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Enzymes, dentinogenesis and dental caries: a literature review.

Larmas M, Sándor GK - J Oral Maxillofac Res (2014)

Bottom Line: Alkaline phosphatase activity sharply decreased when odontoblasts turned into quiescent odontoblasts.Specifically, matrix metalloproteases may have originated partly from activated proenzymes of host origin.Though dental studies are scanty when compared to bone, the active role of large spectrum of enzymes in healthy and carious dentine was given support.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pediatric Dentistry and Cariology, Institute of Dentistry, University of Oulu, Oulu Finland.

ABSTRACT

Objectives: Search in PubMed with keywords "enzymes, dentinogenesis, and dental caries" revealed only 4 items, but when combined with "enzymes, osteogenesis, and osteoporosis" as high as 404 items resulted. Dental caries was associated with an order of magnitude fewer studies than the chronic bone disease, osteoporosis. This observation motivated this review.

Material and methods: A comprehensive review of the available literature on role of enzymes in dentinogenesis and dental caries was undertaken using MEDLINE (PubMed) and Scopus. Keywords for the search were: enzymes and odontoblasts, enzymes and different forms of dentinogenesis as well as dental caries.

Results: Search revealed studies which described odontoblasts harbouring numerous enzymes (hydrolases, including metalloproteinases, transaminases and dehydrogenases) during primary dentinogenesis. Alkaline phosphatase activity sharply decreased when odontoblasts turned into quiescent odontoblasts. Tertiary dentinogenesis was characterized first by reactionary dentine formation when alkaline phosphatase was highly reactivated. Then later some of these odontoblasts may die out and be replaced by other progenitor cells of pulpal origin. This tertiary dentine was called reparative dentine. Pulpal progenitor/stem cells revealed alkaline phosphatase activity in areas encircling inflamed pulp sections. Soft carious dentine revealed high hydrolase, transaminase and dehyrogenase activities that may have originated from invading microbes, saliva or were endogenous. Proteolytic activity was especially demonstrable using histochemical and biochemical means. Specifically, matrix metalloproteases may have originated partly from activated proenzymes of host origin.

Conclusions: Though dental studies are scanty when compared to bone, the active role of large spectrum of enzymes in healthy and carious dentine was given support.

No MeSH data available.


Related in: MedlinePlus

Examples of the presence of certain hydrolases and oxido-reductases in soft carious dentine of extracted human molar teeth. A = Arylaminopeptidase activity in the dentinal tubules of soft carious dentin. Substrate: L-leucyl-2-naphthylamine, Fast Blue B, pH 7.0. Original magnification x48. B = Higher magnification (x165) of arylaminopeptidase on the borderland between hard (under) and soft carious dentine (above). C = Glocose-6-phosphate-dehyrogenase in soft carious dentine. Substrate: sodium glucose 6-phosphate, coenzyme: nitroblue tetrazolium, pH 8.0. Original magnification x48. D = Succinate dehydrogenase in the predentine layer under a carious lesion. Substrate: sodium succinate, coenzyme: neotetrazolium, pH 7.8. Original magnification x451. E = Lactate dehyrorogenase activity in the soft carious dentine. Substrate: sodium lactate, coenzyme: NAD, nitroblue tetrazolium, pH 8.0. Original magnification x48. F = Higher magnification (x451) of lactate dehydrogenase activity on the borderland between hard (fractured) and soft carious dentine revealing enzyme activity in dentinal tubules, ahead microorganims. The picture is reconstructed from the original slides published by Larmas et al. in Acta Odontol Scand 26: 127-136, 1968 (A and B) and Larmas in Arch oral Biol. 17: 1143-1153, 1972 (C - F).
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fig1: Examples of the presence of certain hydrolases and oxido-reductases in soft carious dentine of extracted human molar teeth. A = Arylaminopeptidase activity in the dentinal tubules of soft carious dentin. Substrate: L-leucyl-2-naphthylamine, Fast Blue B, pH 7.0. Original magnification x48. B = Higher magnification (x165) of arylaminopeptidase on the borderland between hard (under) and soft carious dentine (above). C = Glocose-6-phosphate-dehyrogenase in soft carious dentine. Substrate: sodium glucose 6-phosphate, coenzyme: nitroblue tetrazolium, pH 8.0. Original magnification x48. D = Succinate dehydrogenase in the predentine layer under a carious lesion. Substrate: sodium succinate, coenzyme: neotetrazolium, pH 7.8. Original magnification x451. E = Lactate dehyrorogenase activity in the soft carious dentine. Substrate: sodium lactate, coenzyme: NAD, nitroblue tetrazolium, pH 8.0. Original magnification x48. F = Higher magnification (x451) of lactate dehydrogenase activity on the borderland between hard (fractured) and soft carious dentine revealing enzyme activity in dentinal tubules, ahead microorganims. The picture is reconstructed from the original slides published by Larmas et al. in Acta Odontol Scand 26: 127-136, 1968 (A and B) and Larmas in Arch oral Biol. 17: 1143-1153, 1972 (C - F).

