title: The matrix metalloproteinase system in oral squamous cell carcinoma.
abstract: BACKGROUND
  The matrix metalloproteinase (MMP) system is responsible for degradation of tissue in both normal and pathological processes, including tumour invasion and metastasis.
  
  
  OBJECTIVE
  To compare tissue concentrations of components of the MMP system between tumour tissue and normal tissue in patients with oral squamous cell carcinoma, and to correlate concentrations with pathological grade of tumour.
  
  
  METHODS
  Thirty-eight paired tissue samples from tumours and normal tissue were analysed by three laboratory techniques: firstly, enzyme linked immunosorbent assays (ELISA) in ng/mg protein for MMP-1, MMP-3, and tissue inhibitors of metalloproteinases (TIMPs) -1 and -2. Secondly, gelatinase activity assays to measure concentrations of total and endogenous active gelatinases, MMP-2 and MMP-9 (ng/mg protein). And thirdly to use quenched fluorescent substrate hydrolysis to measure total MMP activity (pM/min).
  
  
  RESULTS
  The concentration of all MMPs was significantly higher in tumour than in normal oral tissue (p < 0.05, Mann-Whitney U-test). Tissue concentrations of some of these factors correlated with clinical and pathological indices of aggressiveness of tumours, including T-stage, N-stage, tumour differentiation, and anatomical level of involved nodes. However, the study was not powered to show statistical significance.
  
  
  CONCLUSIONS
  It is the balance between proteinases and their inhibitors that controls tissue degradation at each stage of tumour invasion and metastasis. Measurement of MMPs in oral mucosal biopsy samples may establish the invasive potential of tumours at their initial presentation.
authors.affiliation: Professorial Unit of Surgery, University Hospital of North Tees, Stockton on Tees TS19 8PE, UK. drlizbaker@yahoo.co.uk
authors.forename: E A
authors.initials: EA
authors.lastname: Baker
authors.forename: D J
authors.initials: DJ
authors.lastname: Leaper
authors.forename: J P
authors.initials: JP
authors.lastname: Hayter
authors.forename: A J
authors.initials: AJ
authors.lastname: Dickenson
mesh_terms: D000293:Adolescent; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D002294:Carcinoma, Squamous Cell / Q000201:enzymology* / Q000556:secondary; D002454:Cell Differentiation; D005260:Female; D018093:Gelatinases / Q000032:analysis; D006801:Humans; D008207:Lymphatic Metastasis / Q000473:pathology; D008297:Male; D020781:Matrix Metalloproteinase 1 / Q000032:analysis; D020778:Matrix Metalloproteinase 2 / Q000032:analysis; D019278:Matrix Metalloproteinase 3 / Q000032:analysis; D020780:Matrix Metalloproteinase 9 / Q000032:analysis; D020782:Matrix Metalloproteinases / Q000032:analysis*; D008875:Middle Aged; D009061:Mouth Mucosa / Q000201:enzymology; D009062:Mouth Neoplasms / Q000201:enzymology*; D009361:Neoplasm Invasiveness; D009367:Neoplasm Staging; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000032:analysis; D019716:Tissue Inhibitor of Metalloproteinase-2 / Q000032:analysis
chemical_list: D019715:Tissue Inhibitor of Metalloproteinase-1; D019716:Tissue Inhibitor of Metalloproteinase-2; D018093:Gelatinases; D020782:Matrix Metalloproteinases; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9; D020781:Matrix Metalloproteinase 1