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Molecular mechanisms of dental enamel formation.
Crit Rev Oral Biol Med. 1995; 6(2):84-108.CR

Abstract

Tooth enamel is a unique mineralized tissue in that it is acellular, is more highly mineralized, and is comprised of individual crystallites that are larger and more oriented than other mineralized tissues. Dental enamel forms by matrix-mediated biomineralization. Enamel crystallites precipitate from a supersaturated solution within a well-delineated biological compartment. Mature enamel crystallites are comprised of non-stoichiometric carbonated calcium hydroxyapatite. The earliest crystallites appear suddenly at the dentino-enamel junction (DEJ) as rapidly growing thin ribbons. The shape and growth patterns of these crystallites can be interpreted as evidence for a precursor phase of octacalcium phosphate (OCP). An OCP crystal displays on its (100) face a surface that may act as a template for hydroxyapatite (OHAp) precipitation. Octacalcium phosphate is less stable than hydroxyapatite and can hydrolyze to OHAp. During this process, one unit cell of octacalcium phosphate is converted into two unit cells of hydroxyapatite. During the precipitation of the mineral phase, the degree of saturation of the enamel fluid is regulated. Proteins in the enamel matrix may buffer calcium and hydrogen ion concentrations as a strategy to preclude the precipitation of competing calcium phosphate solid phases. Tuftelin is an acidic enamel protein that concentrates at the DEJ and may participate in the nucleation of enamel crystals. Other enamel proteins may regulate crystal habit by binding to specific faces of the mineral and inhibiting growth. Structural analyses of recombinant amelogenin are consistent with a functional role in establishing and maintaining the spacing between enamel crystallites.

Authors+Show Affiliations

University of Texas School of Dentistry, Health Science Center at San Antonio, Department of Pediatric Dentistry 78284-7888, USA.No affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.
Review

Language

eng

PubMed ID

7548623

Citation

Simmer, J P., and A G. Fincham. "Molecular Mechanisms of Dental Enamel Formation." Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists, vol. 6, no. 2, 1995, pp. 84-108.
Simmer JP, Fincham AG. Molecular mechanisms of dental enamel formation. Crit Rev Oral Biol Med. 1995;6(2):84-108.
Simmer, J. P., & Fincham, A. G. (1995). Molecular mechanisms of dental enamel formation. Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists, 6(2), 84-108.
Simmer JP, Fincham AG. Molecular Mechanisms of Dental Enamel Formation. Crit Rev Oral Biol Med. 1995;6(2):84-108. PubMed PMID: 7548623.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular mechanisms of dental enamel formation. AU - Simmer,J P, AU - Fincham,A G, PY - 1995/1/1/pubmed PY - 1995/1/1/medline PY - 1995/1/1/entrez SP - 84 EP - 108 JF - Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists JO - Crit. Rev. Oral Biol. Med. VL - 6 IS - 2 N2 - Tooth enamel is a unique mineralized tissue in that it is acellular, is more highly mineralized, and is comprised of individual crystallites that are larger and more oriented than other mineralized tissues. Dental enamel forms by matrix-mediated biomineralization. Enamel crystallites precipitate from a supersaturated solution within a well-delineated biological compartment. Mature enamel crystallites are comprised of non-stoichiometric carbonated calcium hydroxyapatite. The earliest crystallites appear suddenly at the dentino-enamel junction (DEJ) as rapidly growing thin ribbons. The shape and growth patterns of these crystallites can be interpreted as evidence for a precursor phase of octacalcium phosphate (OCP). An OCP crystal displays on its (100) face a surface that may act as a template for hydroxyapatite (OHAp) precipitation. Octacalcium phosphate is less stable than hydroxyapatite and can hydrolyze to OHAp. During this process, one unit cell of octacalcium phosphate is converted into two unit cells of hydroxyapatite. During the precipitation of the mineral phase, the degree of saturation of the enamel fluid is regulated. Proteins in the enamel matrix may buffer calcium and hydrogen ion concentrations as a strategy to preclude the precipitation of competing calcium phosphate solid phases. Tuftelin is an acidic enamel protein that concentrates at the DEJ and may participate in the nucleation of enamel crystals. Other enamel proteins may regulate crystal habit by binding to specific faces of the mineral and inhibiting growth. Structural analyses of recombinant amelogenin are consistent with a functional role in establishing and maintaining the spacing between enamel crystallites. SN - 1045-4411 UR - https://www.unboundmedicine.com/medline/citation/7548623/Molecular_mechanisms_of_dental_enamel_formation_ L2 - https://www.lens.org/lens/search?q=citation_id:7548623 DB - PRIME DP - Unbound Medicine ER -