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Novel LRAP-binding partner revealing the plasminogen activation system as a regulator of cementoblast differentiation and mineral nodule formation in vitro.
Martins, Luciane; Amorim, Bruna Rabelo; Salmon, Cristiane Ribeiro; Leme, Adriana Franco Paes; Kantovitz, Kamila Rosamilia; Nociti, Francisco Humberto.
Afiliação
  • Martins L; Department of Prosthodontics and Periodontics, Division of Periodontics, Piracicaba Dental School, State University of Campinas, Piracicaba, SP, Brazil.
  • Amorim BR; Laboratory of Oral Histopathology, Faculty of Health Sciences, University of Brasilia, Brasilia, DF, Brazil.
  • Salmon CR; Department of Prosthodontics and Periodontics, Division of Periodontics, Piracicaba Dental School, State University of Campinas, Piracicaba, SP, Brazil.
  • Leme AFP; UNIP, Dental Research Division, School of Dentistry, Paulista University, Sao Paulo, SP, Brazil.
  • Kantovitz KR; LNBio, Brazilian Center for Research in Energy and Materials (CNPEM), Brazilian Biosciences National Laboratory, Campinas, SP, Brazil.
  • Nociti FH; Department of Pediatric Dentistry, Piracicaba Dental School, State University of Campinas, Piracicaba, SP, Brazil.
J Cell Physiol ; 235(5): 4545-4558, 2020 05.
Article em En | MEDLINE | ID: mdl-31621902
Amelogenin isoforms, including full-length amelogenin (AMEL) and leucine-rich amelogenin peptide (LRAP), are major components of the enamel matrix, and are considered as signaling molecules in epithelial-mesenchymal interactions regulating tooth development and periodontal regeneration. Nevertheless, the molecular mechanisms involved are still poorly understood. The aim of the present study was to identify novel binding partners for amelogenin isoforms in the cementoblast (OCCM-30), using an affinity purification assay (GST pull-down) followed by mass spectrometry and immunoblotting. Protein-protein interaction analysis for AMEL and LRAP evidenced the plasminogen activation system (PAS) as a potential player regulating OCCM-30 response to amelogenin isoforms. For functional assays, PAS was either activated (plasmin) or inhibited (ε-aminocaproic acid [aminocaproic]) in OCCM-30 cells and the cell morphology, mineral nodule formation, and gene expression were assessed. PAS inhibition (EACA 100 mM) dramatically decreased mineral nodule formation and expression of OCCM-30 differentiation markers, including osteocalcin (Bglap), bone sialoprotein (Ibsp), osteopontin (Spp1), tissue-nonspecific alkaline phosphatase (Alpl) and collagen type I (Col1a1), and had no effect on runt-related transcription factor 2 (Runx2) and Osterix (Osx) mRNA levels. PAS activation (plasmin 5 µg/µl) significantly increased Col1a1 and decreased Bglap mRNA levels (p < .05). Together, our findings shed new light on the potential role of plasminogen signaling pathway in the control of the amelogenin isoform-mediated response in cementoblasts and provide new insights into the development of targeted therapies.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Plasminogênio / Diferenciação Celular / Cementogênese / Cemento Dentário / Proteínas do Esmalte Dentário / Amelogenina Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: J Cell Physiol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Plasminogênio / Diferenciação Celular / Cementogênese / Cemento Dentário / Proteínas do Esmalte Dentário / Amelogenina Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: J Cell Physiol Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos