scholarly journals MicroRNA let-7c-5p Suppressed Lipopolysaccharide-Induced Dental Pulp Inflammation by Inhibiting Dentin Matrix Protein-1-Mediated Nuclear Factor kappa B (NF-κB) Pathway In Vitro and In Vivo

2018 ◽  
Vol 24 ◽  
pp. 6656-6665 ◽  
Author(s):  
Hao Yuan ◽  
Hong Zhang ◽  
Lihua Hong ◽  
Hongyan Zhao ◽  
Jiafeng Wang ◽  
...  
2009 ◽  
Vol 20 (5) ◽  
pp. 365-369 ◽  
Author(s):  
Elizabeth Ferreira Martinez ◽  
Luciana Alves Herdy da Silva ◽  
Cristiane Furuse ◽  
Ney Soares de Araújo ◽  
Vera Cavalcanti de Araújo

Dentin matrix protein 1 (DMP1) is an acidic phosphoprotein that plays an important role in mineralized tissue formation by initiation of nucleation and modulation of mineral phase morphology. The purpose of the present study was to examine the immunoexpression of DMP1 in tooth germs of 7 human fetuses at different gestational ages (14, 16, 19, 20, 21, 23 and 24 weeks) comparing with completed tooth formation erupted teeth. The results showed the presence of DMP1 in the dental lamina, as well as in the cells of the external epithelium, stellate reticulum and stratum intermedium of the enamel organ. However, in the internal dental epithelium, cervical loop region and dental papilla some cells have not labeled for DMP1. In the crown stage, DMP1 was expressed in the ameloblast and odontoblast layer, as well as in the dentinal tubules of coronal dentin near the odontoblast area. Erupted teeth with complete tooth formation exhibited immunolabeling for DMP1 only in the dentinal tubules mainly close to the dental pulp. No staining was observed in the enamel, predentin or dental pulp matrix. DMP1 is present in all developing dental structures (dental lamina, enamel organ, dental papilla) presenting few immunoexpression variations, with no staining in mineralized enamel and dentin.


2012 ◽  
Vol 38 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Ashraf Abd-Elmeguid ◽  
Donald C. Yu ◽  
Loren W. Kline ◽  
Redwan Moqbel ◽  
Harissios Vliagoftis

2004 ◽  
Vol 83 (9) ◽  
pp. 664-670 ◽  
Author(s):  
K.U.E. Ogbureke ◽  
L.W. Fisher

Three members of the SIBLING family of integrin-binding phosphoglycoproteins (bone sialoprotein, BSP; osteopontin, OPN; and dentin matrix protein-1, DMP1) were recently shown to bind with high affinity (nM) and to activate 3 different matrix metalloproteinases (MMP-2, MMP-3, and MMP-9, respectively) in vitro. The current study was designed to document the possible biological relevance of the SIBLING-MMP activation pathway in vivo by showing that these 3 SIBLINGs and their known MMP partners are co-expressed in normal adult tissue. BSP, OPN, and DMP1 were invariably co-expressed with their partner MMPs in salivary glands of humans and mice. The 2 SIBLING proteins without known MMP partners, dentin sialophosphoprotein (DSPP) and matrix extracellular phosphoglycoprotein (MEPE), were also expressed in salivary glands. Expression of all SIBLINGs in this normal, non-mineralizing epithelial tissue suggests that they serve at least one function in vivo other than directly promoting matrix mineralization—a function we hypothesize involves local activation of MMPs.


2011 ◽  
Vol 37 (8) ◽  
pp. 1092-1097 ◽  
Author(s):  
Rajaa Alsanea ◽  
Sriram Ravindran ◽  
Mohamed I. Fayad ◽  
Bradford R. Johnson ◽  
Christopher S. Wenckus ◽  
...  

2003 ◽  
Vol 88 (6) ◽  
pp. 1112-1119 ◽  
Author(s):  
Morimichi Mizuno ◽  
Tetsuro Miyamoto ◽  
Keinoshin Wada ◽  
Sanae Watatani ◽  
Gui Xia Zhang

2003 ◽  
Vol 44 (1) ◽  
pp. 240-245 ◽  
Author(s):  
Gen He ◽  
Thomas Dahl ◽  
Arthur Veis ◽  
Anne George

2003 ◽  
Vol 82 (10) ◽  
pp. 776-780 ◽  
Author(s):  
J.Q. Feng ◽  
H. Huang ◽  
Y. Lu ◽  
L. Ye ◽  
Y. Xie ◽  
...  

Dentin Matrix Protein 1 ( Dmp1) was originally identified from dentin. However, its expression and function in vivo are not clear. To clarify these two issues, we have generated mice carrying a truncated Dmp1 gene by using gene targeting to replace exon 6 with a lacZ gene. Northern blot analysis shows the expected 5.8-kb Dmp1-lacZ fusion transcript and loss of the wild-type 2.8-kb Dmp1 transcript, confirmed by a lack of immunostaining for the protein. Using heterozygous animals, we demonstrate that Dmp1 is specific for mineralized tissues. Not previously shown, Dmp1 is also expressed in pulp cells. Dmp1-deficient embryos and newborns display no apparent gross abnormal phenotype, although there are a modest expansion of the hypertrophic chondrocyte zone and a modest increase in the long bone diameter. This suggests that DMP1 is not essential for early mouse skeletal or dental development.


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