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1.
J Periodontal Res ; 49(2): 164-78, 2014 Apr.
Article in English | MEDLINE | ID: mdl-23710575

ABSTRACT

BACKGROUND AND OBJECTIVE: Periodontal disease is a common infectious disease, found worldwide, causing the destruction of the periodontium. The periodontium is a complex structure composed of both soft and hard tissues, thus an agent applied to regenerate the periodontium must be able to stimulate periodontal ligament, cementum and alveolar bone regeneration. Recent studies demonstrated that acemannan, a polysaccharide extracted from Aloe vera gel, stimulated both soft and hard tissue healing. This study investigated effect of acemannan as a bioactive molecule and scaffold for periodontal tissue regeneration. MATERIAL AND METHODS: Primary human periodontal ligament cells were treated with acemannan in vitro. New DNA synthesis, expression of growth/differentiation factor 5 and runt-related transcription factor 2, expression of vascular endothelial growth factor, bone morphogenetic protein-2 and type I collagen, alkaline phosphatase activity, and mineralized nodule formation were determined using [(3)H]-thymidine incorporation, reverse transcription-polymerase chain reaction, enzyme-linked immunoabsorbent assay, biochemical assay and alizarin red staining, respectively. In our in vivo study, premolar class II furcation defects were made in four mongrel dogs. Acemannan sponges were applied into the defects. Untreated defects were used as a negative control group. The amount of new bone, cementum and periodontal ligament formation were evaluated 30 and 60 d after the operation. RESULTS: Acemannan significantly increased periodontal ligament cell proliferation, upregulation of growth/differentiation factor 5, runt-related transcription factor 2, vascular endothelial growth factor, bone morphogenetic protein 2, type I collagen and alkaline phosphatase activity, and mineral deposition as compared with the untreated control group in vitro. Moreover, acemannan significantly accelerated new alveolar bone, cementum and periodontal ligament formation in class II furcation defects. CONCLUSION: Our data suggest that acemannan could be a candidate biomolecule for periodontal tissue regeneration.


Subject(s)
Alveolar Process/drug effects , Dental Cementum/drug effects , Furcation Defects/drug therapy , Mannans/therapeutic use , Periodontal Ligament/drug effects , Phytotherapy/methods , Plant Extracts/therapeutic use , Alkaline Phosphatase/analysis , Animals , Bone Morphogenetic Protein 2/analysis , Bone Regeneration/drug effects , Calcification, Physiologic/drug effects , Cell Culture Techniques , Cell Proliferation/drug effects , Cells, Cultured , Cementogenesis/drug effects , Collagen Type I/analysis , Core Binding Factor Alpha 1 Subunit/analysis , DNA/drug effects , Disease Models, Animal , Dogs , Gels , Growth Differentiation Factor 5/analysis , Humans , Osteogenesis/drug effects , Periodontal Ligament/cytology , Regeneration/drug effects , Vascular Endothelial Growth Factor A/analysis
2.
BMC Cell Biol ; 11: 20, 2010 Mar 15.
Article in English | MEDLINE | ID: mdl-20230640

ABSTRACT

BACKGROUND: Bone morphogenetic proteins (BMPs) contribute to many different aspects of development including mesoderm formation, heart development, neurogenesis, skeletal development, and axis formation. They have previously been recognized only as secreted growth factors, but the present study detected Bmp2, Bmp4, and Gdf5/CDMP1 in the nuclei of cultured cells using immunocytochemistry and immunoblotting of nuclear extracts. RESULTS: In all three proteins, a bipartite nuclear localization signal (NLS) was found to overlap the site at which the proproteins are cleaved to release the mature growth factors from the propeptides. Mutational analyses indicated that the nuclear variants of these three proteins are produced by initiating translation from downstream alternative start codons. The resulting proteins lack N-terminal signal peptides and are therefore translated in the cytoplasm rather than the endoplasmic reticulum, thus avoiding proteolytic processing in the secretory pathway. Instead, the uncleaved proteins (designated nBmp2, nBmp4, and nGdf5) containing the intact NLSs are translocated to the nucleus. Immunostaining of endogenous nBmp2 in cultured cells demonstrated that the amount of nBmp2 as well as its nuclear/cytoplasmic distribution differs between cells that are in M-phase versus other phases of the cell cycle. CONCLUSIONS: The observation that nBmp2 localization varies throughout the cell cycle, as well as the conservation of a nuclear localization mechanism among three different BMP family members, suggests that these novel nuclear variants of BMP family proteins play an important functional role in the cell.


