Mepe-derived asarm peptide impairs dentin mineralization

Bone ◽  
2010 ◽  
Vol 47 ◽  
pp. S235
Author(s):  
B. Salmon ◽  
C. Gaucher ◽  
T. Boukpessi ◽  
T. Léger ◽  
P.S. Rowe ◽  
...  
2013 ◽  
Vol 29 ◽  
pp. e94-e95
Author(s):  
J.D. Padovano ◽  
S. Ravindran ◽  
A. Ramachandran ◽  
A.K. Bedran-Russo ◽  
A. George

Author(s):  
Xueming Zhang ◽  
Preston Beck ◽  
Firoz Rahemtulla ◽  
Huw F. Thomas

2019 ◽  
Vol 103 ◽  
pp. 19-25
Author(s):  
Karina S. Caiaffa ◽  
Fernanda G. Basso ◽  
Norival A. Santos-Filho ◽  
Carlos Alberto de Souza-Costa ◽  
Vivien T. Sakai ◽  
...  

1991 ◽  
Vol 2 (3) ◽  
pp. 369-387 ◽  
Author(s):  
Adele L. Boskey

The extracellular matrix of dentin consists of mineral (hydroxyapatite), collagen, and several noncollagenous matrix proteins. These noncollagenous matrix proteins may be mediators of cell-matrix interactions, matrix maturation, and mineralization. This review describes the current knowledge of the chemistry of mineral crystal formation in dentin with special emphasis on the roles of the dentin matrix proteins. The functions of some of these matrix proteins in the mineralization process have been deduced based on in vitro studies. Functions for others have been postulated based on analogy with some of the bone matrix proteins. Evidence suggests that several of these matrix proteins may have multiple effects on nucleation, crystal growth, and orientation of dentin hydroxyapatite.


Endocrinology ◽  
2007 ◽  
Vol 149 (4) ◽  
pp. 1757-1772 ◽  
Author(s):  
Aline Martin ◽  
Valentin David ◽  
Jennifer S. Laurence ◽  
Patricia M. Schwarz ◽  
Eileen M. Lafer ◽  
...  

Mutations in PHEX (phosphate-regulating gene with homologies to endopeptidases on the X chromosome) and DMP1 (dentin matrix protein 1) result in X-linked hypophosphatemic rickets (HYP) and autosomal-recessive hypophosphatemic-rickets (ARHR), respectively. Specific binding of PHEX to matrix extracellular phosphoglycoprotein (MEPE) regulates the release of small protease-resistant MEPE peptides [acidic serine- and aspartate-rich MEPE-associated motif (ASARM) peptides]. ASARM peptides are potent inhibitors of mineralization (minhibins) that also occur in DMP1 [MEPE-related small integrin-binding ligand, N-linked glycoprotein (SIBLING) protein]. It is not known whether these peptides are directly responsible for the mineralization defect. We therefore used a bone marrow stromal cell (BMSC) coculture model, ASARM peptides, anti-ASARM antibodies, and a small synthetic PHEX peptide (SPR4; 4.2 kDa) to examine this. Surface plasmon resonance (SPR) and two-dimensional 1H/15N nuclear magnetic resonance demonstrated specific binding of SPR4 peptide to ASARM peptide. When cultured individually for 21 d, HYP BMSCs displayed reduced mineralization compared with wild type (WT) (−87%, P < 0.05). When cocultured, both HYP and WT cells failed to mineralize. However, cocultures (HYP and WT) or monocultures of HYP BMSCs treated with SPR4 peptide or anti-ASARM neutralizing antibodies mineralized normally. WT BMSCs treated with ASARM peptide also failed to mineralize properly without SPR4 peptide or anti-ASARM neutralizing antibodies. ASARM peptide treatment decreased PHEX mRNA and protein (−80%, P < 0.05) and SPR4 peptide cotreatment reversed this by binding ASARM peptide. SPR4 peptide also reversed ASARM peptide-mediated changes in expression of key osteoclast and osteoblast differentiation genes. Western blots of HYP calvariae and BMSCs revealed massive degradation of both MEPE and DMP1 protein compared with the WT. We conclude that degradation of MEPE and DMP-1 and release of ASARM peptides are chiefly responsible for the HYP mineralization defect and changes in osteoblast-osteoclast differentiation.


2003 ◽  
Vol 73 (5) ◽  
pp. 470-475 ◽  
Author(s):  
R. Moseley ◽  
R. J. Waddington ◽  
A. J. Sloan ◽  
A. J. Smith ◽  
R. C. Hall ◽  
...  

2013 ◽  
Vol 92 (8) ◽  
pp. 721-727 ◽  
Author(s):  
M.D. McKee ◽  
M.C. Yadav ◽  
B.L. Foster ◽  
M.J. Somerman ◽  
C. Farquharson ◽  
...  

2009 ◽  
Vol 54 (4) ◽  
pp. 299-305 ◽  
Author(s):  
Xueming Zhang ◽  
Firoz Rahemtulla ◽  
Ping Zhang ◽  
Preston Beck ◽  
Huw F. Thomas

1985 ◽  
Vol 33 (6) ◽  
pp. 595-603 ◽  
Author(s):  
D M Lyaruu ◽  
A L Bronckers ◽  
E H Burger ◽  
J H Wöltgens

Potassium pyroantimonate-osmium tetroxide cytochemistry has been used to study the distribution of ionic calcium in hamster tooth germs during cell differentiation and during early dentinogenesis and amelogenesis. Before the onset of mineralization, pyroantimonate (PA) reaction product was found in the nucleus of differentiating preameloblasts and preodontoblasts. In the predentin, it was preferentially located along striated collagen fibrils, lying perpendicular to the basal lamina. At the onset of mineralization, a pronounced increase of PA reaction product was evident in the predentin and on the plasma membrane and in mitochondria of both preodontoblasts and preameloblasts opposite the mineralizing mantle dentin. During early enamel mineralization, PA reaction product was present in the "growing" crystal ends, while in the secretory ameloblasts, most of the PA reaction product was localized on the cytoplasmic side of the apical plasma membranes and in mitochondria. When Tomes' processes developed, PA reaction product, both cytoplasmic and membrane bound, was low or absent deep in the processes, but gradually increased toward the apical terminal web. A corresponding gradient of PA reaction product was observed on the opposing enamel crystallites. From this study we conclude that both preodontoblasts and preameloblasts seem to be involved in calcium acquisition necessary for the early stages of mantle dentin mineralization. Tomes' processes seem to regulate the entry of calcium into the enamel mineralization front.


2008 ◽  
Vol 106 (1) ◽  
pp. 214-222 ◽  
Author(s):  
Eija Salmela ◽  
Carin Sahlberg ◽  
Satu Alaluusua ◽  
Pirjo-Liisa Lukinmaa

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