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The diagnostic potential of salivary protease activities in periodontal health and disease

Identifieur interne : 001447 ( Main/Exploration ); précédent : 001446; suivant : 001448

The diagnostic potential of salivary protease activities in periodontal health and disease

Auteurs : K. Thomadaki [États-Unis] ; Ja Bosch [Pays-Bas, Allemagne] ; Fg Oppenheim [États-Unis] ; Ej Helmerhorst [États-Unis]

Source :

Oral Diseases [ 1354-523X ] ; 2013-11.

RBID : ISTEX:2D1976030B516D20A73F9569C49B10D110B58F83

Descripteurs français

Wicri :
- topic : Médecine dentaire, Enzyme.

English descriptors

Abstract

Periodontal disease is characterised by proteolytic processes involving enzymes that are released by host immune cells and periodontal bacteria. These enzymes, when detectable in whole saliva, may serve as valuable diagnostic markers for disease states and progression. Because the substrate specificities of salivary proteases in periodontal health and disease are poorly characterised, we probed these activities using several relevant substrates: (i) gelatin and collagen type IV; (ii) the Arg/Lys–rich human salivary substrate histatin‐5; and (iii) a histatin‐derived synthetic analog benzyloxycarbonyl‐Arg‐Gly‐Tyr‐Arg‐methyl cumaryl amide (Z‐RGYR‐MCA). Substrate degradation was assessed in gel (zymography) and in solution. Whole saliva supernatant enzyme activities directed at gelatin, quantified from the 42 kDa, 92 kDa and 130 kDa bands in the zymograms, were 1.3, 1.4 and 2.0‐fold higher, respectively, in the periodontal patient group (P < 0.01), consistent with enhanced activities observed towards collagen type IV. On the other hand, histatin 5 degraded equally fast in healthy and periodontal patients' whole saliva supernatant samples (P > 0.10). Likewise, the hydrolysis rates of the Z‐RGYR‐MCA substrate were the same in the healthy and periodontal patient groups (P > 0.10). In conclusion, gelatinolytic/collagenolytic activities but not trypsin‐like activities in human saliva differentiate health from periodontal disease and may thus provide an adjuvant to diagnosis for monitoring disease activity.

Url:

https://api.istex.fr/document/2D1976030B516D20A73F9569C49B10D110B58F83/fulltext/pdf

DOI: 10.1111/odi.12069

Affiliations:

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Le document en format XML

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<front><div type="abstract">Periodontal disease is characterised by proteolytic processes involving enzymes that are released by host immune cells and periodontal bacteria. These enzymes, when detectable in whole saliva, may serve as valuable diagnostic markers for disease states and progression. Because the substrate specificities of salivary proteases in periodontal health and disease are poorly characterised, we probed these activities using several relevant substrates: (i) gelatin and collagen type IV; (ii) the Arg/Lys–rich human salivary substrate histatin‐5; and (iii) a histatin‐derived synthetic analog benzyloxycarbonyl‐Arg‐Gly‐Tyr‐Arg‐methyl cumaryl amide (Z‐RGYR‐MCA). Substrate degradation was assessed in gel (zymography) and in solution. Whole saliva supernatant enzyme activities directed at gelatin, quantified from the 42 kDa, 92 kDa and 130 kDa bands in the zymograms, were 1.3, 1.4 and 2.0‐fold higher, respectively, in the periodontal patient group (P < 0.01), consistent with enhanced activities observed towards collagen type IV. On the other hand, histatin 5 degraded equally fast in healthy and periodontal patients' whole saliva supernatant samples (P > 0.10). Likewise, the hydrolysis rates of the Z‐RGYR‐MCA substrate were the same in the healthy and periodontal patient groups (P > 0.10). In conclusion, gelatinolytic/collagenolytic activities but not trypsin‐like activities in human saliva differentiate health from periodontal disease and may thus provide an adjuvant to diagnosis for monitoring disease activity.</div>
</front>
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The diagnostic potential of salivary protease activities in periodontal health and disease

The diagnostic potential of salivary protease activities in periodontal health and disease

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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