Collagenase, Dipeptidylpeptidase IV, and Cathepsin D Activities in Gingival Fluid and Whole Saliva from Patients with Periodontal Disease

Ando, Kazue

doi:10.2329/perio.22.387

Cited by 19 publications

(6 citation statements)

References 18 publications

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“…Glycyl-prolyl-p3-naphthylamidase activity is often signifi-| Is | cantly elevated in periodontitis lesions as compared with healthy 8 T6T32128 periodontal sites (Ando, 1980). In this study, almost all the black-pigmented Bacteroides strains, especially B. gingivalis, strongly hydrolyzed dipeptide substrates, including glycyl-Lroth on N-CBzproline-4-methoxy-,3-naphthylamide.…”

Section: Discussionmentioning

confidence: 53%

Arylaminopeptidase Activities of Oral Bacteria

et al. 1986

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Protease and peptidase enzymes are thought to play a role in the virulence of many oral organisms, especially those associated with periodontal diseases. In order to evaluate the peptidases of periodontopathogens, we compared the arylaminopeptidase activities of Bacteroides gingivalis with those of other oral and non-oral bacteria. Sixty-three bacterial strains representing the prominent cultivable organisms in human periodontal pockets were tested, including representatives of the black-pigmented Bacteroides, Actinobacillus, Actinomyces, Campylobacter, Capnocytophaga, Eikenella, Fusobacterium, Haemophilus, Lactobacillus, Streptococcus, and Veillonella species. Each micro-organism was examined for its ability to hydrolyze 18 synthetic substrates of beta-naphthylamide derivatives of amino acids, dipeptides, and tripeptides. Quantitation of the enzyme activity was accomplished by colorimetric measurement of the amounts of released beta-naphthylamines. N-CBz-glycyl-glycyl-L-arginine-beta-naphthylamide was readily cleaved by B. gingivalis, but slightly or not at all by the other oral strains tested. L-arginine-beta-naphthylamide was cleaved by B. gingivalis, Capnocytophaga species, and Streptococcus species, but not readily by the other Bacteroides strains. Some dipeptide substrates tested, such as glycyl-L-arginine- and glycyl-L-proline-beta-naphthylamide, were strongly cleaved by B. gingivalis and weakly cleaved by other Bacteroides strains. Since high levels of N-CBz-glycyl-glycyl-L-arginyl-aminopeptidase activity are characteristic of B. gingivalis, its measurement may be valuable in the identification of this organism in clinical samples as an aid in diagnosis and monitoring of periodontal infections. Furthermore, this and other aminopeptidases produced by B. gingivalis and other oral organisms may play a role in the tissue destruction seen in periodontal disease.

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Section: Discussionmentioning

confidence: 53%

Arylaminopeptidase Activities of Oral Bacteria

et al. 1986

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“…DPP IV is found in several human tissues (45)(46)(47) and a similar enzyme has been purified from B. gingivalis (8,10). DPP IV-like activity has also been reported in GCF (48); this increased with the severity of periodontal disease but was not characterized. Enzyme activity was detected with glycyl-proline-containing substrates in all these studies.…”

Section: Detection Of Crevicular Fluid Proteases 359mentioning

confidence: 97%

“…Our findings in this case are thus compatible with the observed increase with bacterial counts of DPP IV-like activity in subgingival material (II). The host component indicated in our GCF activity could, as with the trypsinlike enzyme(s), have derived from serum, inflamed gingival tissue or saliva, since DPP IV-like activity is present in all these sources (8,45,48,50).…”

Section: Detection Of Crevicular Fluid Proteases 359mentioning

confidence: 99%

Detection of cathepsin B‐ and L‐, elstase‐, tryptase‐, trypsin‐, and dipeptidyl peptidase IV‐like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7‐amino‐4‐trifluoromethyl coumarin

