title: Two members of the SIBLING family of proteins, DSPP and BSP, may predict the transition of oral epithelial dysplasia to oral squamous cell carcinoma.
abstract: BACKGROUND
  : Patients with oral premalignant lesions (OPL) present with oral squamous cell carcinomas (OSCC) at a much higher rate than the general population. There are currently no useful markers that indicate specifically which OPLs are most likely to progress. Three small integrin binding ligands N-linked glycoprotein (SIBLING) family proteins, bone sialoprotein (BSP), osteopontin (OPN), and dentin sialophosphoprotein (DSPP), have been shown to be up-regulated in many cancers, including OSCC. The status of SIBLING expression in OPLs and their correlation to transition to oral cancer are unknown.
  
  
  METHODS
  : Sixty archival surgical biopsies of dysplastic OPLs were evaluated by immunohistochemistry for expression of BSP, DSPP, and OPN and correlated with local transformation to OSCC at sites adjacent to surgically removed dysplastic OPL.
  
  
  RESULTS
  : The OPL patient population was representative of previous studies with 20% progressing to OSCC, and no correlation between degree of dysplasia and progression. Eighty-seven percent were positive for at least 1 SIBLING protein. OPN expression had no correlation with progression. The BSP+/DSPP- expression pattern however correlated with decreased transformation to OSCC (point prevalence = 0%; 95% confidence interval [CI], 0-20.6), whereas the BSP-/DSPP+ pattern was associated with more frequent progression (point prevalence = 77.8%; 95%CI, 47.8-95.4). Incrementally higher expression scores (0 to 3) of BSP and DSPP were also associated with increased predictive values (odds ratio, 25.53; 95% CI, 2.14-304.7 and 10.13; 95% CI, 2.0-50.0, respectively, for each increment).
  
  
  CONCLUSIONS
  : BSP and DSPP are excellent candidate markers for successful OPL surgical intervention and may be predictors of OPL-OSCC progression. Cancer 2010. (c) 2010 American Cancer Society.
authors.affiliation: School of Dentistry, Medical College of Georgia, Augusta, Georgia, USA. kogbureke@mail.mcg.edu
authors.forename: Kalu U E
authors.initials: KU
authors.lastname: Ogbureke
authors.forename: Rafik A
authors.initials: RA
authors.lastname: Abdelsayed
authors.forename: Harvey
authors.initials: H
authors.lastname: Kushner
authors.forename: Li
authors.initials: L
authors.lastname: Li
authors.forename: Larry W
authors.initials: LW
authors.lastname: Fisher
mesh_terms: D002294:Carcinoma, Squamous Cell / Q000378:metabolism*; D002471:Cell Transformation, Neoplastic; D018450:Disease Progression; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D058574:Integrin-Binding Sialoprotein; D008297:Male; D009061:Mouth Mucosa / Q000473:pathology*; D009062:Mouth Neoplasms / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D011230:Precancerous Conditions / Q000378:metabolism; D012189:Retrospective Studies; D012795:Sialoglycoproteins / Q000378:metabolism*; D000099311:Dentin Sialophosphoprotein
chemical_list: D016326:Extracellular Matrix Proteins; D058574:Integrin-Binding Sialoprotein; D010750:Phosphoproteins; D012795:Sialoglycoproteins; D000099311:Dentin Sialophosphoprotein; C546871:IBSP protein, human