Salivary collagenase, elastase‐and trypsin‐like proteases as biochemical markers of periodontal tissue destruction in adult and localized juvenile periodontitis

Abstract

The profile of salivary proteases and their cellular origin, with special reference to polymorphonuclear leukocytes and bacteria, was studied in localized juvenile periodontitis and compared with adult periodontitis and healthy controls. General proteolytic activity in saliva as well as collagenase, elastase-like and trypsin-like activity was measured. In addition, the sensitivity of salivary collagenase of patients with localized juvenile periodontitis to doxycycline inhibition was studied. The saliva of localized juvenile periodontitis patients contained low amounts of collagenase compared with adult periodontitis saliva, and almost all salivary collagenase was found to exist in endogenously active form, as was found to be the case also in adult periodontitis patients and healthy controls. The salivary collagenase of localized juvenile periodontitis patients was relatively insensitive to 100 mumol/l doxycycline but was completely inhibited by 600 mumol/l doxycycline, reflecting rather matrix metalloproteinase-1 (fibroblast-type) than matrix metalloproteinase-8 (polymorphonuclear leukocyte) enzyme. The saliva of localized juvenile periodontitis patients also contained low amounts of elastase-like activity compared with the saliva of untreated adult periodontitis patients. Scaling and root planing caused a significant decrease in elastase-like activity in the saliva of adult periodontitis patients. General proteolytic and trypsin-like activities were also low in the saliva of localized juvenile periodontitis patients. Furthermore, the reducing agent beta-mercaptoethanol did not activate or inhibit the salivary trypsin-like activity of localized juvenile periodontitis or adult periodontitis patients, although the reductant readily activated partially purified Porphyromonas gingivalis trypsin-like protease in a characteristic manner.(ABSTRACT TRUNCATED AT 250 WORDS)

In vivo inhibition of human neutrophil collagenase (MMP-8) activity during long-term combination therapy of doxycycline and non-steroidal anti-inflammatory drugs (NSAID) in acute reactive arthritis

“…Stimulated, whole salivary samples were collected from acute ReA patients before and after 2 months doxycycline treatment according to Ingman et al [22] and serum samples according to Bergman et al [23].…”

“…The purity of type I collagen substrate was examined by cyanogen bromide cleavage peptide analysis [22]. Human polymorphonuclear leucocyte and fibroblast type collagenases were purified from neutral salt extract of human neutrophils and human synovial fibroblast culture medium, respectively, as described previously [13,24,25].…”

“…Saliva samples were assayed for interstitial collagenase activities by the quantitative SDS PAGE Laser densitometric modification [17][18][19]21,22] of the original assay developed by Turto et al [26]. Salivary samples were assayed for interstitial collagenase activities with (total collagenase activity) and without (endogenously active interstitial collagenase) 1 mM aminophenylmercuric acetate (APMA) treatment, an optimal organomercurial activator of both latent fibroblasl type and neutrophil interstitial collagenases.…”

Factors Affecting IL-1-Mediated Collagen Metabolism By Fibroblasts and the Pathogenesis of Periodontal Disease: A Review of the Literature

“…(5) MMPS AND TIMPS IN SALIVA Collagenase, often in the active form, has been detected occasionally but not universally in fresh saliva from CAP and LIP patients (Larivee et al, 1986;Ingman et al, 1993;Hayakawa H, et al, 1994). TIMP-1 has been found in lower concentrations in whole saliva from periodontally diseased subjects than in that from clinically healthy and edentulous persons, and this trend was reversed by treatment (Hayakawa H, et al, 1994a (Schmidt et al, 1982;Kimball et al, 1984;Postlethwaite et al, 1988;Takeshita et al, 1992;DuFour et al, 1993) but far from all (D'Alessandro et al, 1985;Bitterman et al, 1986;Singh et al, 1988;Oates et al, 1993), studies.…”

Inhibition of Trypsin-Like Cysteine Proteinases (Gingipains) fromPorphyromonas gingivalisby Tetracycline and Its Analogues

“…Thus, when this is all taken into account it can be anticipated that inhibition of gingipains by antibiotics may significantly potentiate their therapeutic effects in the treatment of periodontitis. A recent report has indicated that treatment of periodontitis patients with minocycline reduced salivary protease activity (2), some of which is likely to be due to the presence of gingipains (31). This finding prompted us to investigate the direct inhibitory activity of tetracycline and its analogues for gingipains.…”