CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE

SORSA T, DING YL, INGMAN T, SALO T, WESTERLUND U, HAAPASALO M, Tschesche H, KONTTINEN YT (1995)
JOURNAL OF CLINICAL PERIODONTOLOGY 22(9): 709-717.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Dental plaque is the major aetiological factor in periodontal diseases and contains several proteolytic enzymes. The origin of these proteinases is, however, poorly studied. This study was undertaken to characterize collagenase present in dental plaque of adult periodontitis patients. Vertebrate-type rather than bacterial-derived collagenase activity was detected in extracts of both supra- and subgingival dental plaque extracts of adult periodontitis patients. Dental plaque collagenase was found to exist predominantly in autoactive form. Dental plaque collagenase from periodontally healthy individuals existed in latent form. Latent dental plaque collagenase from periodontitis lesions could be activated by a 95 kD chymotrypsin-like proteinase from Treponema denticola and human leukocyte cathepsin G but not by human plasmin. Incubation of purified latent leukocyte collagenase with whole cells of Fusobacterium nucleatum, Eubacterium saburreum, Prevotella buccae and Porphyromonas gingivalis, however, did not result to the activation of the enzyme. Doxycycline in vitro inhibited dental plaque collagenase with an IC50-value of 20 mu M. Dental plaque collagenase degraded more efficiently type I and II collagens than type III collagen. Western-blot analysis with specific anti-human neutrophil collagenase-antibody revealed that both in supra-and subgingival dental plaque extracts dental plaque collagenase had undergone proteolytic conversion from an 80 kD preform to a 58 kD active form which is associated with catalytic autoactivity as measured by functional collagenase assay. This reflects proteolytic activation of leukocyte collagenase in dental plaque probably by other proteases derived from potent periodontopathogenic bacteria such as T. denticola or other PMN proteases such as cathepsin G. Multiple different molecular weight gelatinases (20-200 kD) including fragmented low molecular weight human neutrophil 92 kD gelatinase species were detected in both supra- and subgingival dental plaque extracts. Leukocyte collagenase, previously found to be the main type of collagenase present in adult periodontitis gingiva, gingiva crevicular fluid and saliva, is also the predominant type of collagenase in the plaque of periodontitis patients. Fragmented but catalytically active neutrophil gelatinase species are also present in dental plaque. The dental plaque has potential to serve as a reservoir and site of activation of neutrophil (PMN)-derived matrix metalloproteinases in the periodontal inflammation.
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Zeitschriftentitel
JOURNAL OF CLINICAL PERIODONTOLOGY
Band
22
Zeitschriftennummer
9
Seite
709-717
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SORSA T, DING YL, INGMAN T, et al. CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE. JOURNAL OF CLINICAL PERIODONTOLOGY. 1995;22(9):709-717.
SORSA, T., DING, Y. L., INGMAN, T., SALO, T., WESTERLUND, U., HAAPASALO, M., Tschesche, H., et al. (1995). CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE. JOURNAL OF CLINICAL PERIODONTOLOGY, 22(9), 709-717. doi:10.1111/j.1600-051X.1995.tb00831.x
SORSA, T., DING, Y. L., INGMAN, T., SALO, T., WESTERLUND, U., HAAPASALO, M., Tschesche, H., and KONTTINEN, Y. T. (1995). CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE. JOURNAL OF CLINICAL PERIODONTOLOGY 22, 709-717.
SORSA, T., et al., 1995. CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE. JOURNAL OF CLINICAL PERIODONTOLOGY, 22(9), p 709-717.
T. SORSA, et al., “CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE”, JOURNAL OF CLINICAL PERIODONTOLOGY, vol. 22, 1995, pp. 709-717.
SORSA, T., DING, Y.L., INGMAN, T., SALO, T., WESTERLUND, U., HAAPASALO, M., Tschesche, H., KONTTINEN, Y.T.: CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE. JOURNAL OF CLINICAL PERIODONTOLOGY. 22, 709-717 (1995).
SORSA, T, DING, YL, INGMAN, T, SALO, T, WESTERLUND, U, HAAPASALO, M, Tschesche, Harald, and KONTTINEN, YT. “CELLULAR SOURCE, ACTIVATION AND INHIBITION OF DENTAL PLAQUE COLLAGENASE”. JOURNAL OF CLINICAL PERIODONTOLOGY 22.9 (1995): 709-717.

