteolytic tissue degradation is a typical phenomenon in chronic inflammatory periodontal disease. The proteolytic enzymes can be both host- and bacteria-derived. The proteases of the inflammatory cells are aimed for digestion of bacteria, enhanced locomotion through connective tissue, demarcation of the site of infection and tissue remodeling. Uncontrolled release of proteases in inflammation causes self-digestion and tissue destruction. The potential of the bacterial proteases in degradation of connective tissue is not yet known. Biochemical and immunologic mediators of inflammation are released by proteolytic reactions. Immunoglobulin-cleaving proteases present a specific mechanism in perturbation of host defenses. The 2 main protease inhibitors in serum, alpha-1-antitrypsin and alpha-2-macroglobulin, are also present in the gingival tissue fluid guarding the function of proteases. It has been suggested, although not confirmed, that deficiency in serum protease inhibiting capacity could be correlated with susceptibility to periodontal disease. Mucous secretions contain local low molecular weight protease inhibitors, but their possible rôle in saliva is not known. Bacteria-derived, antiproteolytic short peptides may prove to be useful in pharmacological control of tissue destruction at inflammatory sites.

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“…The role of bacterial collagenases in collagen turnover in vivo is not yet clear and it is uncertain if this bacterial enzyme is directly involved in host tissue damage. It has been suggested that extracellular proteinases activate latent host collagenases, which in turn can lead to the hydrolysis of collagen I and IV [17,18]. Furthermore, in spite of the numerous reports of collagenolytic activity by P. gingivalis, the location of this enzyme in the bacterial cell remains uncertain.…”

Section: Speciesmentioning

confidence: 99%