Relative Levels of mRNA Encoding Enamel Proteins in Enamel Organ Epithelia and Odontoblasts

Nagano, Takatoshi; Oida, Shinichiro; Ando, Hironori; Gomi, Kazuhiro; Arai, Takashi; Fukae, Makoto

doi:10.1177/154405910308201209

Cited by 69 publications

(60 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Amelogenin expression was identified in secretory ameloblasts and stratum intermedium cells at the apical bud of the incisor (21,22). Both maturation stage ameloblasts and stratum intermedium cells associated with maturation and secretion stage ameloblasts are amelogenin-negative (20).…”

Section: Discussionmentioning

confidence: 93%

Sodium-Calcium Exchangers in Rat Ameloblasts

et al. 2010

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 93%

Sodium-Calcium Exchangers in Rat Ameloblasts

et al. 2010

View full text Add to dashboard Cite

show abstract

“…As molecular probing techniques have become more sensitive, these gene expression pattern profiles are being challenged and/or corrected. In mice, the mRNAs of amelogenin, ameloblastin, and enamelin, in addition to being a product of ameloblast cells, are also apparent in presecretory and secretory odontoblasts (18,(43)(44)(45)(46). The mRNA and protein expression of dentin-matrix protein 1 and Dspp, in addition to odontoblasts, are also apparent in presecretory ameloblasts (14,16,17,47,48).…”

Section: Discussionmentioning

confidence: 99%

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

Paine

Luo

Wang

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

The gene for dentin sialophosphoprotein produces a single protein that is post-translationally modified to generate two distinct extracellular proteins: dentin sialoprotein and dentin phosphoprotein. In teeth, dentin sialophosphoprotein is expressed primarily by odontoblast cells, but is also transiently expressed by presecretory ameloblasts. Because of this expression profile it appears that dentin sialophosphoprotein contributes to the early events of amelogenesis, and in particular to those events that result in the formation of the dentinoenamel junction and the adjacent "aprismatic" enamel. Using a transgenic animal approach we have extended dentin sialoprotein or dentin phosphoprotein expression throughout the developmental stages of amelogenesis. Overexpression of dentin sialoprotein results in an increased rate of enamel mineralization, however, the enamel morphology is not significantly altered. In wildtype animals, the inclusion of dentin sialoprotein in the forming aprismatic enamel may account for its increased hardness properties, when compared with bulk enamel. In contrast, the overexpression of dentin phosphoprotein creates "pitted" and "chalky" enamel of nonuniform thickness that is more prone to wear. Disruptions to the prismatic enamel structure are also a characteristic of the dentin phosphoprotein overexpressing animals. These data support the previous suggestion that dentin sialoprotein and dentin phosphoprotein have distinct functions related to tooth formation, and that the dentino-enamel junction should be viewed as a unique transition zone between enamel and the underlying dentin. These results support the notion that the dentin proteins expressed by presecretory ameloblasts contribute to the unique properties of the dentino-enamel junction.Dentin is an ectomesenchymal derived, collagen containing, calcified tissue that forms the major part of the tooth. Genetic diseases that result in abnormal dentin are classified in a subgrouping of dentinogenesis imperfecta. Dentinogenesis imperfecta type I (DI-I) 1 is always associated with one of the osteogenesis imperfectas, where mutations have been characterized in the following collagens: COL1A1, COL1A2, COL5A1, and COL2A1 (1), whereas dentinogenesis imperfecta type II (DI-II) is a disorder in dentin mineralization. Dentinogenesis imperfecta type III (DI-III) has a more extreme abnormal dental phenotype that impacts beyond dentin to the enamel and the pulps of affected teeth (2, 3).In dentin, two of the noncollagenous dentin matrix proteins are dentin siaolprotein (DSP) and dentin phosphoprotein (DPP). Both DSP and DPP are products of a single gene called dentin sialophosphoprotein (DSPP). Following transcription and translation of DSPP, the resulting product is post-translational cleaved to produce DSP and DPP that are primarily expressed in the dentin matrix (4). DPP (also known as phosphophoryn) is a highly acidic protein and is the major noncollagenous matrix component of dentin (ϳ90% of the dentin matrix is collagen) (5, 6). DSP is a glyco...

show abstract

“…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

View full text Add to dashboard Cite

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.

show abstract

Relative Levels of mRNA Encoding Enamel Proteins in Enamel Organ Epithelia and Odontoblasts

Cited by 69 publications

References 20 publications

Sodium-Calcium Exchangers in Rat Ameloblasts

Sodium-Calcium Exchangers in Rat Ameloblasts

Dentin Sialoprotein and Dentin Phosphoprotein Overexpression during Amelogenesis

The Amelogenin Proteins and Enamel Development in Humans and Mice

Contact Info

Product

Resources

About