Ultrastructural localization of alkaline and acid phosphatase activities in dental plaque

Storto, Stefano; Silvestrini, G.; Bonucci, E.

doi:10.1111/j.1600-0765.1992.tb01664.x

Cited by 13 publications

(5 citation statements)

References 32 publications

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“…ALP hydrolysed phosphoserine, phosphothreonine and phosphotyrosine with little differences at different pH values. ALP is located intracellularly [2,3]. Intracellular pH is easily changed [37].…”

Section: Discussionmentioning

confidence: 99%

Amino Acid Phosphatase Activity of Alkaline Phosphatase

Shinozaki

Watanabe

Arita

et al. 1995

European Journal of Biochemistry

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Alkaline phosphatase (ALP) hydrolyzed phosvitin and amino acid phosphates demonstrating nonisotropy at different pH. Orthovanadate, a protein phosphatase inhibitor, more specifically inhibited the serine and tyrosine phosphatase activities of ALP than that of threonine phosphatase at concentrations >0.1 mM or 0.01 mM, respectively. Calyculin A and okadaic acid at increased concentrations increased ALP amino acid phosphatase activity. Bisphosphonates, such as disodium-I -hydroxy-1 -aminopropylidine-1 ,I-diphosphonate (APD) and ethane-1-hydroxy-I ,I-diphosphonate (HEBP), at increased concentrations, inhibited ALP amino acid phosphatase activity. These results suggest that ALP may function as a protein phosphatase. In terms of protein kinase inhibitors, N-[2-(metylamino)ethyl]-5-isoquinolinesulfonamide, N-(6-arninoheyxl)-5-chloro-l-naphthalenesulfomide hydrochloride and 4',5,7-trihydroxyisoflavone had little effect on ALP amino acid phosphatase activity. Staurosporine slightly enhanced ALP serine and threonine phosphatase activities at a concentration of 0.1 mM. These results suggest that protein phosphatase activity does not depend on the protein kinase activity of ALP, since duality between the former and the latter is not supported. ALP may function less as a protein kinase than as a protein phosphatase. The coupling mechanism of phosphate dynamics may be regulated indirectly.Keywords. Alkaline phosphatase ; amino acid phosphatase ; protein phosphatase ; protein kinase ; intracellular functions.Alkaline phosphatase (ALP) is expressed in most tissues [I] and located intracellularly [2, 31. However, the biological function of ALP is still unclear [l, 41. Recently, phosphate ester hydrolysis [5] as well as protein phosphorylation [6-91 in biological systems has been recognized as an important process in the control of cellular metabolism. It is uncertain whether or not ALP can work as a protein phosphatase, although it has broad substrate specificity [I, 4, 101. ALP has not only phosphate hydrolysis activity but also transphosphorylating activity [ll]. The evidence suggests that ALP may work as a protein kinase as well as a protein phosphatase. In order to demonstrate the natural ligand of ALP, we investigated the effects of protein phosphatase inhibitors, protein kinase inhibitors and bisphosphonates on ALP. and Sumitomo Pharmaceuticals Co., respectively. Acid-washed glassware and disposable plasticware were used throughout these experiments. Hydrolysis of phosvitin by ALP. 0.1 mM phosvitin was incubated with 5 U ALP in 800 p1 0.1 M Tris/HCl with different pH at 37°C for 30 min. Controls without ALP were routinely included to adjust for nonenzymic hydrolysis of substrate. The ALP protein phosphatase activity was evaluated as release of inorganic phosphate, measured as described by Chen et al. [12] with some modifications. The absorbance was read at 620nm using a spectrophotometer . EXPERIMENTAL PROCEDURES MaterialsEffects of pH on ALP amino acid phosphatase activity. 1 mh4 amino acid phosphates was incubated w...

