Asporin in compressed periodontal ligament cells inhibits bone formation

Ueda, Masae; Goto, Tetsuya; Kuroishi, Kayoko N.; Gunjigake, Kaori; Ikeda, Erina; Kataoka, Shinji; Nakatomi, Mitsushiro; Toyono, Takashi; Seta, Yuji; Kawamoto, T.

doi:10.1016/j.archoralbio.2015.11.010

Cited by 31 publications

(31 citation statements)

References 26 publications

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“…Various methods have been developed for the application of compressive forces in vitro, including weighted glass cylinders (18), hydrostatic pressure (2), the release of a pre-stretched membrane (16), and centrifugal force (25,28). Cell damage such as apoptosis (13) must also be considered during the application of force.…”

Section: Discussionmentioning

confidence: 99%

Response to light compressive force in human cementoblasts in vitro

et al. 2016

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The objective of this study is to investigate the responses of human cementoblasts to light compressive force in vitro. A human cementoblast cell line (HCEM) was loaded for 12 h by mounting coverslips (0.25 gf/cm 2 ). The coverslips were removed and the cells were cultured for up to 21 days. Cells without glass loading were used as controls. Cell growth, morphological changes, and the mRNA expression of RUNX2, ALP, WNT5A and SPON1 were investigated. No significant differences were observed in cell numbers between the compressed group and control group. Morphology of the compressed cells was slightly flattened on day 0; however, no indications of cell death were detected. Expression of differentiation markers including RUNX2, ALP and WNT5A was significantly lower in the compressed group (0.7, 0.75 and 0.75-fold respectively, P < 0.05) than in the control group on day 7. The expression levels of SPON1, a differentiation marker of cementoblasts, were higher on days 7 and 14 than on day 0, but were lower in the compressed group than in the control group (P < 0.01). These results suggest that light compressive force does not affect cell growth and morphology, but restrains higher expression of cementogenic differentiation markers in human cementoblasts in vitro.

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Section: Discussionmentioning

confidence: 99%

Response to light compressive force in human cementoblasts in vitro

et al. 2016

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“…as a member of the small leucine-rich repeat proteoglycan (SlrP) family (1,2), periodontal ligament-associated protein-1 (PlaP-1) plays an important role in maintaining the homeostasis of the periodontium (3,4), and protects the periodontal ligament from excessive osteogenesis by the negative regulation of the osteoblastic differentiation of periodontal fibroblasts (5) and periodontal ligament stem cells (PDLSCs) into mineralized tissue-forming cells (3,6). dental follicle stem cells (dfScs) and PdlScs are potentially able to differentiate into the periodontal lineage (7), and are therefore of value in dental tissue engineering (8).…”

Section: Introductionmentioning

confidence: 99%

Periodontal ligament‑associated protein‑1 delays rat periodontal bone defect repair by regulating osteogenic differentiation of bone marrow stromal cells and osteoclast activation

Liu

Wang

et al. 2017

Int J Mol Med

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The aim of the present study was to assess the roles of periodontal ligament‑associated protein‑1 (PLAP‑1) in the osteogenic differentiation of rat bone marrow stromal cells (rBMSCs) and in osteoclast activation during the repair of rat periodontal bone defects. Male, 6‑week‑old, Wistar rats treated with periodontal bone defects were randomly assigned to 3 groups: The PLAP‑1‑transfected rBMSC group (PLAP‑1 group), the empty vector‑transfected rBMSC group (vector group) and the normal rBMSC group (control group). Specimens were obtained at 2, 4 and 6 weeks post‑surgery. Histological observation and micro‑computed tomography were applied to evaluate the repair effect. The bone defect areas of the mandible were dissected for western blotting and reverse transcription-quantitative polymerase chain reaction (RT‑qPCR). Osteogenesis‑associated proteins, including alkaline phosphatase (ALP), bone sialoprotein (BSP), runt-related transcription factor 2 (Runx2), Osterix (Osx) and osteocalcin (OC), as indicators of rBMSC‑induced osteogenesis, were examined by RT-qPCR and western blotting. Osteoclasts were identified and quantified using tartrate‑resistant acid phosphatase staining. Meanwhile, the receptor activator of nuclear factor κΒ ligand (RANKL)/οsteoprotegerin (OPG) ratio was quantified to assess osteoclast activation by western blotting. Τhe repair effect of the PLAP‑1 group was significantly worse than that of the vector and control groups. In the PLAP‑1 group, newly formed and mineralized bones were significantly less in quantity than that in the other two groups (P<0.05), and the expression of osteogenic proteins (ALP, BSP, Runx2, Osx and OC) was also reduced (P<0.01). However, there was no significant difference between the vector and control groups. The RANKL/OPG ratio was upregulated in the PLAP‑1 group due to decreased OPG protein expression and a simultaneous increase in RANKL protein expression (P<0.01), and more osteoclasts were activated in the PLAP‑1 group (P<0.01). In conclusion, the present study found that PLAP‑1 delays rat periodontal bone defect repair by inhibiting osteogenic differentiation and promoting osteoclast activation, mainly dependent on the upregulation of the RANKL/OPG ratio.

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“…Asporin expression has been detected in dermis, perichondrium and periosteum, tendon, and eye sclera [ 21 , 22 ]. Concluded from several in vitro studies, asporin function has been related to collagen fibrillogenesis and collagen mineralization [ 17 , 23 – 25 ]. Asporin has also been suggested to modulate cellular response to FGF-2 [ 26 ], BMP-2 [ 24 ], and TGF-β [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Asporin-deficient mice have tougher skin and altered skin glycosaminoglycan content and structure

et al. 2017

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The main structural component of connective tissues is fibrillar, cross-linked collagen whose fibrillogenesis can be modulated by Small Leucine-Rich Proteins/Proteoglycans (SLRPs). Not all SLRPs’ effects on collagen and extracellular matrix in vivo have been elucidated; one of the less investigated SLRPs is asporin. Here we describe the successful generation of an Aspn-/- mouse model and the investigation of the Aspn-/- skin phenotype. Functionally, Aspn-/- mice had an increased skin mechanical toughness, although there were no structural changes present on histology or immunohistochemistry. Electron microscopy analyses showed 7% thinner collagen fibrils in Aspn-/- mice (not statistically significant). Several matrix genes were upregulated, including collagens (Col1a1, Col1a2, Col3a1), matrix metalloproteinases (Mmp2, Mmp3) and lysyl oxidases (Lox, Loxl2), while lysyl hydroxylase (Plod2) was downregulated. Intriguingly no differences were observed in collagen protein content or in collagen cross-linking-related lysine oxidation or hydroxylation. The glycosaminoglycan content and structure in Aspn-/- skin was profoundly altered: chondroitin/dermatan sulfate was more than doubled and had an altered composition, while heparan sulfate was halved and had a decreased sulfation. Also, decorin and biglycan were doubled in Aspn-/- skin. Overall, asporin deficiency changes skin glycosaminoglycan composition, and decorin and biglycan content, which may explain the changes in skin mechanical properties.

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Asporin in compressed periodontal ligament cells inhibits bone formation

Cited by 31 publications

References 26 publications

<b>Response to light compressive force in human cementoblasts </b><i><b>in </b></i><i><b>vitro </b></i>

<b>Response to light compressive force in human cementoblasts </b><i><b>in </b></i><i><b>vitro </b></i>

Periodontal ligament‑associated protein‑1 delays rat periodontal bone defect repair by regulating osteogenic differentiation of bone marrow stromal cells and osteoclast activation

Asporin-deficient mice have tougher skin and altered skin glycosaminoglycan content and structure

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