GC MI Paste with Recaldent Research

Home > Recaldent > MI Paste > Research

J Dent Res. 1997 Sep;76(9):1587-95.

Remineralization of enamel subsurface lesions by casein phosphopeptide-stabilized calcium phosphate solutions.

Reynolds EC.

Biochemistry and Molecular Biology Unit, School of Dental Science, University ofvMelbourne, Australia.

Casein phosphopeptides (CPP) stabilize amorphous calcium phosphate (ACP), localize ACP in dental plaque, and are anticariogenic in animal and in situ human caries model. In this vitro study, CPP-stabilized calcium phosphate solutions were shown to remineralize subsurface lesions in human third-molar enamel. Solutions were used examine the effect of CPP-calcium phosphate concentration on remineralization.

Other solutions were used to examine the effect of increasing pH, which decreased the concentrations of free calcium and phosphate ions and increased the level of CPP-bound ACP. Although most of the remineralizing solutions were supersaturated with respect to the amorphous and crystalline calcium phosphate phases, the solutions were stabilized by the CPP such that spontaneous precipitation of calcium phosphate did not occur. After a ten-day remineralization period, enamel lesions were sectioned, subjected to microradiography, and the mineral content determined by microdensitometry. All solutions deposited mineral into the bodies of the lesions, with the 1.0% CPP-calcium phosphate (pH 7.0) solution replacing 63.9 +/- 20.1% of mineral lost at an averaged rate of 3.9 +/- 0.8 x 10(-8) mol hydroxyapatite/m2/s. The remineralizing capacity was greater for the solutions with the higher levels of CPP-stabilized free calcium and phosphate ions. Remineralization was not significantly correlated with either the CPP-bound ACP of the degrees of saturation for hydroxyapatite, octacalcium phosphate, or ACP. However, remineralization was significantly correlated with the degree of saturation for dicalcium phosphate dihydrate (CaHPO4.2H2O), but his was attributed to the significant correlation of

remineralization with the activity gradients from the solution into the lesion of some calcium phosphate ions and ion pairs, in particular the neutral ion pair CaHPO4(0). The CPP, by stabilizing calcium phosphate in solution, maintain high-concentration gradients of calcium and phosphate ions and ion pairs into the subsurface lesion and thus effect high rates of enamel remineralization.

PMID: 9294493 [PubMed - indexed for MEDLINE]

Arch Oral Biol. 2000 Jul;45(7):569-75.

Effects of an anticariogenic casein phosphopeptide on calcium diffusion in streptococcal model dental plaques.

Rose RK.

Division of Restorative Dentistry, The Dental School, Bristol, UK.

keith.rose@bristol.ac.uk

Casein phosphopeptides (CPP) stabilize amorphous calcium phosphate (ACP) and may be used to localize ACP in dental plaque, maintaining a state of supersaturation with respect to tooth enamel, reducing demineralization and enhancing remineralization. The aim here was to investigate these effects by measuring the effect of CPP-ACP on calcium diffusion in plaque. Using Dibdin's effusion system, calcium diffusion was measured in streptococcal model plaques. This demonstrated that by providing a large number of possible binding sites for calcium, 0.1% CPP-ACP reduces the calcium diffusion coefficient by about 65% at pH 7 and 35% at pH 5.

Hence, CPP-ACP binds well to plaque, providing a large calcium reservoir within the plaque and slowing diffusion of free calcium. This is likely to restrict mineral loss during a cariogenic episode and provide a potential source of calcium for subsequent remineralization. Overall, once in place, CPP-ACP will restrict the caries process.

PMID: 10785520 [PubMed - indexed for MEDLINE]

J Dent Res. 1996 Oct;75(10):1779-88.

Incorporation of caseinoglycomacropeptide andcasein ophosphopeptide into the salivary pellicle inhibits adherence of mutans streptococci.

Schupbach P, Neeser JR, Golliard M, Rouvet M, Guggenheim B.

Institute of Oral Microbiology and General Immunology, University of Zurich,

Switzerland.