Subject(s)
Bone Morphogenetic Protein 2/metabolism , Bone Morphogenetic Protein 4/metabolism , Cell Nucleus/metabolism , Amino Acid Sequence , Animals , Bone Morphogenetic Protein 2/analysis , Bone Morphogenetic Protein 2/genetics , Bone Morphogenetic Protein 4/analysis , Bone Morphogenetic Protein 4/genetics , Cell Division , Cell Line , Codon, Initiator , Growth Differentiation Factor 5/analysis , Growth Differentiation Factor 5/metabolism , Mice , Molecular Sequence Data , Signal Transduction
3.
J Periodontal Res ; 44(4): 425-33, 2009 Aug.
Article in English | MEDLINE | ID: mdl-18973549

ABSTRACT

BACKGROUND AND OBJECTIVE: Although periodontal ligament-derived cells are expected to be a useful source of cells for periodontal tissue engineering, the characteristic changes of primary cultured cells have not been well studied. Therefore, the aim of this study was to investigate the characteristics of periodontal ligament-derived cells and their changes during passage. MATERIAL AND METHODS: Human periodontal ligament tissue was obtained from extracted third molars. Cells were subcultured until passage 6 and the cell characteristics from early to late passages were evaluated using immunofluorescence microscopy, alkaline phosphatase activity analyses, reverse transcription-polymerase chain reaction and quantitative real-time polymerase chain reaction. To examine the function of periodontal ligament-derived cells further, cells were transplanted into the renal subcapsule of an immunocompromised rat. RESULTS: Immunofluorescence results showed relatively uniform expression of MSX-2 and osteonectin from passage 1 until passage 6. The STRO-1-positive fraction was 33.5% at passage 0, which was reduced to 14.7% at passage 3. Cultured cells at passage 1 expressed mRNA for collagen type I, collagen type XII, Runx2, alkaline phosphatase, osteonectin, osteopontin, scleraxis, tenomodulin, Msx2, GDF5 and GDF7 genes, but not for bone sialoprotein. The level of mRNA expression from tenomodulin and collagen type XII genes decreased after passage 3. Alkaline phosphatase activity decreased in cells at later passages. Osteogenic induction of periodontal ligament-derived cells resulted in a down-regulation of the tenomodulin gene. Transplanted cells from both early and late passages produced dense collagen fiber bundles without calcified tissue. CONCLUSION: Cultured periodontal ligament-derived cells were a morphologically homogeneous population, although expression of STRO-1 was limited in primary culture. Cultured cells showed de-differentiation during passage for both osteogenesis- and tendo/ligamentogenesis-related genes.


Subject(s)
Periodontal Ligament/cytology , Tissue Engineering/methods , Adult , Alkaline Phosphatase/analysis , Animals , Antigens, Surface/analysis , Basic Helix-Loop-Helix Transcription Factors/analysis , Bone Morphogenetic Proteins/analysis , Cell Culture Techniques , Cell Transplantation , Collagen Type I/analysis , Collagen Type XII/analysis , Core Binding Factor Alpha 1 Subunit/analysis , Female , Growth Differentiation Factor 5/analysis , Growth Differentiation Factors/analysis , Helix-Loop-Helix Motifs , Homeodomain Proteins/analysis , Humans , Kidney/surgery , Male , Membrane Proteins/analysis , Osteogenesis/physiology , Osteonectin/analysis , Osteopontin/analysis , Rats
4.
J Craniomaxillofac Surg ; 37(1): 30-5, 2009 Jan.
Article in English | MEDLINE | ID: mdl-18948011

ABSTRACT

INTRODUCTION: The purpose of the study was to compare the efficacy on rat skull defects of two bone growth factors derived from the GDF-5 family. MATERIAL AND METHODS: The study was conducted on 17 adult Wistar rats. On each animal, two symmetrical 6-mm wide, full-thickness, skull defects were carried out in the parietal regions. In 15 out of 17 animals, both experimental defects were filled by the implants. In the group I (n=2), both defects were left empty for control. The 15 other rats were divided into 3 groups: In group II (n=5), a collagen sponge was implanted. In group III (n=5), a collagen sponge impregnated with rhGDF-5 (the genuine dimeric form) was implanted. In group IV (n=5), a collagen sponge impregnated with rhGDF-5C465A (a monomeric form of GDF-5) was implanted. All animals were sacrificed at 8 weeks. The harvested specimens were processed for contact radiography and standard histological examination. The quantitative results were assessed with a semi-quantitative histological scoring system. RESULTS: One animal in the group II was excluded because it died of unknown reasons. In group I, no bone healing was observed in the defects. In group II, no bone healing was observed in 4 out of 10 defects, and partial bone healing was observed in 5 out of 10 defects. In group III, partial bone healing was also observed in 3 out of 8 defects and complete bone healing in 4 out of 8 defects. In group IV, partial bone healing was observed in 8 out of 10 defects and complete bone healing in 2 out of 10 defects. CONCLUSION: Bone healing was improved in all treated groups. Further studies are necessary to determine the optimal formulation of these composite implants.


Subject(s)
Bone Diseases/drug therapy , Growth Differentiation Factor 5/therapeutic use , Parietal Bone/drug effects , Absorbable Implants , Alanine/analysis , Animals , Bone Diseases/pathology , Collagen , Cysteine/analysis , Disulfides/analysis , Drug Carriers , Growth Differentiation Factor 5/analysis , Osteogenesis/physiology , Parietal Bone/pathology , Protein Multimerization , Rats , Rats, Wistar , Recombinant Proteins , Treatment Outcome , Wound Healing
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