Cox

Eley

1989

J of Periodontal Research

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Crevicular fluid samples were collected from 20 gingivitis and periodontitis patients using filter paper strips; these were then eluted into buffer. Portions of each sample were combined and the activities of this pooled eluate against different peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin (AFC) were examined with respect to their pH profiles and effector responses. Ca-thepsin B- and L-like activity was detected with Bz-Val-Lys-Lys-Arg-AFC; elastase-like activity with MeOSuc-Ala-Ala-Pro-Val-AFC; tryptase-like activity with Z-Ala-Ala-Lys-AFC; trypsin-like activity with Z-Gly-Gly-Arg-AFC; and dipeptidyl peptidase (DPP) IV-like activity with Ala-Pro-AFC. The selectivity and sensitivity of these assays were improved by choice of appropriate conditions. The cathepsin B- and L-, elastase-, tryptase-, and trypsin-like activities all had properties consistent with those from host sources, whilst partial inactivation of the DPP IV-like activity by heat treatment (60 degrees C for 30 min) suggested that it may have represented a mixture of human and Bacteroides gingivalis enzymes. Individual patient eluates showed wide variations in enzyme concentrations, but generally elastase-like activity was by far the highest. The sensitivity of the assays with AFC-linked substrates was such that it should prove possible to measure all five different types of activity in crevicular fluid samples from local periodontal disease sites.

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“…The 24 subjects studied had activities (Nakamura 1979), collagenase and not received dental treatment and had not dipeptidyl peptidase IV activities (Ando taken any antibiotics for at least three 1980), cathepsin D activity (Nakamura months prior to this study. 1979, Ando 1980, kininase activity (Tonzetich et al 1969) and unspecified proteolytic Saliva enzyme activity (Chauncey 1961) appear to Eight milliliters of mixed whole unstimuincrease with increasing severity of lated saliva was collected by expectoration periodontal disease. In addition, certain en-following a brief rinsing of the mouth with zyme activities of the gingival crevicular water, and the saliva was centrifuged at fiuid correlate positively with the degree of 5,000 x g for 15 min at 4°C.…”

mentioning

confidence: 99%

Salivary enzymes

Nakamura¹,

Slots²

1983

J of Periodontal Research

129

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Seventy‐six enzyme activities of mixed whole saliva, parotid saliva, serum, and polymorphonuclear leukocytes were examined in 10 individuals with healthy periodontium, 10 adult periodontitis patients, and 4 localized juvenile periodontitis patients by using the API ZYM (Analytab Products Inc., Plainview, N. Y.) and API ZYM AP (API System, La Balme les Grottes, France) semi‐quantitative micromethod systems. Enzymes assayed included phosphatases, esterase, lipase, glycosidases, and proteases including numerous aminopeptidases. Among the three study groups, mixed whole saliva of adult periodontitis patients revealed the highest and mixed whole saliva of healthy individuals the lowest enzyme activities. Statistically significant differences were found for alkaline phosphatase, esterase, β‐glucuronidase, α‐glucosidase, and some aminopeptidases. Bacterial sediment of whole saliva exhibited higher enzyme activities than whole saliva supernatant. Serum contained numerous aminopeptidases which were virtually undetectable in whole saliva. Some enzyme activities found in mixed whole saliva could not be detected in parotid saliva. Polymorphonuclear leukocytes demonstrated a distinct enzyme profile. The present study shows that varying enzyme profiles exist among the various components which make up whole saliva. It also indicates that numerous salivary enzymes originate from oral microorganisms and that the enzyme activity of whole saliva is higher in individuals with periodontal disease than in periodontally healthy subjects.

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Collagenase, Dipeptidylpeptidase IV, and Cathepsin D Activities in Gingival Fluid and Whole Saliva from Patients with Periodontal Disease

Cited by 19 publications

References 18 publications

Arylaminopeptidase Activities of Oral Bacteria

Arylaminopeptidase Activities of Oral Bacteria

Detection of cathepsin B‐ and L‐, elstase‐, tryptase‐, trypsin‐, and dipeptidyl peptidase IV‐like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7‐amino‐4‐trifluoromethyl coumarin

Salivary enzymes

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