Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
1.
Chinese Journal of Stomatology ; (12): 435-438, 2010.
Article in Chinese | WPRIM | ID: wpr-243156

ABSTRACT

<p><b>OBJECTIVE</b>To evaluate the clinical short-term results of the acellular dermal matrix for guided bone regeneration.</p><p><b>METHODS</b>Sixty-four patients with bone defect in anterior maxillary area (average bone width: 3 mm) were included. Ridge-splitting technique with simultaneous placement of implants and artificial bone material implantation was performed in 21 patients (non-membrane group). Forty-three patients received the same procedure but with acellular dermal matrix covering the surgical sites (membrane group). The patients were followed up for three months and the new bone formation was checked in clinic and by X-ray.</p><p><b>RESULTS</b>Three months after operation, the membrane group showed good osseointegration and high bone density over the implant cover screws. In the second operation, the membranes became thinner and the new bone fully covered the implant in the membrane group. The labial bone exhibited slight absorption and labial surface of 7 implants in 7 patients was exposed in non-membrane group. The width and the height of the ridge in the second operation were greater in membrane group than in non-membrane group (P < 0.05).</p><p><b>CONCLUSIONS</b>The acellular dermal matrix can effectively resist the growth of soft tissue to allow bone regeneration around the implant.</p>


Subject(s)
Humans , Acellular Dermis , Bone Regeneration , Bone Substitutes , Dental Implants , Guided Tissue Regeneration, Periodontal
2.
West China Journal of Stomatology ; (6): 313-316, 2009.
Article in Chinese | WPRIM | ID: wpr-248242

ABSTRACT

<p><b>OBJECTIVE</b>To study the effects of Simvastatin on the osteoblast activity of human periodontal ligament (PDL) cells.</p><p><b>METHODS</b>The third passage human PDL were cultured in conditional mineralization medium with different concentrations of Simvastatin. The cells were divided into A group (0 mol/L), B group (1 x 10(-9) mol/L), C group (1 x 10(-8) mol/L), D group (1 x 10(-7) mol/L) and E group (1 x 10(-6) mol/L). Alkaline phosphatase (ALP) activity, osteopontin (OPN) and capability of mineralization were measured.</p><p><b>RESULTS</b>Differentiation osteoblast and mineralization of human PDL were improved in all treatment groups with different concentrations of Simvastatin (1 x 10(-9), 1 x 10(-8), 1 x 10(-7), 1 x 10(-6) mol/L). Compared with control group, statistically significant differences were found in 1 x 10(-8) mol/L, 1 x 10(-7) mol/L and 1 x 10(-6) mol/L groups (P<0.05). The maximum effect was observed at the concentration of 1 x 10(-7) mol/L.</p><p><b>CONCLUSION</b>Optimal concentration of Simvastatin can improve the osteoblastic activity of human PDL.</p>


Subject(s)
Humans , Alkaline Phosphatase , Cell Differentiation , Cells, Cultured , Osteoblasts , Osteogenesis , Osteopontin , Periodontal Ligament , Simvastatin
3.
West China Journal of Stomatology ; (6): 27-30, 2008.
Article in Chinese | WPRIM | ID: wpr-296724

ABSTRACT

<p><b>OBJECTIVE</b>To establish the expression and purification route for the gene encoding human amelongenin (AMG) mature peptide in Escherichia coli (E. coli).</p><p><b>METHODS</b>Recombined plasmid pGEX-4T-1/AMG was identified by double endonuclease digestion electrophoretogram and DNA sequence analysis. The recombined plasmid was transformed to E. coli BL21. The inducing time, isopropyl-beta-D-thiogalactopyranoside (IPTG) concentration and inducing temperature were optimized for the express system. Under the optimized condition, the target fusing protein in superatant, periplasm, plasm and inclusion body was analyzed separately. A great amount of target fusing protein was found in the dissoluble protein. AMG fusing protein was purified by the GSTrapFF affinity column.</p><p><b>RESULTS</b>Double endonuclease digestion electrophoretogram and DNA sequence analysis were done to identify the recombined vector pGEX-4T-1/AMG. The results were consistent with the anticipation. The optimum inducing time was 14.5 hours. The optimum IPTG concentration was 1.0 mmol/L. The optimum inducing temperature was 20 degrees C. Under this condition, the target protein was expressed to a maximum. Plentiful target protein was expressed in plasm and inclusion body under the optimized condition. A mount of plasm protein was obtained and purified by the GSTrapFF affinity column. The purified liquid was collected and analyzed by SDS-polyacrylamide gel electrophoresis (SDS-PACE). The protein electrophoresis map showed that AMG fusing protein was purified successfully. After twice elution, high pure fusing protein was obtained.</p><p><b>CONCLUSION</b>pGEX-4T-1/AMG system is used successfully to express human AMG fusing protein.</p>


Subject(s)
Humans , Amelogenin , Escherichia coli , Genetic Vectors
4.
Cancer Research and Clinic ; (6)2006.
Article in Chinese | WPRIM | ID: wpr-676672

ABSTRACT

Objective To study Caveolin-1,EGFR expression in bladder transitional call carcinoma and their prognostic value. Methods Immunohistochemical method was used to detect Caveolin-1,EGFR in 89 cases.of bladder transitional call carcinoma.Results In 89 cases,the percentage of abnormal Caveolin-1 and EGFR expression were 37.1% and 50.6 % respectively.Significant change was observed in different grade case,P

SELECTION OF CITATIONS
SEARCH DETAIL