42 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Inhibition of proteolytic, serpinolytic, and progelatinase-b activation activities of periodontopathogens by doxycycline and the non-antimicrobial chemically modified tetracycline derivatives.
Grenier D, Plamondon P, Sorsa T, Lee HM, McNamara T, Ramamurthy NS, Golub LM, Teronen O, Mayrand D., J Periodontol 73(1), 2002
PMID: 11846203
The expression of MMP-8 in human odontoblasts and dental pulp cells is down-regulated by TGF-beta1.
Palosaari H, Wahlgren J, Larmas M, Rönkä H, Sorsa T, Salo T, Tjäderhane L., J Dent Res 79(1), 2000
PMID: 10690664
Inhibition of the activities of matrix metalloproteinases 2, 8, and 9 by chlorhexidine.
Gendron R, Grenier D, Sorsa T, Mayrand D., Clin Diagn Lab Immunol 6(3), 1999
PMID: 10225852
Activation of neutrophil collagenase in periodontitis.
Romanelli R, Mancini S, Laschinger C, Overall CM, Sodek J, McCulloch CA., Infect Immun 67(5), 1999
PMID: 10225890
Virulence factors of oral treponemes.
Fenno JC, McBride BC., Anaerobe 4(1), 1998
PMID: 16887619
The activation and function of host matrix metalloproteinases in dentin matrix breakdown in caries lesions.
Tjäderhane L, Larjava H, Sorsa T, Uitto VJ, Larmas M, Salo T., J Dent Res 77(8), 1998
PMID: 9719036
Cathepsin G in gingival tissue and crevicular fluid in adult periodontitis.
Tervahartiala T, Konttinen YT, INgman T, Häyrinen-Immonen R, Ding Y, Sorsa T., J Clin Periodontol 23(2), 1996
PMID: 8849841
Human neutrophil gelatinase and associated lipocalin in adult and localized juvenile periodontitis.
Westerlund U, Ingman T, Lukinmaa PL, Salo T, Kjeldsen L, Borregaard N, Tjäderhane L, Konttinen YT, Sorsa T., J Dent Res 75(8), 1996
PMID: 8906123
Matrix metalloproteinases-1 and -8 and TIMP-1 mRNA levels in normal and diseased human gingivae.
Aiba T, Akeno N, Kawane T, Okamoto H, Horiuchi N., Eur J Oral Sci 104(5-6), 1996
PMID: 9021326
Periodontal diseases: diagnosis.
Armitage GC., Ann Periodontol 1(1), 1996
PMID: 9118264
Non-surgical pocket therapy: pharmacotherapeutics.
Drisko CH., Ann Periodontol 1(1), 1996
PMID: 9118269
Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients.
Ingman T, Tervahartiala T, Ding Y, Tschesche H, Haerian A, Kinane DF, Konttinen YT, Sorsa T., J Clin Periodontol 23(12), 1996
PMID: 8997658

39 References

Daten bereitgestellt von Europe PubMed Central.

Activation of latent human neutrophil collagenase by reactive oxygen species and serine proteases.
Saari H, Suomalainen K, Lindy O, Konttinen YT, Sorsa T., Biochem. Biophys. Res. Commun. 171(3), 1990
PMID: 2171513
Collagenase, gelatinase and elastase activities in sulcular fluid of osseointegrated implants and natural teeth.
Ingman T, Kononen M, Konttinen YT, Siirila HS, Suomalainen K, Sorsa T., J. Clin. Periodontol. 21(4), 1994
PMID: 8195449
Multiple forms of gelatinases/type IV collagenases in saliva and gingival crevicular fluid of periodontitis patients.
Ingman T, Sorsa T, Lindy O, Koski H, Konttinen YT., J. Clin. Periodontol. 21(1), 1994
PMID: 8126240
Characterization of collagenolytic activity from strains of Bacteroides gingivalis.
Birkedal-Hansen H, Taylor RE, Zambon JJ, Barwa PK, Neiders ME., J. Periodont. Res. 23(4), 1988
PMID: 2846816
A trypsin-like protease from Bacteroides gingivalis: partial purification and characterization.
Sorsa T, Uitto VJ, Suomalainen K, Turto H, Lindy S., J. Periodont. Res. 22(5), 1987
PMID: 2826746
Comparison of interstitial collagenases from human gingiva, sulcular fluid and polymorphonuclear leukocytes.
Sorsa T, Uitto VJ, Suomalainen K, Vauhkonen M, Lindy S., J. Periodont. Res. 23(6), 1988
PMID: 2851042
Salivary collagenase. Origin, characteristics and relationship to periodontal health.
Uitto VJ, Suomalainen K, Sorsa T., J. Periodont. Res. 25(3), 1990
PMID: 2163444
Detection of interleukin-8 and matrix metalloproteinases transcripts in healthy and diseased gingival biopsies by RNA/PCR.
Tonetti MS, Freiburghaus K, Lang NP, Bickel M., J. Periodont. Res. 28(6 Pt 2), 1993
PMID: 8263721
Oxidative autoactivation of latent collagenase by human neutrophils.
Weiss SJ, Peppin G, Ortiz X, Ragsdale C, Test ST., Science 227(4688), 1985
PMID: 2982211
Effects of tetracyclines on neutrophil, gingival, and salivary collagenases. A functional and western-blot assessment with special reference to their cellular sources in periodontal diseases.
Sorsa T, Ding Y, Salo T, Lauhio A, Teronen O, Ingman T, Ohtani H, Andoh N, Takeha S, Konttinen YT., Ann. N. Y. Acad. Sci. 732(), 1994
PMID: 7978785
Collagenase activity in gingival crevicular fluid of patients with juvenile periodontitis.
Suomalainen K, Sorsa T, Saxen L, Vauhkonen M, Uitto VJ., Oral Microbiol. Immunol. 6(1), 1991
PMID: 1658711
Tetracycline inhibition identifies the cellular origin of interstitial collagenases in human periodontal diseases in vivo.
Suomalainen K, Sorsa T, Ingman T, Lindy O, Golub LM., Oral Microbiol. Immunol. 7(2), 1992
PMID: 1326740
Salivary collagenase, elastase- and trypsin-like proteases as biochemical markers of periodontal tissue destruction in adult and localized juvenile periodontitis.
Ingman T, Sorsa T, Konttinen YT, Liede K, Saari H, Lindy O, Suomalainen K., Oral Microbiol. Immunol. 8(5), 1993
PMID: 8265204

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