Amino acid composition, distribution and origin of “tuft” protein in human and bovine dental enamel

Robinson, C.; Lowe, Norman R.; Weatherell, J.A.

doi:10.1016/0003-9969(75)90149-1

Cited by 110 publications

(61 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results were confirmed later using chromatographic, electrophoretic, and amino acid analyses (35). On the other hand, major differences between protein contents of primary bovine and human enamel were found in another study (36). Jameson et al (37) showed that the magnitude of water loss was significantly greater for bovine than for human dentin.…”

Section: Chemical Composition Studiesmentioning

confidence: 84%

“…Therefore, 68 papers were included in the final review. The studies covered seven main categories: morphology (5 studies) (22)(23)(24)(25)(26), chemical composition (11 studies) (27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37), physical properties (12 studies) (38)(39)(40)(41)(42)(43)(44)(45)(46)(47)(48)(49), dental caries (7 studies) (6,9,(50)(51)(52)(53)(54), dental erosion/abrasion (10 studies) (55)(56)(57)(58)(59)(60)(61)(62)(63)(64), bonding/adhesive strength (17 studies) (65)(66)(67)(68)…”

Section: Search Resultsmentioning

confidence: 99%

“…Eleven studies were reviewed (27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37). Bisaz et al (27) showed detectable amounts of inorganic pyrophosphate in enamel and dentin of both human and bovine teeth.…”

Section: Chemical Composition Studiesmentioning

confidence: 99%

See 2 more Smart Citations

Bovine teeth as substitute for human teeth in dental research: a review of literature

2011

View full text Add to dashboard Cite

The aim of this paper was to review in vitro and in situ studies that directly compared the use of bovine teeth as a substitute for human teeth in dental experiments. A PubMed search was conducted for papers published from 1953 to December 30, 2010 using the following keywords: "human bovine enamel" or "human bovine dentin" or "human bovine teeth". The abstracts of the studies resulting from the keyword search were read, and all papers that compared human and bovine teeth were fully read. Only original articles written in English and directly comparing human and bovine substrates were included in the review. The search was supplemented by manual searches of the reference lists from each identified paper. Out of 76 studies initially selected, 68 fulfilled the selection criteria for inclusion. The studies covered seven categories: dental morphology, chemical composition, physical properties, dental caries, dental erosion/abrasion, bonding/adhesive strength, and marginal microleakage. Inconsistent data exist regarding whether bovine teeth can be considered an appropriate substitute for human teeth in dental research. Morphological, chemical composition and physical property differences between the two substrates must be considered when interpreting results obtained from any experiment using bovine tooth substrate. (J Oral Sci 53, 273-282, 2011)

show abstract

Section: Chemical Composition Studiesmentioning

confidence: 84%

Section: Search Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Bovine teeth as substitute for human teeth in dental research: a review of literature

2011

View full text Add to dashboard Cite

show abstract

“…Of these, "tuft proteins" are found at the dentino-enamel junction (Robinson et al 1975), whereas sheathlin is believed to accumulate in the so-called "prism sheath" (Uchida et al 1995;Hu et al 1997a). Patches of electron-dense organic matrix are clearly visible near the dentino-enamel junction from midmaturation and beyond.…”

Section: Figure 16mentioning

confidence: 99%

“…However, as maturation proceeds and massive protein degradation takes place, the spaces become filled with electron-dense material (see Figure 16). Although these accumulations of matrix are situated at the dentinoenamel junction like "tuft protein" (Robinson et al 1975;Robinson et al 1989), they do not contain a single and distinct protein but consist essentially of a mixture of proteins, comprising at least intact amelogenin and/or its fragments and portions of ameloblastin.…”

Section: Figure 16mentioning

confidence: 99%

Comparative Immunochemical Analyses of the Developmental Expression and Distribution of Ameloblastin and Amelogenin in Rat Incisors

Nanci

Zalzal

Lavoie

et al. 1998

J Histochem Cytochem.

127

155

View full text Add to dashboard Cite

SUMMARYMineralized tissues are unique in using proteins to attract and organize calcium and phosphate ions into a structured mineral phase. A precise knowledge of the expression and extracellular distribution of matrix proteins is therefore very important in understanding their function. The purpose of this investigation was to obtain comparative information on the expression, intracellular and extracellular distribution, and dynamics of proteins representative of the two main classes of enamel matrix proteins. Amelogenins were visualized using an antibody and an mRNA probe prepared against the major alternatively spliced isoform in rodents, and nonamelogenins by antibodies and mRNA probes specific to one enamel protein referred to by three names: ameloblastin, amelin, and sheathlin. Qualitative and quantitative immunocytochemistry, in combination with immunoblotting and in situ hybridization, indicated a correlation between mRNA signal and sites of protein secretion for amelogenin, but not for ameloblastin, during the early presecretory and midto late maturation stages, during which mRNA signals were detected but no proteins appeared to be secreted. Extracellular amelogenin immunoreactivity was generally weak near secretory surfaces, increasing over a distance of about 1.25 m to reach a level slightly above an amount expected if the protein were being deposited evenly across the enamel layer. Immunolabeling for ameloblastin showed an inverse pattern, with relatively more gold particles near secretory surfaces and much fewer deeper into the enamel layer. Administration of brefeldin A and cycloheximide to stop protein secretion revealed that the immunoblotting pattern of amelogenin was relatively stable, whereas ameloblastin broke down rapidly into lower molecular weight fragments. The distance from the cell surface at which immunolabeling for amelogenin stabilized generally corresponded to the point at which that for ameloblastin started to show a net reduction. These data suggest a correlation between the distribution of amelogenin and ameloblastin and that intact ameloblastin has a transient role in promoting/stabilizing crystal elongation. A meloblasts , like all hard tissue-forming cells, release an intricate set of extracellular matrix proteins optimized for promoting the development of a closely associated mineral phase (reviewed in Deutsch et al.

show abstract

Enamel Maturation

Robinson¹,

Brookes²,

Bonass³

et al. 2007

Novartis Foundation Symposia

View full text Add to dashboard Cite

Amino acid composition, distribution and origin of “tuft” protein in human and bovine dental enamel

Cited by 110 publications

References 9 publications

Bovine teeth as substitute for human teeth in dental research: a review of literature

Bovine teeth as substitute for human teeth in dental research: a review of literature

Comparative Immunochemical Analyses of the Developmental Expression and Distribution of Ameloblastin and Amelogenin in Rat Incisors

Enamel Maturation

Contact Info

Product

Resources

About