The protective effects of milk and milk products against dental caries have been demonstrated in many animal studies. We have shown that this effect was mediated by micellar casein or caseinopeptide derivatives. A reduction in the Streptococcus sobrinus population in the oral microbiota of animals fed diets supplemented withthese milk components was consistently observed. A possible explanation for these findings is that milk components are incorporated into the salivary pellicle, thereby reducing the adherence of S. sobrinus. This hypothesis was tested in vitro by the incubation of bovine enamel discs with unstimulated saliva. The resulting pellicle was

washed and incubated with caseinoglycomacropeptide (CGMP) and/or

caseinophosphopeptide (CPP) labeled with 17- and 12-nm gold particles. All samples were prepared for electron microscopy by high-pressure freezing followed by freezesubstitution.It was demonstrated by high-resolution scanning electron microscopy

with back-scattered electron imaging, as well as by transmission electron

microscopy, that both peptides were incorporated into the pellicle in exchange for albumin, confirming previous findings. This protein was identified with a mouse antihuman serum albumin followed by goat anti-mouse IgG labeled with 25-nm gold particles. Incorporation of CGMP and/or CPP into salivary pellicles reduced the adherence of both S. sobrinus and S. mutans significantly. It is suggested that the calcium and phosphate-rich micellar casein or caseinopeptides are incorporated into the pellicle. The resulting ecological shifts, together with the increased remineralization potential of this biofilm, may explain its modified cariogenic

potential.

PMID: 8955673 [PubMed - indexed for MEDLINE]

J Dent Res. 1978 Feb;57(2):187-93.

Dentin permeability: determinants of hydraulic conductance.

Reeder OW Jr, Walton RE, Livingston MJ, Pashley DH.

A technique is described which permits measurements of the ease with which fluid permeates dentin. This value, the hydraulic conductance of dentin, increased as surface area increases and/or as dentin thickness decreases. It increased 32-fold when dentin was acid etched due to removal of surface debris occluding the tubules.

PMID: 277512 [PubMed - indexed for MEDLINE]

J Dent Res. 2001 Dec;80(12):2066-70.

Comment in:

J Dent Res. 2002 Apr;81(4):228.

Remineralization of enamel subsurface lesions by sugarfree chewing gum containing casein phosphopeptideamorphous calcium phosphate.

Shen P, Cai F, Nowicki A, Vincent J, Reynolds EC.

School of Dental Science, The University of Melbourne, Victoria, Australia.

Casein phosphopeptide-amorphous calcium phosphate nanocomplexes (CPP-ACP)exhibit anticariogenic potential in laboratory, animal, and human in situ experiments. The aim of this study was to determine the ability of CPP-ACP in sugar-free chewing gum to remineralize enamel subsurface lesions in a human in situ model. Thirty subjects in randomized, cross-over, double-blind studies wore removable palatal appliances with six human-enamel half-slabs inset containing sub-surface demineralized lesions. The appliances were inserted immediately before gumchewing for 20 min and then retained for another 20 min. This was performed four times per day for 14 days. At the completion of each treatment, the enamel halfslabs were paired with their respective demineralized control half-slabs, embedded, sectioned, and subjected to microradiography and densitometric image analysis, for

measurement of the level of remineralization. The addition of CPP-ACP to either sorbitol- or xylitol-based gum resulted in a dose-related increase in enamel remineralization, with 0.19, 10.0, 18.8, and 56.4 mg of CPP-ACP producing an increase in enamel remineralization of 9, 63, 102, and 152%, respectively, relative to the control gum, independent of gum weight or type.

Publication Types:

Clinical Trial

Randomized Controlled Trial

PMID: 11808763 [PubMed - indexed for MEDLINE]

Spec Care Dentist. 1998 Jan-Feb;18(1):8-16.

Anticariogenic complexes of amorphous calcium phosphate stabilized by casein phosphopeptides: a review.

Reynolds EC.

School of Dental Science, University of Melbourne, Australia.

Using laboratory, animal, and human in situ caries models, investigators have shown

that casein phosphopeptide amorphous calcium phosphate complexes (CPP-ACP)exhibit an anticariogenic activity. The casein phosphopeptides (CPP) are producedfrom a tryptic digest of the milk protein casein by aggregation with calciumphosphate and purification by ultrafiltration. The CPP have a remarkable ability to stabilize calcium phosphate in solution and substantially increase the level of calcium phosphate in dental plaque. Through their multiple phosphoseryl residues, the CPP bind to forming clusters of amorphous calcium phosphate (ACP) in metastable solution, preventing their growth to the critical size required for nucleation and precipitation. The proposed mechanism of anticariogenicity for the CPP-ACP is that

they localize ACP in dental plaque, which buffers the free calcium and phosphate lon

Review

Review, Tutorial

PMID: 9791302 [PubMed - indexed for MEDLINE]

CLICK HERE TO BUY MI PASTE!