Mentions: Histochemical methods of the localization of many enzymes in sound and carious human teeth in different developmental or pathological stages were conducted some decades ago (Figure 1). Hydrolysis of numerous naphthol derivatives was histochemically detected in the dental plaque on advanced carious lesions and in the tubules of soft carious dentine, indicating the occurrence of arylaminopeptidases [32], carboxylic ester hydrolases [33], acid phosphatase [34], phosphoamidases, pyrophosphatases, glycosidases, and arylsulphatase [35] in dentinal tubules of soft carious dentine (Figure 1). Dental plaque and dentinal tubules of carious dentine also revealed LDH, glucose-6-phosphate, and SDH activity (Figure 1E, 1F), LDH activity was demonstrable even in the area where no microorganisms (Figure 1F) were seen under the carious lesion [36].


Enzymes, dentinogenesis and dental caries: a literature review.

Larmas M, Sándor GK - J Oral Maxillofac Res (2014)

Examples of the presence of certain hydrolases and oxido-reductases in soft carious dentine of extracted human molar teeth. A = Arylaminopeptidase activity in the dentinal tubules of soft carious dentin. Substrate: L-leucyl-2-naphthylamine, Fast Blue B, pH 7.0. Original magnification x48. B = Higher magnification (x165) of arylaminopeptidase on the borderland between hard (under) and soft carious dentine (above). C = Glocose-6-phosphate-dehyrogenase in soft carious dentine. Substrate: sodium glucose 6-phosphate, coenzyme: nitroblue tetrazolium, pH 8.0. Original magnification x48. D = Succinate dehydrogenase in the predentine layer under a carious lesion. Substrate: sodium succinate, coenzyme: neotetrazolium, pH 7.8. Original magnification x451. E = Lactate dehyrorogenase activity in the soft carious dentine. Substrate: sodium lactate, coenzyme: NAD, nitroblue tetrazolium, pH 8.0. Original magnification x48. F = Higher magnification (x451) of lactate dehydrogenase activity on the borderland between hard (fractured) and soft carious dentine revealing enzyme activity in dentinal tubules, ahead microorganims. The picture is reconstructed from the original slides published by Larmas et al. in Acta Odontol Scand 26: 127-136, 1968 (A and B) and Larmas in Arch oral Biol. 17: 1143-1153, 1972 (C - F).
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4306321&req=5

