Expression of amelogenin in odontoblasts

Papagerakis, Pétros; MacDougall, Mary; Hotton, Dominique; Bailleul-Forestier, I.; Oboeuf, M.; Berdal, Ariane

doi:10.1016/s8756-3282(02)00978-x

Cited by 107 publications

(88 citation statements)

References 61 publications

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“…Even though it has been reported that odontoblasts express amelogenin mRNA (Veis et al 2000;Oida et al 2002) and that amelogenin is expressed in relatively small amounts in a temporal-dependent pattern by rodent odontoblasts (Papagerakis et al 2003), the odontoblasts were never labeled in either the control or treated specimens, thus confirming previous studies with the same antibody (Nanci et al 1996;Bosshardt and Nanci 1997;Arana-Chavez and Nanci 2001). At least 14 isoforms are translated by an alternative splicing that takes place during amelogenin processing (Tompkins et al 2005b).…”

Section: The Journal Of Histochemistry and Cytochemistrysupporting

confidence: 70%

Immunocytochemical Study of Amelogenin Deposition during the Early Odontogenesis of Molars in Alendronate-treated Newborn Rats

Massa

Bradaschia-Corrêa

Arana-Chavez

2006

J Histochem Cytochem.

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S U M M A R Y Newborn rats were treated with sodium alendronate to study how enamel is formed and the effect of alendronate during early odontogenesis. Ultrastructural analysis combined with high-resolution immunocytochemistry for amelogenin was carried out. Twelve rats were subjected to daily SC injections of sodium alendronate (2.5 mg/kg/day) for 3 days on their dorsal region, whereas three rats were daily injected with saline solution as a control. Molar tooth germs from 3-day-old rats were fixed under microwave irradiation in 0.1% glutaraldehyde 1 4% formaldehyde buffered at pH 7.2 with 0.1 M sodium cacodylate. The specimens were left undecalcified, postfixed with osmium tetroxide, dehydrated, and embedded in LR White resin. Ultrathin sections were incubated with a chicken anti-24-kDa rat amelogenin antibody, a secondary antibody, and finally with a protein A-gold complex. Large patches of amelogenin were present over the unmineralized mantle dentin and at early secretory ameloblasts. At more advanced stages, they were also detected at the enamel matrix, as well as in the mineralized dentin, at the periodontoblastic space of the dentinal tubules, and at the predentin. It is likely that the main effect of alendronate at early stages of odontogenesis is the increase of synthesis/secretion of amelogenin, promoting its deposition within the forming dentin and enamel. (J Histochem Cytochem 54:713 -725, 2006)

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Section: The Journal Of Histochemistry and Cytochemistrysupporting

confidence: 70%

Immunocytochemical Study of Amelogenin Deposition during the Early Odontogenesis of Molars in Alendronate-treated Newborn Rats

Massa

Bradaschia-Corrêa

Arana-Chavez

2006

J Histochem Cytochem.

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“…Amelogenin message and protein have been detected by various strategies in other tissues, including dental pulp cells [34][35][36][37] , periodontium, bone, brain and other tissues 38,39 . The reader is directed to a recent review for discussion 40 , but major defects have not yet been reported outside of the enamel in either murine models or in humans with AI specific gene mutations.…”

Section: Amelogenin Expression In Other Tissuesmentioning

confidence: 99%

The Amelogenin Proteins and Enamel Development in Humans and Mice

Gibson

2011

Journal of Oral Biosciences

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Before a tooth erupts into the oral cavity, the mineralized enamel and dentin layers begin to develop. During these early stages of enamel formation, an abundant group of proteins known as amelogenins are secreted by ameloblast cells within the developing tooth. These proteins are required for the enamel layer to reach its normal thickness and attain its intricate structure. Human patients with amelogenin gene mutations have a condition referred to as amelogenesis imperfecta, and we have analyzed human gene defects so that we can recreate them in mice. We have generated mice with a null amelogenin mutation where no amelogenin is produced, mice that over-express normal and mutated amelogenins, and over-expressors have been mated to null mice for rescue experiments. Because there are at least 15 messages that are alternatively spliced from a single amelogenin primary RNA transcript, these approaches have begun to reveal the functions of individual amelogenin proteins during enamel development. Finally, amelogenins are processed by carefully regulated proteolytic digestion leading to many additional amelogenin peptides and it is likely that protein function is altered during this developmental process. We have also had some surprises, as one of our mouse models develops odontogenic tumors, and we know now that some of the amelogenins are expressed in other regions of the body outside of the oral cavity, and may have a role in signal transduction.

