title: Gingival, dermal, and periodontal ligament fibroblasts express different extracellular matrix receptors.
abstract: BACKGROUND
  Fibroblasts are the predominant cells of the periodontal ligament and the gingiva and have important roles in the function and regeneration of the tooth support apparatus. The goal of this study was to investigate the possible differences in the adhesion properties and expression of extracellular matrix (ECM) receptors among different fibroblast populations.
  
  
  METHODS
  The adhesion of gingival (GF), dermal (DF), and periodontal ligament fibroblast (PDLF) cultures to ECM proteins (fibronectin, laminin, vitronectin, RGD peptide, collagen type I, and collagen type IV) adsorbed to tissue culture plastic was evaluated fluorometrically. Quantitative reverse transcription-polymerase chain reactions (RT-PCR) were performed using primers specific for 19 integrin subunits to quantify ECM receptor transcript expression.
  
  
  RESULTS
  Our data demonstrated that GF and PDLF adhere to vitronectin and collagen types I and IV more avidly than do DF. PDLF adhered well to laminin, whereas GF and DF did not. Quantitation of integrin expression demonstrated that the different fibroblast types expressed different integrin transcripts, further demonstrating their innate differences.
  
  
  CONCLUSIONS
  The 3 fibroblast types studied behave differently and expressed different ECM receptors. However, gingival fibroblasts and periodontal ligament fibroblasts are more similar in their attachment and integrin expression than either is to dermal fibroblasts. Therefore, experiments using DF will not necessarily be valid for oral tissues.
authors.affiliation: Louisiana State University Health Sciences Center, School of Dentistry, Department of Periodontology, New Orleans 70119, USA.
authors.forename: A A
authors.initials: AA
authors.lastname: Palaiologou
authors.forename: R A
authors.initials: RA
authors.lastname: Yukna
authors.forename: R
authors.initials: R
authors.lastname: Moses
authors.forename: T E
authors.initials: TE
authors.lastname: Lallier
mesh_terms: D002448:Cell Adhesion; D002460:Cell Line; D002478:Cells, Cultured; D003094:Collagen / Q000032:analysis / Q000235:genetics; D016326:Extracellular Matrix Proteins / Q000032:analysis / Q000235:genetics*; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism*; D005353:Fibronectins / Q000032:analysis / Q000235:genetics; D005470:Fluorometry; D005881:Gingiva / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000032:analysis / Q000235:genetics*; D007797:Laminin / Q000032:analysis / Q000235:genetics; D009842:Oligopeptides / Q000032:analysis / Q000235:genetics; D010513:Periodontal Ligament / Q000166:cytology / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000032:analysis / Q000235:genetics*; D011971:Receptors, Immunologic / Q000032:analysis / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012867:Skin / Q000166:cytology / Q000378:metabolism*; D019096:Vitronectin / Q000032:analysis / Q000235:genetics
chemical_list: D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D016023:Integrins; D007797:Laminin; D009842:Oligopeptides; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D019096:Vitronectin; C047981:arginyl-glycyl-aspartic acid; D003094:Collagen