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1.
J Clin Pediatr Dent ; 39(1): 57-9, 2014.
Article in English | MEDLINE | ID: mdl-25631728

ABSTRACT

Matrix metalloproteinases (MMPs) seem to play a dual role in dentistry. While several MMPs have an important role to play in developmental defects of teeth and in caries, some MMPs also seem to have a defensive role. The main organic component of tooth structure is collagen and MMPs that degrade collagen and the extra cellular matrix have been implicated in progression of dental caries. MMPs have also been shown to be active in pulpitis and studies have shown that they can be used as diagnostic markers of pulpal inflammation. This paper reviews the role of MMPs in restorative dentistry and endodontics.


Subject(s)
Matrix Metalloproteinases/physiology , Tooth Diseases/enzymology , Tooth/enzymology , Biomarkers/analysis , Dental Caries/enzymology , Dental Pulp Diseases/enzymology , Humans , Matrix Metalloproteinases/analysis
2.
Drug Alcohol Depend ; 129(1-2): 33-40, 2013 Apr 01.
Article in English | MEDLINE | ID: mdl-23026815

ABSTRACT

BACKGROUND: A sensitive alcohol marker, ß-hexosaminidase (HEX), in the saliva of alcoholics, is investigated for the first time. METHODS: The activity, specific-activity and output of total HEX and its isoenzymes HEX A and HEX B were measured in the saliva of healthy controls (C), alcohol-dependent non-smokers (ANS), and alcohol-dependent smokers (AS). RESULTS: We observed a significantly increased activity/specific-activity and output of HEX A in the ANS and AS groups, due to the inflammatory state of the oral-cavity/salivary-glands. Significantly increased activity of HEX A contributed to an increase in the salivary activity of the total HEX in the ANS group. A significant decrease in the activity/specific-activity of HEX B in AS seemed to be due to HEX B inactivation by cigarette smoke. We noticed a tendency for deteriorated dental state (lower decayed-missing-filled-teeth index - DMFT), worse periodontal state (higher gingival index - GI and papilla-bleeding index - PBI) in AS, and worse periodontal state (higher GI) in ANS, as compared to the controls. We found no differences in the salivary protein concentrations between all groups and decreased salivary flow in both alcoholic groups as compared to the controls. In alcoholics, the area under the curve (AUC) for HEX A activity/specific-activity was significantly greater than for HEX and HEX B. The salivary HEX A activity/specific-activity had good/excellent sensitivity and specificity in smoking and non-smoking alcoholics, whereas salivary HEX and HEX B had poor/fair sensitivity and specificity. CONCLUSIONS: Salivary HEX A may be helpful in the diagnosis of chronic alcohol intoxication, even in smokers.


Subject(s)
Alcoholism/enzymology , Hexosaminidases/analysis , Periodontal Diseases/enzymology , Saliva/enzymology , Smoking/metabolism , Tooth Diseases/enzymology , Adult , Alcoholism/complications , Area Under Curve , Biomarkers , Data Interpretation, Statistical , Female , Gingiva/pathology , Health Status , Humans , Isoenzymes/analysis , Male , Middle Aged , Mouth/enzymology , Mouth/pathology , Periodontal Diseases/complications , Periodontal Diseases/pathology , Periodontal Index , Salivary Proteins and Peptides/analysis , Smoking/adverse effects , Tooth Diseases/complications , Tooth Diseases/pathology , Young Adult
4.
Zhonghua Kou Qiang Yi Xue Za Zhi ; 34(6): 341-3, 1999 Nov.
Article in Chinese | MEDLINE | ID: mdl-11776874

ABSTRACT

OBJECTIVE: To direct selecting proper sampling methods and sites in clinical research. METHODS: Gingival crevicular fluid (GCF) was sampled separately at the mesial-buccal and distal-buccal sites in the same teeth, which were destroyed differently. Clinical parameters were recorded in the subject sites and its adjacent sites. Aspartate Aminotransferase (AST) and Alkaline Phosphatase (ALP) in the GCF were determined. Difference of the enzyme levels between the two sampling sites, and relations between the enzyme level and all the clinical parameters were assessed. RESULTS: GCF-AST, ALP per sample at severely diseased sites were much higher than that from healthy and/or mild sites in the same teeth. Significant positive correlation (P < 0.001, r > 0.5) was demonstrated between enzyme levels in the sampling sites and probing depth (PD) and attachment level (AL) of the lingual sites. However, there was mild significant correlation (P < 0.05, r = 0.275) between ALP level in the sampling sites and PD of the proximal-buccal sites of its adjacent teeth. No significant correlation (P > 0.05) was found between AST level in the sampling sites and PD, AL of the adjacent teeth sites, and also between ALP level in the sampling sites and AL of the adjacent teeth sites. CONCLUSION: Site-specificity of periodontal disease was further demonstrated. GCF components were influenced reciprocally more obviously in the same proximal than by other sites.


Subject(s)
Gingival Crevicular Fluid/enzymology , Tooth/enzymology , Adult , Alkaline Phosphatase/metabolism , Aspartate Aminotransferases/metabolism , Female , Humans , Male , Middle Aged , Tooth/pathology , Tooth Diseases/enzymology
5.
Lab Delo ; (4): 13-5, 1991.
Article in Russian | MEDLINE | ID: mdl-1715420

ABSTRACT

A micromethod for lysozyme measurement with a Uniskan-1 spectrophotometer has been developed. The concentration of this enzyme was measured in 5-10 microliters of saliva and blood. Lysozyme levels were measured in miners of deep mines who had various dental conditions.


Subject(s)
Muramidase/blood , Nephelometry and Turbidimetry/methods , Saliva/enzymology , Coal Mining , Humans , Periodontal Diseases/enzymology , Tooth Diseases/enzymology
7.
J Dent Res ; 59(3): 594-601, 1980 Mar.
Article in English | MEDLINE | ID: mdl-6937492

ABSTRACT

The presence of a mucopolysaccharidase in resorbing deciduous teeth was investigated using histochemical techniques. The loss of toluidine blue metachromasia within glycosaminoglycan film substrates indicated the presence of enzyme activity, and was related to physiologic resorption. Such activity was localized to the periodontal ligament of these teeth.


Subject(s)
Glucuronidase/metabolism , Lyases/metabolism , Tooth Resorption/enzymology , Tooth, Deciduous/enzymology , Adolescent , Adult , Ankylosis/enzymology , Child , Humans , Periodontal Ligament/enzymology , Tooth/enzymology , Tooth Diseases/enzymology , Tooth Root/enzymology , Tooth, Supernumerary/enzymology
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