Calcium phosphate precipitation in experimental gaps between fluoride-containing fast-setting calcium silicate cement and dentin

2018 ◽  
Vol 126 (2) ◽  
pp. 118-125 ◽  
Author(s):  
Bahram Ranjkesh ◽  
Ming Ding ◽  
Michel Dalstra ◽  
Jens R. Nyengaard ◽  
Jacques Chevallier ◽  
...  
2006 ◽  
Vol 309-311 ◽  
pp. 829-832 ◽  
Author(s):  
Hakan Engqvist ◽  
S. Edlund ◽  
Gunilla Gómez-Ortega ◽  
Jesper Lööf ◽  
Leif Hermansson

The objective of the paper is to investigate the mechanical and the handling properties of a novel injectable bone void filler based on calcium silicate. The orthopaedic cement based on calcium silicate was compared to a calcium phosphate cement, Norian SRS from Syntes Stratec, with regard to the working (ejection through 14 G needle) and setting time (Gillmore needles), Young’s modulus and the flexural (ASTM F-394) and compressive (ISO 9917) strength after storage in phosphate buffer saline at body temperature for time points from 1h up to 16 weeks. The calcium silicate cement is composed of a calcium silicate powder (grain size below 20 µm) that is mixed with a liquid (water and CaCl2) into a paste using a spatula and a mixing cup. The water to cement ratio used was about 0.5. The calcium silicate had a working time of 15 minutes and a setting time of 17 minutes compared to 5 and 10 minutes respectively for the calcium phosphate cement. The compressive strength was considerably higher for the calcium silicate cement (>100 MPa) compared to the calcium phosphate cement (>40 MPa). Regarding the flexural strength the calcium silicate cement had high values for up to 1 week (> 40 MPa) but it decreased to 25 MPa after 16 weeks. The phosphate cement had a constant flexural strength of about 25 MPa. The results show that calcium silicate cement has the mechanical and handling potential to be used as high strength bone void filler.


2015 ◽  
Vol 3 (4) ◽  
pp. 570-580 ◽  
Author(s):  
Shu-Ching Huang ◽  
Buor-Chang Wu ◽  
Shinn-Jyh Ding

The calcium silicate cement (CSC) on osteogenic differentiation of hMSCs and bacteriostatic abilities was more effective than calcium phosphate cement (CPC).


Author(s):  
Mariano S. Pedano ◽  
Kumiko Yoshihara ◽  
Xin Li ◽  
Bernardo Camargo ◽  
Kirsten Van Landuyt ◽  
...  

2017 ◽  
Vol 116 (9) ◽  
pp. 679-688 ◽  
Author(s):  
Yuan-Chien Chen ◽  
Ming-You Shie ◽  
Yuan-Haw Andrew Wu ◽  
Kai-Xing Alvin Lee ◽  
Li-Ju Wei ◽  
...  

protocols.io ◽  
2018 ◽  
Author(s):  
Helena Parra ◽  
N ria ◽  
Alberto Perez ◽  
Aleksandra Kozyczkowska ◽  
Sebasti n

1987 ◽  
Vol 66 (2) ◽  
pp. 462-466 ◽  
Author(s):  
F.G. Oppenheim ◽  
D.I. Hay ◽  
D.J. Smith ◽  
G.D. Offner ◽  
R.F. Troxler

Acidic proline-rich phosphoproteins and phosphopeptides are abundant components of parotid and submandibular salivary secretions in man and in the subhuman primate, Macaca fascicularis. The major acidic proline-rich proteins and the proline-rich phosphopeptide, statherin, of man and macaques have been shown to be potent inhibitors of calcium phosphate precipitation and are thought to function in the oral environment by maintaining saliva supersaturated with respect to calcium phosphate salts. Little is known about the biosynthesis of these proline-rich phosphoproteins and peptides, and the aim of the present work was to determine the structural relationship between statherin precursors and native human and macaque statherin. RNA was isolated from human submandibular gland, and poly(A+) mRNA was selected by affinity chromatography on oligo(dT) cellulose and translated in a reticulocyte lysate. Electrophoretic analysis of the translation products revealed that this mRNA directed the synthesis of a large number of polypeptides with M,s ranging from 5000 to 70,000. Immunoprecipitates, prepared with an antiserum directed against human statherin, contained a single component with a Mr of 7800, approximately 2000 daltons larger than native statherin. Radiosequencing of the in vitro precursor of statherin in immunoprecipitates demonstrated the presence of a 19-residue signal peptide. These results suggest that statherin is derived from a unique structural gene, and does not result from proteolytic processing of a large polyprotein precursor.


Biomatter ◽  
2011 ◽  
Vol 1 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Cecilia Persson ◽  
Håkan Engqvist

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