Periostin is required for matricellular localization of CCN3 in periodontal ligament of mice

Takayama, Issei; Tanabe, Hideyuki; Nishiyama, Takashi; Ito, Hiromitsu; Amizuka, Norio; Li, Minqi; Katsube, Ken‐ichi; Kii, Isao; Kudo, Akira

doi:10.1007/s12079-016-0371-5

Cited by 18 publications

(17 citation statements)

References 63 publications

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“…Thus, we propose that ECM proteins, such as fibronectin and collagen, might dock to the concave side of the dimer where the EMI domain inhabits. Meanwhile, the four Fas1 domains of periostin may bind to tenascin , BMP‐1 , CCN3 , and integrin . Noteworthy to mention, monoclonal antibodies recognizing a region covering residues 136–151 in the Fas1 domain may inhibit integrin‐mediated cell migration .…”

Section: Discussionmentioning

confidence: 99%

Structural characterizations of human periostin dimerization and cysteinylation

Liu

Zhang

et al. 2018

FEBS Letters

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Human periostin plays a multifaceted role in remodeling the extracellular matrix milieu by interacting with other proteins and itself in both a heterophilic and homophilic manner. However, the structural mechanism for its extensive interactions has remained elusive. Here, we report the crystal structures of human periostin (EMI-Fas1 ) and its Cys60Ala mutant. In combination with multi-angle light-scattering analysis and biochemical assays, the crystal structures reveal that periostin mainly exists as a dimer in solution and its homophilic interaction is mainly mediated by the EMI domain. Furthermore, Cys60 undergoes cysteinylation as confirmed by mass spectroscopy, and this site hardly affects the homophilic interaction. Also, the structures yield insights into how periostin forms heterophilic interactions with other proteins under physiological or pathological conditions.

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Section: Discussionmentioning

confidence: 99%

Structural characterizations of human periostin dimerization and cysteinylation

Liu

Zhang

et al. 2018

FEBS Letters

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“…This matched case-control study was conducted on 53 patients with chronic periodontitis and 53 healthy peers. Three periodontal parameters were evaluated and recorded for each patient: Bleeding on Probing (BOP) [3], Clinical Attachment Level (CAL) [13], and Probing Pocket Depth (PPD). All evaluations were performed by a periodontist.…”

Section: Methodsmentioning

confidence: 99%

“…It is characterized by loss of gingival adhesions and, in more advanced stages of the disease, alveolar bone resorption [1]. Perios-P tin is a matriarchal protein secreted by periodontal ligament fibroblasts [3]. The role of periostin in tooth development is very important [4].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Salivary and Gingival Crevicular Fluid Periostin Levels in Chronic Periodontitis Patients and Healthy Subjects

Momeni

Nakhostin

Bayani

2020

J. Arak Univ. Med. Sci.

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Background and Aim Periostin acts as necessary protein in tissue development and has a key role in tooth-supporting tissues such as periodontal ligament. The effect of inflammation on reducing periostin level has been shown in some studies. The aim of this study was to compare the salivary and Gingival Crevicular Fluid (GCF) periostin levels in patients with chronic periodontitis and healthy peers. Methods & Materials In this matched case-control study, 106 participants (53 patients with chronic periodontitis and 53 healthy controls) were studies after signing a informed consent form. They were matched for age, gender, weight, and Body Mass Index (BMI). The GCF and salivary samples were collected from all participants and were assessed using standard Enzyme-Linked Immunosorbent Assay (ELISA). The statistical analysis was conducted in Stata V. 11. Ethical Considerations This study was approved by the Research Ethics Committee of Arak University of Medical Sciences (Code: IR.ARAKMU.REC.1397.34). Results The salivary and GCF periostin levels was significantly lower in patients than in healthy subjects (P<0.001). Moreover, the periostin levels was significantly different based on periodontal parameters (P<0.001). Conclusion There is association between the incidence of chronic periodontitis and salivary and GCF periostin levels. Hence, the periostin may act as a potential biomarker for the diagnosis of chronic periodontitis and prevention of its progression.

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“…Periostin is reported to bind to several extracellular matrix (ECM) molecules and growth factors such as type I collagen and Notch1 8 , 9 . It has been reported that Periostin directly interacts with Fibronectin 10 through its EMI domain, while Tenascin-C 7 , CCN3 11 and BMP1 12 through Fas I domain. These findings suggest that Periostin is a multi-functional protein possibly through orchestrating these binding proteins inside and outside of the cell 13 .…”

Section: Introductionmentioning

confidence: 99%

“…while Tenascin-C 7 , CCN3 11 and BMP1 12 through Fas I domain. These findings suggest that Periostin is a multifunctional protein possibly through orchestrating these binding proteins inside and outside of the cell 13 .…”

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confidence: 99%

FAM20C directly binds to and phosphorylates Periostin

Lin

Ohyama

et al. 2020

Sci Rep

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It is widely accepted that FAM20C functions as a Golgi casein kinase and has large numbers of kinase substrates within the secretory pathway. It has been previously reported that FAM20C is required for maintenance of healthy periodontal tissues. However, there has been no report that any extracellular matrix molecules expressed in periodontal tissues are indeed substrates of FAM20C. In this study, we sought to identify the binding partner(s) of FAM20C. FAM20C wild-type (WT) and its kinase inactive form D478A proteins were generated. These proteins were electrophoresed and the Coomassie Brilliant Blue (CBB)-positive bands were analyzed to identify FAM20C-binding protein(s) by Mass Spectrometry (MS) analysis. Periostin was found by the analysis and the binding between FAM20C and Periostin was investigated in cell cultures and in vitro. We further determined the binding region(s) within Periostin responsible for FAM20C-binding. Immunolocalization of FAM20C and Periostin was examined using mouse periodontium tissues by immunohistochemical analysis. In vitro kinase assay was performed using Periostin and FAM20C proteins to see whether FAM20C phosphorylates Periostin in vitro. We identified Periostin as one of FAM20C-binding proteins by MS analysis. Periostin interacted with FAM20C in a kinase-activity independent manner and the binding was direct in vitro. We further identified the binding domain of FAM20C in Periostin, which was mapped within Fasciclin (Fas) I domain 1–4 of Periostin. Immunolocalization of FAM20C was observed in periodontal ligament (PDL) extracellular matrix where that of Periostin was also immunostained in murine periodontal tissues. FAM20C WT, but not D478A, phosphorylated Periostin in vitro. Consistent with the overlapped expression pattern of FAM20C and Periostin, our data demonstrate for the first time that Periostin is a direct FAM20C-binding partner and that FAM20C phosphorylates Periostin in vitro.

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Periostin is required for matricellular localization of CCN3 in periodontal ligament of mice

Cited by 18 publications

References 63 publications

Structural characterizations of human periostin dimerization and cysteinylation

Structural characterizations of human periostin dimerization and cysteinylation

Comparison of Salivary and Gingival Crevicular Fluid Periostin Levels in Chronic Periodontitis Patients and Healthy Subjects

FAM20C directly binds to and phosphorylates Periostin

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