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Leucine-Rich Amelogenin Peptide (LRAP) Uptake by Cementoblast Requires Flotillin-1 Mediated Endocytosis.
Martins, Luciane; Leme, Adriana Franco Paes; Kantovitz, Kamila Rosamilia; de Luciane Martins, Em Nome; Sallum, Enilson Antonio; Casati, Márcio Zaffalon; Nociti, Francisco Humberto.
Afiliação
  • Martins L; Division of Periodontics, Department of Prosthodontics and Periodontics, Piracicaba Dental School, University of Campinas-UNICAMP, Piracicaba, Sao Paulo, Brazil.
  • Leme AF; Brazilian Biosciences National Laboratory (LNBio), CNPEM, Campinas, Brazil.
  • Kantovitz KR; Department of Pediatric Dentistry, Piracicaba Dental School, University of Campinas-UNICAMP, Piracicaba, Sao Paulo, Brazil.
  • de Luciane Martins EN; Department of Dental Materials, São Leopoldo Mandic Research Center, Campinas, Sao Paulo, Brazil.
  • Sallum EA; Division of Periodontics, Department of Prosthodontics and Periodontics, Piracicaba Dental School, University of Campinas-UNICAMP, Piracicaba, Sao Paulo, Brazil.
  • Casati MZ; Division of Periodontics, Department of Prosthodontics and Periodontics, Piracicaba Dental School, University of Campinas-UNICAMP, Piracicaba, Sao Paulo, Brazil.
  • Nociti FH; Division of Periodontics, Department of Prosthodontics and Periodontics, Piracicaba Dental School, University of Campinas-UNICAMP, Piracicaba, Sao Paulo, Brazil.
J Cell Physiol ; 232(3): 556-565, 2017 Mar.
Article em En | MEDLINE | ID: mdl-27277399
Basic, pre-clinical, and clinical studies have documented the potential of amelogenin, and its variants, to affect cell response and tissue regeneration. However, the mechanisms are unclear. Thus, the aim of the present study was to identify, in cementoblasts, novel binding partners for an alternatively spliced amelogenin form (Leucine-Rich Amelogenin Peptide-LRAP), which is supposed to act as a signaling molecule in epithelial-mesenchymal interactions. LRAP-binding protein complexes from immortalized murine cementoblasts (OCCM-30) were achieved by capture affinity assay (GST pull down) and proteins present in these complexes were identified by mass spectrometry and immunoblotting. Flotillin-1, which functions as a platform for signal transduction, vesicle trafficking, endocytosis, and exocytosis, was identified and confirmed by co-precipitation and co-localization assays as a protein-binding partner for LRAP in OCCM-30 cells. In addition, we found that exogenously added GST-LRAP recombinant protein was internalized by OCCM-30 cells, predominantly localized in the perinuclear region and, that inhibition of flotillin1-dependent functions by small interference RNA (siRNA) methodology significantly affected LRAP uptake and its biological properties on OCCM-30 cells, including LRAP effect on the expression of genes encoding osteocalcin (Ocn), bone sialoprotein (Bsp), and runt-related transcription factor 2 (RunX2). In conclusion, LRAP uptake by cementoblast involves flotillin-assisted endocytosis, which suggests an involvement of LRAP in lipid-raft-dependent signaling pathways which are mediated by flotillin-1. J. Cell. Physiol. 232: 556-565, 2017. © 2016 Wiley Periodicals, Inc.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Cemento Dentário / Proteínas do Esmalte Dentário / Endocitose / Proteínas de Membrana Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: J Cell Physiol Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Cemento Dentário / Proteínas do Esmalte Dentário / Endocitose / Proteínas de Membrana Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Revista: J Cell Physiol Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos