The dynamics of formation of a collagen-phosphophoryn conjugate in relation to the passage of the mineralization front in rat incisor dentin.

Maier, Gerhard; Lechner, Joseph H.; Veis, Arthur

doi:10.1016/s0021-9258(18)33007-2

Cited by 35 publications

(13 citation statements)

References 24 publications

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“…This avoided any confusion with dentin collagen and non-collagenous matrix components that also incorporate high amounts of serine and proline. L-[3-3H]serine was used to avoid labeled glycine as a result of the Veis, 1978;Maier et al, 1983), since both serine and glycine are prominent amino acid constituents of enamel proteins (Eastoe, 1979;Termine et al, 1979;Strawich and Glimcher, 1985;MacDougall et al, 1998b). In amelogenins, approximately one-quarter of all amino acid residues are proline (250/1000 amino acids).…”

Section: Discussionmentioning

confidence: 99%

Inositol Hexasulphate, a Casein Kinase Inhibitor, Alters Enamel Formation in Cultured Embryonic Mouse Tooth Germs

Torres‐Quintana¹,

Lécolle²,

Septier³

et al. 2000

J Dent Res

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Post-translational modification of enamel proteins is regulated by casein kinases (CK) and results in binding sites for calcium ions that subsequently play a key role during the initial stages of mineralization. Phosphorylation may also influence the secretion and extracellular organization of enamel proteins. Previous studies indicated that inositol hexasulphate inhibited the activity of CK-I and/or CK-II in mouse tooth germs (Torres-Quintana et al., 1998). We hypothesized that inositol hexasulphate would also inhibit the activity of the specific casein kinase(s) identified in secretory ameloblasts, and would prove useful for determination of the extent to which phosphorylation might influence the organization of enamel proteins at early stages of enamel formation. To test this hypothesis, we dissected mandibular first molars from 18-day-old mouse embryos and cultured them for 11 days in the presence of 0-0.1 mM inositol hexasulphate. Ultastructural analysis revealed that the formation of enamel was largely impaired at an inhibitor concentration > or = 0.08 mM. Quantitative radioautographic analysis of [33P]phosphate incorporation indicated that radiolabeled phosphate normally secreted into forming enamel was retained within ameloblasts. In contrast, no significant difference was observed between control and inositol-hexasulphate-treated tooth germs when cultures were labeled with [3H]serine and [3H]proline. SDS-PAGE and Western blot analysis confirmed that while inositol hexasulphate inhibited CK-mediated phosphorylation, it did not significantly alter protein synthesis. We conclude that impairment of phosphorylation leads to intracellular accumulation of [3H]phosphate-containing material by ameloblasts. We also conclude that when non-phosphorylated enamel matrix proteins are secreted, they are either unable to form an enamel matrix that supports mineralization, or they diffuse throughout a poorly mineralized dentin.

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Section: Discussionmentioning

confidence: 99%

Inositol Hexasulphate, a Casein Kinase Inhibitor, Alters Enamel Formation in Cultured Embryonic Mouse Tooth Germs

Torres‐Quintana¹,

Lécolle²,

Septier³

et al. 2000

J Dent Res

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“…CP nanocomposites following different iterations (1,4,8,12) of precipitation were characterized using X-ray diffraction (XRD), SEM, X-ray dispersive analysis, and z potential measurements as described earlier for the protein-coated SNPs. For XRD, samples were prepared by drying the sediment on an aluminum sample dish and the spectrum was obtained using a Rigaku mini-flex system, scanning 2q from 20 to 50 at a speed of 0.02 per min.…”

Section: Characterization Of Np-cp Compositesmentioning

confidence: 99%

“…1,2 For example, in bone mineralization, collagen fibers are interwoven with hydroxyapatite (HAp) (a type of calcium phosphate (CP)) 3 and phosphoproteins such as bone sialoprotein (BSP) are thought to mediate the nucleation of HAp. 2,4 While this complexity cannot be mimicked through simple engineering of a material surface (or interface), establishing semi-empirical relationships between surface variables such as charge, radius of curvature, and protein structural requirements on HAp formation can aid in the development of materials that can foster bone formation in vivo.…”

Section: Introductionmentioning

confidence: 99%

Influence of surface charge and protein intermediary layer on the formation of biomimetic calcium phosphate on silica nanoparticles

2012

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The biomineralization process in bone involves the assembly of calcium phosphate (CP) as a bioinorganic nanocomposite in association with extracellular matrix proteins. Towards developing synthetic systems that can promote the formation of biomimetic hydroxyapatite, the formation of CP from solution onto the surfaces of a model system composed of silica nanoparticles (SNPs) of differing physiochemical characteristics was studied. In addition to varying charge, two protein mediators collagen and phosvitin were adsorbed onto the surface of SNPs to form protein-coated SNPs, and the precipitation of CP onto the SNP from solutions containing physiologically relevant concentrations of calcium and phosphate ions was studied. A comparison of zeta potential (z) versus pH isotherms between the protein-coated SNP and native protein reveals deviation in z that can be attributed to perturbation in the protein structure. Analysis of the z versus pH isotherms for CP-protein-silica nanocomposites and the native CP indicates that CP deposition on SNPs occurs in a heterogeneous manner with segregated regions of CP. Interestingly, SNP composites containing phosvitin exhibit lower component segregation relative to composites containing collagen, and that the difference in segregation originates from the difference in z of each adsorbed protein. This suggests that proteinmediated biomineralization might be governed by surface energetics as much as biology.

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“…The PP was shown to be associated with mineralized dentin (Carmichael et al, 1977) and absent from the predentin. The soluble PP from rat incisors was not homogeneous, shown both on gels and by biosynthetic labeling studies (DiMuzio and Veis, 1978a,b;Maier et al, 1981Maier et al, , 1983. 31 P-NMR studies verified that the phosphates were phosphate esters, with pK ␣ = 6.8 (Lee et al, 1977).…”

mentioning

confidence: 99%

Biomineralization: On the Trail of the Phosphate. Part II: Phosphophoryn, the DMPs, and More

Veis

2004

J Dent Res

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The dynamics of formation of a collagen-phosphophoryn conjugate in relation to the passage of the mineralization front in rat incisor dentin.

Cited by 35 publications

References 24 publications

Inositol Hexasulphate, a Casein Kinase Inhibitor, Alters Enamel Formation in Cultured Embryonic Mouse Tooth Germs

Inositol Hexasulphate, a Casein Kinase Inhibitor, Alters Enamel Formation in Cultured Embryonic Mouse Tooth Germs

Influence of surface charge and protein intermediary layer on the formation of biomimetic calcium phosphate on silica nanoparticles

Biomineralization: On the Trail of the Phosphate. Part II: Phosphophoryn, the DMPs, and More

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