Disruption of periodontal integrity induces expression of apin by epithelial cell rests of Malassez

Nishio, Clarice; Wazen, Rima; Kuroda, Shingo; Moffatt, Pierre; Nanci, Antonio

doi:10.1111/j.1600-0765.2010.01288.x

Cited by 29 publications

(32 citation statements)

References 30 publications

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“…With respect to cellular functions of ODAM, those indicated in ameloblasts are varied, and include an extracellular role at the cell-tooth interface in the junctional epithelium, roles in enamel maturation, and in the response to peridontal disruption [31,32]. ODAM is secreted [13,33] yet may also have a role in the cell nucleus regulating matrix metalloproteinase expression via direct chromatin binding [34].…”

Section: Discussionmentioning

confidence: 99%

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

et al. 2013

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BackgroundThe Odontogenic Ameloblast-associated Protein (ODAM) is expressed in a wide range of normal epithelial, and neoplastic tissues, and we have posited that ODAM serves as a novel prognostic biomarker for breast cancer and melanoma. Transfection of ODAM into breast cancer cells yields suppression of cellular growth, motility, and in vivo tumorigenicity. Herein we have extended these studies to the effects of ODAM on cultured melanoma cell lines.MethodsThe A375 and C8161 melanoma cell lines were stably transfected with ODAM and assayed for properties associated with tumorigenicity including cell growth, motility, and extracellular matrix adhesion. In addition, ODAM–transfected cells were assayed for signal transduction via AKT which promotes cell proliferation and survival in many neoplasms.ResultsODAM expression in A375 and C8161 cells strongly inhibited cell growth and motility in vitro, increased cell adhesion to extracellular matrix, and yielded significant cytoskeletal/morphologic rearrangement. Furthermore, AKT activity was downregulated by ODAM expression while an increase was noted in expression of the PTEN (phosphatase and tensin homolog on chromosome 10) tumor suppressor gene, an antagonist of AKT activation. Increased PTEN in ODAM-expressing cells was associated with increases in PTEN mRNA levels and de novo protein synthesis. Silencing of PTEN expression yielded recovery of AKT activity in ODAM-expressing melanoma cells. Similar PTEN elevation and inhibition of AKT by ODAM was observed in MDA-MB-231 breast cancer cells while ODAM expression had no effect in PTEN-deficient BT-549 breast cancer cells.ConclusionsThe apparent anti-neoplastic effects of ODAM in cultured melanoma and breast cancer cells are associated with increased PTEN expression, and suppression of AKT activity. This association should serve to clarify the clinical import of ODAM expression and any role it may serve as an indicator of tumor behavior.

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Section: Discussionmentioning

confidence: 99%

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

et al. 2013

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“…), or by Epithelial Rests of Malassez either under normal conditions or following a periodontal challenge (Nishio et al. ). No amelogenin expressed sequence tags (EST) were identified among the 3.32 million ESTs reported for normal human tissues (Hs.654436), which did not sample developing teeth.…”

Section: Introductionmentioning

confidence: 99%

Enamel ribbons, surface nodules, and octacalcium phosphate in C57BL/6Amelx^−/−mice andAmelx^+/−lyonization

Smith

Cai

et al. 2016

Mol Genet Genomic Med

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BackgroundAmelogenin is required for normal enamel formation and is the most abundant protein in developing enamel.Methods Amelx +/+, Amelx +/−, and Amelx −/− molars and incisors from C57BL/6 mice were characterized using RT‐PCR, Western blotting, dissecting and light microscopy, immunohistochemistry (IHC), transmission electron microscopy (TEM), scanning electron microscopy (SEM), backscattered SEM (bSEM), nanohardness testing, and X‐ray diffraction.ResultsNo amelogenin protein was detected by Western blot analyses of enamel extracts from Amelx −/− mice. Amelx −/− incisor enamel averaged 20.3 ± 3.3 μm in thickness, or only 1/6th that of the wild type (122.3 ± 7.9 μm). Amelx −/− incisor enamel nanohardness was 1.6 Gpa, less than half that of wild‐type enamel (3.6 Gpa). Amelx +/− incisors and molars showed vertical banding patterns unique to each tooth. IHC detected no amelogenin in Amelx −/− enamel and varied levels of amelogenin in Amelx +/− incisors, which correlated positively with enamel thickness, strongly supporting lyonization as the cause of the variations in enamel thickness. TEM analyses showed characteristic mineral ribbons in Amelx +/+ and Amelx −/− enamel extending from mineralized dentin collagen to the ameloblast. The Amelx −/− enamel ribbons were not well separated by matrix and appeared to fuse together, forming plates. X‐ray diffraction determined that the predominant mineral in Amelx −/− enamel is octacalcium phosphate (not calcium hydroxyapatite). Amelx −/− ameloblasts were similar to wild‐type ameloblasts except no Tomes’ processes extended into the thin enamel. Amelx −/− and Amelx +/− molars both showed calcified nodules on their occlusal surfaces. Histology of D5 and D11 developing molars showed nodules forming during the maturation stage.ConclusionAmelogenin forms a resorbable matrix that separates and supports, but does not shape early secretory‐stage enamel ribbons. Amelogenin may facilitate the conversion of enamel ribbons into hydroxyapatite by inhibiting the formation of octacalcium phosphate. Amelogenin is necessary for thickening the enamel layer, which helps maintain ribbon organization and development and maintenance of the Tomes’ process.

