scholarly journals Ablation of Fam20c causes amelogenesis imperfecta via inhibiting Smad dependent BMP signaling pathway

2020 ◽  
Vol 15 (1) ◽  
Author(s):  
Jing Liu ◽  
Wuliji Saiyin ◽  
Xiaohua Xie ◽  
Limin Mao ◽  
Lili Li
Keyword(s):  
Signaling Pathway ◽  
Target Genes ◽  
Kinase Inhibitor ◽  
Bmp Signaling ◽  
Matrix Proteins ◽  
Amelogenesis Imperfecta ◽  
Hereditary Diseases ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
Cyclin Dependent Kinase Inhibitor

Abstract Background Amelogenesis imperfecta (AI) is a type of hereditary diseases that manifest defects in the formation or mineralization of enamel. Recently, it is reported that inactivation of FAM20C, a well-known Golgi casein kinase, caused AI. However, the mechanism of it is still unknown. The aim of this study was to explore the molecular mechanism of AI, which caused by ablation of FAM20C. Results In the Sox2-Cre;Fam20Cfl/fl (cKO) mouse, we found abnormal differentiation of ameloblasts, improper formation and mineralization of enamel, and downregulation of both mRNA and protein level of enamel matrix proteins, including amelogenin (AMEL), ameloblastin (AMBN) and enamelin (ENAM). The levels of BMP2, BMP4 and BMP7, the ligands of BMP signaling pathway, and phosphorylation of Smad1/5/8, the key regulators of BMP signaling pathway, were all decreased in the enamel matrix and the ameloblast of the cKO mice, respectively. The expression of cyclin-dependent kinase inhibitor (P21), muscle segment homeobox genes 2 (Msx2), which are the target genes of the BMP signaling pathway, and laminin 3, the downstream factor of Msx2, were all significantly decreased in the ameloblasts of the cKO mice compared to the control mice. Conclusion the results of our study suggest that ablation of FAM20C leads to AI through inhibiting the Smad dependent BMP signaling pathway in the process of amelogenesis.

Effects of enamel matrix proteins on multi-lineage differentiation of periodontal ligament cells in vitro

2013 ◽  
Vol 9 (1) ◽  
pp. 4796-4805 ◽  
Author(s):  
Harsh D. Amin ◽  
Irwin Olsen ◽  
Jonathan C. Knowles ◽  
Michel Dard ◽  
Nikolaos Donos
Keyword(s):  
Periodontal Ligament ◽  
Matrix Proteins ◽  
Periodontal Ligament Cells ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
Lineage Differentiation

scholarly journals Enamel-like tissue regeneration by using biomimetic enamel matrix proteins

2021 ◽  
Author(s):  
Zehui Fang ◽  
Mengxi Guo ◽  
Qingli Zhou ◽  
Quanli Li ◽  
Hai Ming Wong ◽  
...  
Keyword(s):  
Tissue Regeneration ◽  
Matrix Proteins ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins

Correlation of Apical and Lateral Membrane Modulations of Maturation Ameloblasts

1985 ◽  
Vol 64 (8) ◽  
pp. 1055-1061 ◽  
Author(s):  
Z. Skobe ◽  
F. LaFrazia ◽  
K. Prostak
Keyword(s):  
Apical Membrane ◽  
Apical Cell ◽  
Matrix Proteins ◽  
Maturation Stage ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
Rat Incisor ◽  
Lateral Membrane ◽  
Apical Junctions ◽  
Scanning Electron

Maturation ameloblasts of rat incisor teeth have smooth-ended and ruffle-ended apical membrane configurations. It has also been reported that maturation ameloblasts have several lateral membrane configurations. The purpose of this study was to determine the correlation between the modulations of lateral and apical cell membranes of murine incisor ameloblasts in the maturation stage of amelogenesis. Maxillary and mandibular incisors were dissected, demineralized, embedded in paraffin, sectioned and then de-paraffinized, and the enamel organs were prepared for scanning electron microscopy. Additional mouse and rat incisor enamel organs were fixed and teased apart during dehydration, then observed in the SEM. The lengths of smooth- and ruffle-ended ameloblast segments were measured, and the site, length, and frequency of each lateral membrane configuration were determined within each segment. The lateral membrane configuration with folds forming from 12 to 14 channels around the periphery of the cells was most predominant in both smooth- and ruffle-ended cells. Cells surrounded by from six to eight channels were the only other lateral membrane configuration observed in ruffle-ended ameloblasts. Smooth-ended ameloblasts had lateral membrane configurations with either dense or sparse microvillous projections in addition to both types of channel cells. The observation that channelled extracellular spaces are always associated with ruffle-ended cells suggests that channels somehow function in conjunction with the ruffled apical membrane in resorption and removal of enamel matrix proteins. The smooth-ended ameloblasts lack tight apical junctions, and their microvillous lateral membranes permit the passage of plasma fluids around cells to the maturing enamel surface. Analysis of our data indicates that specific lateral membrane configurations are related to the type of apical membrane present.

scholarly journals Effect of enamel matrix proteins on the treatment of intrabony defects: a split-mouth randomized controlled trial study