fig1: Examples of the presence of certain hydrolases and oxido-reductases in soft carious dentine of extracted human molar teeth. A = Arylaminopeptidase activity in the dentinal tubules of soft carious dentin. Substrate: L-leucyl-2-naphthylamine, Fast Blue B, pH 7.0. Original magnification x48. B = Higher magnification (x165) of arylaminopeptidase on the borderland between hard (under) and soft carious dentine (above). C = Glocose-6-phosphate-dehyrogenase in soft carious dentine. Substrate: sodium glucose 6-phosphate, coenzyme: nitroblue tetrazolium, pH 8.0. Original magnification x48. D = Succinate dehydrogenase in the predentine layer under a carious lesion. Substrate: sodium succinate, coenzyme: neotetrazolium, pH 7.8. Original magnification x451. E = Lactate dehyrorogenase activity in the soft carious dentine. Substrate: sodium lactate, coenzyme: NAD, nitroblue tetrazolium, pH 8.0. Original magnification x48. F = Higher magnification (x451) of lactate dehydrogenase activity on the borderland between hard (fractured) and soft carious dentine revealing enzyme activity in dentinal tubules, ahead microorganims. The picture is reconstructed from the original slides published by Larmas et al. in Acta Odontol Scand 26: 127-136, 1968 (A and B) and Larmas in Arch oral Biol. 17: 1143-1153, 1972 (C - F).
Mentions: Histochemical methods of the localization of many enzymes in sound and carious human teeth in different developmental or pathological stages were conducted some decades ago (Figure 1). Hydrolysis of numerous naphthol derivatives was histochemically detected in the dental plaque on advanced carious lesions and in the tubules of soft carious dentine, indicating the occurrence of arylaminopeptidases [32], carboxylic ester hydrolases [33], acid phosphatase [34], phosphoamidases, pyrophosphatases, glycosidases, and arylsulphatase [35] in dentinal tubules of soft carious dentine (Figure 1). Dental plaque and dentinal tubules of carious dentine also revealed LDH, glucose-6-phosphate, and SDH activity (Figure 1E, 1F), LDH activity was demonstrable even in the area where no microorganisms (Figure 1F) were seen under the carious lesion [36].

Bottom Line: Alkaline phosphatase activity sharply decreased when odontoblasts turned into quiescent odontoblasts.Specifically, matrix metalloproteases may have originated partly from activated proenzymes of host origin.Though dental studies are scanty when compared to bone, the active role of large spectrum of enzymes in healthy and carious dentine was given support.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Pediatric Dentistry and Cariology, Institute of Dentistry, University of Oulu, Oulu Finland.

ABSTRACT

Objectives: Search in PubMed with keywords "enzymes, dentinogenesis, and dental caries" revealed only 4 items, but when combined with "enzymes, osteogenesis, and osteoporosis" as high as 404 items resulted. Dental caries was associated with an order of magnitude fewer studies than the chronic bone disease, osteoporosis. This observation motivated this review.

Material and methods: A comprehensive review of the available literature on role of enzymes in dentinogenesis and dental caries was undertaken using MEDLINE (PubMed) and Scopus. Keywords for the search were: enzymes and odontoblasts, enzymes and different forms of dentinogenesis as well as dental caries.

Results: Search revealed studies which described odontoblasts harbouring numerous enzymes (hydrolases, including metalloproteinases, transaminases and dehydrogenases) during primary dentinogenesis. Alkaline phosphatase activity sharply decreased when odontoblasts turned into quiescent odontoblasts. Tertiary dentinogenesis was characterized first by reactionary dentine formation when alkaline phosphatase was highly reactivated. Then later some of these odontoblasts may die out and be replaced by other progenitor cells of pulpal origin. This tertiary dentine was called reparative dentine. Pulpal progenitor/stem cells revealed alkaline phosphatase activity in areas encircling inflamed pulp sections. Soft carious dentine revealed high hydrolase, transaminase and dehyrogenase activities that may have originated from invading microbes, saliva or were endogenous. Proteolytic activity was especially demonstrable using histochemical and biochemical means. Specifically, matrix metalloproteases may have originated partly from activated proenzymes of host origin.

Conclusions: Though dental studies are scanty when compared to bone, the active role of large spectrum of enzymes in healthy and carious dentine was given support.

No MeSH data available.


Related in: MedlinePlus