title: Proteomic analysis of porcine bone-conditioned medium.
abstract: OBJECTIVE
  Autografts are considered to support bone regeneration. Paracrine factors released from cortical bone might contribute to the overall process of graft consolidation. The aim of this study was to characterize the paracrine factors by means of proteomic analysis.
  
  
  METHODS
  Bone-conditioned medium (BCM) was prepared from fresh bone chips of porcine mandibles and subjected to proteomic analysis. Proteins were categorized and clustered using the bioinformatic tools UNIPROT and PANTHER, respectively.
  
  
  RESULTS
  Proteomic analysis showed that BCM contains more than 150 proteins, of which 43 were categorized into "secreted" and "extracellular matrix." Growth factors that are not only detectable in BCM, but potentially also target cellular processes involved in bone regeneration, eg, pleiotrophin, galectin-1, transforming growth factor beta (TGF-β)-induced gene (TGFBI), lactotransferrin, insulin-like growth factor (IGF)-binding protein 5, latency-associated peptide forming a complex with TGF-β1, and TGF-β2, were discovered.
  
  
  CONCLUSIONS
  The present results demonstrate that cortical bone chips release a large spectrum of proteins with the possibility of modulating cellular aspects of bone regeneration. The data provide the basis for future studies to understand how these paracrine factors may contribute to the complex process of graft consolidation.
authors.forename: Jordi
authors.initials: J
authors.lastname: Caballé-Serrano
authors.forename: Dieter D
authors.initials: DD
authors.lastname: Bosshardt
authors.forename: Daniel
authors.initials: D
authors.lastname: Buser
authors.forename: Reinhard
authors.initials: R
authors.lastname: Gruber
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000032:analysis; D018929:Cell Culture Techniques; D017077:Culture Media, Conditioned; D016207:Cytokines / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000032:analysis; D037483:Galectin 1 / Q000032:analysis; D018975:Insulin-Like Growth Factor Binding Protein 5 / Q000032:analysis; D036341:Intercellular Signaling Peptides and Proteins / Q000032:analysis*; D007781:Lactoferrin / Q000032:analysis; D008334:Mandible / Q000737:chemistry*; D019899:Paracrine Communication / Q000502:physiology; D060066:Protein Interaction Maps; D040901:Proteomics; D013552:Swine; D053719:Tandem Mass Spectrometry; D015533:Transcriptional Activation; D016212:Transforming Growth Factor beta / Q000032:analysis; D053773:Transforming Growth Factor beta1 / Q000032:analysis; D000099222:betaIG-H3 Protein
chemical_list: D002352:Carrier Proteins; D017077:Culture Media, Conditioned; D016207:Cytokines; D016326:Extracellular Matrix Proteins; D037483:Galectin 1; D018975:Insulin-Like Growth Factor Binding Protein 5; D036341:Intercellular Signaling Peptides and Proteins; D007781:Lactoferrin; D016212:Transforming Growth Factor beta; D053773:Transforming Growth Factor beta1; D000099222:betaIG-H3 Protein; C066845:pleiotrophin