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“…Specifically, a number of enamel proteins including amelogenin, the major protein of forming enamel, is also expressed by odontoblasts at the onset of dentin formation and found in the mantle dentin (41,42), while the major noncollagenous dentin protein DSPP is transiently expressed by early ameloblasts (43,44). Such unique extracellular matrix composition of mantle dentin and aprismatic enamel at the DEB is likely to be essential for the proper formation and function of this interface.…”

mentioning

confidence: 99%

Amelogenin-Collagen Interactions Regulate Calcium Phosphate Mineralization in Vitro

Deshpande

Fang

Simmer

et al. 2010

Journal of Biological Chemistry

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Collagen and amelogenin are two major extracellular organic matrix proteins of dentin and enamel, the mineralized tissues comprising a tooth crown. They both are present at the dentinenamel boundary (DEB), a remarkably robust interface holding dentin and enamel together. It is believed that interactions of dentin and enamel protein assemblies regulate growth and structural organization of mineral crystals at the DEB, leading to a continuum at the molecular level between dentin and enamel organic and mineral phases. To gain insight into the mechanisms of the DEB formation and structural basis of its mechanical resiliency we have studied the interactions between collagen fibrils, amelogenin assemblies, and forming mineral in vitro, using electron microscopy. Our data indicate that collagen fibrils guide assembly of amelogenin into elongated chain or filament-like structures oriented along the long axes of the fibrils. We also show that the interactions between collagen fibrils and amelogenin-calcium phosphate mineral complexes lead to oriented deposition of elongated amorphous mineral particles along the fibril axes, triggering mineralization of the bulk of collagen fibril. The resulting structure was similar to the mineralized collagen fibrils found at the DEB, with arrays of smaller well organized crystals inside the collagen fibrils and bundles of larger crystals on the outside of the fibrils. These data suggest that interactions between collagen and amelogenin might play an important role in the formation of the DEB providing structural continuity between dentin and enamel.Dentin and enamel, the two mineralized tissues that comprise a tooth crown, are strikingly different in terms of their compositional, structural, and mechanical properties (1). Despite these differences, dentin and enamel work together for decades under severe mechanical stress, without delamination or catastrophic failure.Dentin is a mineralized tissue similar to bone, comprised primarily of fibrillar collagen type I, carbonated apatite and water (2). There are other so-called noncollagenous macromolecules present that, in total, represent less then 10% by mass of organic material, although they play important roles in the formation and function of these tissues. All bone materials share the same basic building block, a collagen fibril, in which plateshaped apatitic crystals are organized in parallel arrays with their c-axes co-aligned with the long axis of the fibril (2-4). Collagen type I triple helical molecules, are super-coiled assemblies of two identical ␣1-chains and one ␣2-chain with a different sequence (5, 6). Each chain contains more than 1000 amino acids and is primarily composed of Gly-X-Y repeats, where amino acids proline (Pro) and hydroxyproline (Hyp) predominantly occupy X and Y positions. All three chains in the molecule adopt a polyproline II (PPII)-like structure, which is stabilized by direct and water mediated inter-and intra-chain hydrogen bonds (5, 6). Collagen fibrils form via a self-assembly process in which collag...

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Expression of amelogenin in odontoblasts

Cited by 107 publications

References 61 publications

Immunocytochemical Study of Amelogenin Deposition during the Early Odontogenesis of Molars in Alendronate-treated Newborn Rats

Immunocytochemical Study of Amelogenin Deposition during the Early Odontogenesis of Molars in Alendronate-treated Newborn Rats

The Amelogenin Proteins and Enamel Development in Humans and Mice

Amelogenin-Collagen Interactions Regulate Calcium Phosphate Mineralization in Vitro

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