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Section: Discussionmentioning

confidence: 99%

Amino Acid Phosphatase Activity of Alkaline Phosphatase

Shinozaki

Watanabe

Arita

et al. 1995

European Journal of Biochemistry

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“…There is good evidence that plaque bacteria produce alkaline phosphatase, and a recent histological study by Lo Storto et al, (1992) demonstrated the presence of ALP in the periplasmic spaces of gram -ve bacteria and also in the extracellular plaque matrix. The extracellular enzyme was found attached to the membranes around small microbial vesicles and also non-complexed in the intermicrobial ground space, without any association to specific structures.…”

Section: Discussionmentioning

confidence: 99%

Site‐specific alkaline phosphatase levels in gingival crevicular fluid in health and gingivitis: cross‐sectional studies

Chapple¹,

Glenwright²,

Matthews³

et al. 1994

J Clinic Periodontology

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Using a recently developed chemiluminescent assay enabling alkaline phosphatase (ALP) quantification in nanolitre volumes of gingival crevicular fluid (GCF), we have investigated GCF ALP levels in health and in the presence of gingivitis. In gingival health, there was a site-specific pattern of ALP concentration with higher enzyme concentrations around the upper and lower anterior teeth. Furthermore, clinically normal sites that had been subjected to different levels of plaque control produced significantly different ALP levels, (p < 0.03). This indicates that biochemical components of GCF may be used to measure subclinical inflammatory status. The ratio of GCF to serum ALP varied from 6:1 to 11:1, suggesting that a major source of the enzyme is through local production. The main cross-sectional study of 30 patients with gingivitis (276 sites) demonstrated that total GCF ALP levels, collected over a 30-s sampling time were higher for a gingival index of 1 than of 0 (p < 0.014). There was no significant relationship between total GCF ALP and plaque levels of the enzyme, and analysis of plaque within the study group demonstrated very low levels of ALP, indicating that the enzyme is likely to be largely derived from the periodontal tissues. The ratio of GCF ALP levels to those of saliva within individuals was 530:1, thereby eliminating saliva contamination as a risk, when total GCF ALP is being measured.

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“…The association of exogenous polyPs with mineral inhibition may have prevented Takazoe and Nakamura [ 102 ] from associating these intracellular granules within Bacterionema matruchotii as a Pi source for phosphate mineral formation. The identification of polyP within Bacterionema matruchotii , and the association of APase activity with bacteria of dental plaque [ 106 , 107 ] provide two clues to a possible chemical mechanism for increasing calcium phosphate mineral supersaturation within oral microbial biofilms.…”

Section: Biologically Induced Apatite Nucleation: Oral Bacteriamentioning

confidence: 99%

A Review of Phosphate Mineral Nucleation in Biology and Geobiology

et al. 2013

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Relationships between geological phosphorite deposition and biological apatite nucleation have often been overlooked. However, similarities in biological apatite and phosphorite mineralogy suggest that their chemical formation mechanisms may be similar. This review serves to draw parallels between two newly described phosphorite mineralization processes, and proposes a similar novel mechanism for biologically controlled apatite mineral nucleation. This mechanism integrates polyphosphate biochemistry with crystal nucleation theory. Recently, the roles of polyphosphates in the nucleation of marine phosphorites were discovered. Marine bacteria and diatoms have been shown to store and concentrate inorganic phosphate (Pi) as amorphous, polyphosphate granules. Subsequent release of these P reserves into the local marine environment as Pi results in biologically induced phosphorite nucleation. Pi storage and release through an intracellular polyphosphate intermediate may also occur in mineralizing oral bacteria. Polyphosphates may be associated with biologically controlled apatite nucleation within vertebrates and invertebrates. Historically, biological apatite nucleation has been attributed to either a biochemical increase in local Pi concentration or matrix-mediated apatite nucleation control. This review proposes a mechanism that integrates both theories. Intracellular and extracellular amorphous granules, rich in both calcium and phosphorus, have been observed in apatite-biomineralizing vertebrates, protists, and atremate brachiopods. These granules may represent stores of calcium-polyphosphate. Not unlike phosphorite nucleation by bacteria and diatoms, polyphosphate depolymerization to Pi would be controlled by phosphatase activity. Enzymatic polyphosphate depolymerization would increase apatite saturation to the level required for mineral nucleation, while matrix proteins would simultaneously control the progression of new biological apatite formation.

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Ultrastructural localization of alkaline and acid phosphatase activities in dental plaque

Cited by 13 publications

References 32 publications

Amino Acid Phosphatase Activity of Alkaline Phosphatase

Amino Acid Phosphatase Activity of Alkaline Phosphatase

Site‐specific alkaline phosphatase levels in gingival crevicular fluid in health and gingivitis: cross‐sectional studies

A Review of Phosphate Mineral Nucleation in Biology and Geobiology

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