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“…In this context it is interesting to note that the presence of AMTN during formation of the primary JE has only been detected by immunohistochemistry, but not by in situ hybridization, which either indicates insufficient sensitivity of the technique to detect low abundance Amtn mRNA transcripts, or that the AMTN protein found in the JE is residual from production by the reduced enamel epithelium (Sawada et al, 2013). Regardless, both AMTN and ODAM are re-expressed in the JE after gingivectomy and regain their normal expression pattern after the gingival tissue has regenerated (Nishio et al, 2010a). Notably, ODAM expression is induced in epithelial rests of Malassez (ERM) after experimental periodontal detachment and ODAM is re-expressed during orthodontic tooth movement (Nishio et al, 2010b; Jue et al, 2013), indicating that ODAM may play a role in periodontal regeneration.…”

Section: Roles In the Junctional Epitheliummentioning

confidence: 99%

“…Regardless, both AMTN and ODAM are re-expressed in the JE after gingivectomy and regain their normal expression pattern after the gingival tissue has regenerated (Nishio et al, 2010a). Notably, ODAM expression is induced in epithelial rests of Malassez (ERM) after experimental periodontal detachment and ODAM is re-expressed during orthodontic tooth movement (Nishio et al, 2010b; Jue et al, 2013), indicating that ODAM may play a role in periodontal regeneration. However, the work to date is largely descriptive and functional studies have not been published.…”

Section: Roles In the Junctional Epitheliummentioning

confidence: 99%

Maturation and beyond: proteins in the developmental continuum from enamel epithelium to junctional epithelium

Ganß

Abbarin

2014

Front. Physiol.

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Enamel, covering the surface of teeth, is the hardest substance in mammals. It is designed to last a lifetime in spite of severe environmental challenges. Enamel is formed in a biomineralization process that is essentially divided into secretory and maturation stages. While the molecular events of enamel formation during the secretory stage have been elucidated to some extent, the mechanisms of enamel maturation are less defined, and little is known about the molecules present beyond the maturation stage. Several genes, all located within the secreted calcium-binding phosphoprotein (SCPP) gene cluster, were recently shown to be expressed during the developmental continuum from maturation stage ameloblasts to junctional epithelium (JE). This review introduces four such genes and their protein products, and presents our current state of knowledge on their roles, primarily in enamel formation and JE biology. The discovery of these proteins, and a more detailed analysis of their biological functions, will likely contribute to a more thorough understanding of the molecular mechanisms of enamel maturation and dentogingival attachment.

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Disruption of periodontal integrity induces expression of apin by epithelial cell rests of Malassez

Abstract: The expression of APIN at an early time-point following disruption of periodontal integrity suggests that this protein may be part of the cascade of events leading to the activation of ERM during periodontal healing and regeneration.

Cited by 29 publications

References 30 publications

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

Enamel ribbons, surface nodules, and octacalcium phosphate in C57BL/6Amelx^−/−mice andAmelx^+/−lyonization

Maturation and beyond: proteins in the developmental continuum from enamel epithelium to junctional epithelium

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Disruption of periodontal integrity induces expression of apin by epithelial cell rests of Malassez

Abstract: The expression of APIN at an early time-point following disruption of periodontal integrity suggests that this protein may be part of the cascade of events leading to the activation of ERM during periodontal healing and regeneration.

Cited by 29 publications

References 30 publications

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

Odontogenic ameloblast-associated protein (ODAM) inhibits growth and migration of human melanoma cells and elicits PTEN elevation and inactivation of PI3K/AKT signaling

Enamel ribbons, surface nodules, and octacalcium phosphate in C57BL/6Amelx−/−mice andAmelx+/−lyonization

Maturation and beyond: proteins in the developmental continuum from enamel epithelium to junctional epithelium

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Enamel ribbons, surface nodules, and octacalcium phosphate in C57BL/6Amelx^−/−mice andAmelx^+/−lyonization