title: Protein biomarker analysis of primary Peyronie's disease cells.
abstract: BACKGROUND
  The molecular pathogenesis of Peyronie's Disease (PD) remains unclear more than 250 years after its initial description. Because of this, no test is currently available to accurately predict PD progression among those affected.
  
  
  OBJECTIVE
  To investigate the expression of wound healing and fibrosis-associated proteins in primary cell cultures of PD fibroblasts to determine whether altered protein expression patterns can be used as predictors of clinical course and natural history.
  
  
  METHODS
  Primary cell cultures derived from normal Tunica albuginea tissue and PD plaque tissue were examined by immuno-cytochemistry. Protein expression profiles were analyzed by Surface-Enhanced Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (SELDI-TOF-MS) and Western immunoblotting.
  
  
  METHODS
  Expression of wound healing and fibrosis-associated proteins and protein expression patterns were assessed.
  
  
  RESULTS
  Statistically significant increases in smooth muscle alpha-actin, beta-catenin, and Heat shock proteins (Hsp47) were identified in cells derived from PD relative to cells derived from normal Tunica albuginea tissue. Changes in TGFbeta-1 receptor and Fibronectin were also observed. In addition, altered expression of additional as yet unidentified proteins at 4.7, 8.9, 10.8, 16.8, and 76.8 kDa were detected by complementary SELDI-TOF-MS approaches.
  
  
  CONCLUSIONS
  Primary cells derived from PD plaques display up-regulated expression of several proteins that are established components of fibrosis and wound healing. In addition, changes in other, as yet unidentified proteins were measured. It will be of interest to conduct further studies to see whether these dysregulated protein peaks represent potential biological markers of disease progression.
authors.affiliation: Lawson Health Research Institute, Urology, London, ON, Canada. ldeyoung@lawsonimaging.ca
authors.forename: Ling X
authors.initials: LX
authors.lastname: De Young
authors.forename: Anthony J
authors.initials: AJ
authors.lastname: Bella
authors.forename: David B
authors.initials: DB
authors.lastname: O'Gorman
authors.forename: Bing S
authors.initials: BS
authors.lastname: Gan
authors.forename: Kok B
authors.initials: KB
authors.lastname: Lim
authors.forename: Gerald B
authors.initials: GB
authors.lastname: Brock
mesh_terms: D000199:Actins / Q000378:metabolism; D015415:Biomarkers / Q000378:metabolism*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000473:pathology*; D005353:Fibronectins / Q000378:metabolism; D005355:Fibrosis / Q000473:pathology; D050958:HSP47 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D008297:Male; D010411:Penile Induration / Q000473:pathology*; D040081:Protein Array Analysis / Q000379:methods*; D040901:Proteomics / Q000379:methods*; D053773:Transforming Growth Factor beta1 / Q000378:metabolism; D015854:Up-Regulation / Q000502:physiology; D014945:Wound Healing / Q000502:physiology; D051176:beta Catenin / Q000378:metabolism
chemical_list: C541116:ACTA2 protein, human; D000199:Actins; D015415:Biomarkers; C495270:CTNNB1 protein, human; D005353:Fibronectins; D050958:HSP47 Heat-Shock Proteins; C494660:SERPINH1 protein, human; D053773:Transforming Growth Factor beta1; D051176:beta Catenin