2007 ◽  
Vol 21 (3) ◽  
pp. 241-246 ◽  
Author(s):  
Daniela Chambrone ◽  
Ivan Munhoz Pasin ◽  
Marina Clemente Conde ◽  
Claudio Panutti ◽  
Silvia Carneiro ◽  
...  
Keyword(s):  
Randomized Controlled Trial ◽  
Controlled Trial ◽  
Matrix Proteins ◽  
Treatment Modalities ◽  
Enamel Matrix ◽  
Intrabony Defects ◽  
Enamel Matrix Proteins ◽  
Pocket Depth ◽  
Randomized Controlled ◽  
Significant Difference

The objective of this split-mouth, double-blind, randomized controlled trial was to compare the clinical effect of treatment of 2- or 3-wall intrabony defects with open flap debridement (OFD) combined or not with enamel matrix proteins (EMP). Thirteen volunteers were selected with one pair of or more intrabony defects and probing pocket depth (PPD) > 5 mm. All individuals received instructions regarding oral hygiene and were submitted to scaling and root planing. Each participant received the two treatment modalities: test sites were treated with OFD and EMP, and control sites received only OFD. After 6 months, a significant reduction was observed in PPD for the EMP group (from 6.42 ± 1.08 mm to 2.67 ± 1.15 mm) and for the OFD group (from 6.08 ± 1.00 mm to 2.00 ± 0.95 mm) (p < 0.0001), but with no significant difference between groups (p = 0.13). A significant gain in relative attachment level (RAL) was observed in both groups (EMP: from 13.42 ± 1.88 mm to 10.75 ± 2.26 mm, p < 0.001; OFD: from 12.42 ± 1.98 mm to 10.58 ± 2.23 mm, p = 0.013), but with no significant difference between groups (p = 0.85). Gingival recession (GR) was higher in the EMP group (from 1.08 ± 1.50 mm to 2.33 ± 1.43 mm; p = 0.0009) than in the OFD group (from 0.66 ± 1.15 mm to 1.16 ± 1.33 mm; p = 0.16), but this difference was not significant (p = 0.06). In conclusion, the results showed that OFD combined with EMP was not able to improve treatment of intrabony defects compared to OFD alone.

Effect of enamel matrix proteins (Emdogain® ) on healing after re-implantation of “periodontally compromised” roots

2003 ◽  
Vol 30 (10) ◽  
pp. 855-861 ◽  
Author(s):  
M. Araújo ◽  
R. Hayacibara ◽  
M. Sonohara ◽  
G. Cardaropoli ◽  
J. Lindhe
Keyword(s):  
Matrix Proteins ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins

scholarly journals Protein nanoribbons template enamel mineralization

2020 ◽  
Vol 117 (32) ◽  
pp. 19201-19208 ◽  
Author(s):  
Yushi Bai ◽  
Zanlin Yu ◽  
Larry Ackerman ◽  
Yan Zhang ◽  
Johan Bonde ◽  
...  
Keyword(s):  
Supramolecular Assembly ◽  
Organic Content ◽  
Matrix Proteins ◽  
Maturation Stage ◽  
Enamel Matrix ◽  
Structural Protein ◽  
Enamel Matrix Proteins ◽  
Tissue Hardness ◽  
Enamel Mineralization

As the hardest tissue formed by vertebrates, enamel represents nature’s engineering masterpiece with complex organizations of fibrous apatite crystals at the nanometer scale. Supramolecular assemblies of enamel matrix proteins (EMPs) play a key role as the structural scaffolds for regulating mineral morphology during enamel development. However, to achieve maximum tissue hardness, most organic content in enamel is digested and removed at the maturation stage, and thus knowledge of a structural protein template that could guide enamel mineralization is limited at this date. Herein, by examining a gene-modified mouse that lacked enzymatic degradation of EMPs, we demonstrate the presence of protein nanoribbons as the structural scaffolds in developing enamel matrix. Using in vitro mineralization assays we showed that both recombinant and enamel-tissue–based amelogenin nanoribbons are capable of guiding fibrous apatite nanocrystal formation. In accordance with our understanding of the natural process of enamel formation, templated crystal growth was achieved by interaction of amelogenin scaffolds with acidic macromolecules that facilitate the formation of an amorphous calcium phosphate precursor which gradually transforms into oriented apatite fibers along the protein nanoribbons. Furthermore, this study elucidated that matrix metalloproteinase-20 is a critical regulator of the enamel mineralization as only a recombinant analog of a MMP20-cleavage product of amelogenin was capable of guiding apatite mineralization. This study highlights that supramolecular assembly of the scaffold protein, its enzymatic processing, and its ability to interact with acidic carrier proteins are critical steps for proper enamel development.

scholarly journals Effects of enamel matrix proteins on adherence, proliferation and migration of epithelial cells: A real-time in vitro study

2016 ◽  
Vol 13 (1) ◽  
pp. 160-168 ◽  
Author(s):  
Marzena Wyganowska-Swiatkowska ◽  
Paulina Urbaniak ◽  
Daniel Lipinski ◽  
Marlena Szalata ◽  
Karolina Borysiak ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Real Time ◽  
In Vitro Study ◽  
Vitro Study ◽  
Matrix Proteins ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
And Migration ◽  
Proliferation And Migration
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