title: Stromal laminin chain distribution in normal, hyperplastic and malignant oral mucosa: relation to myofibroblast occurrence and vessel formation.
abstract: BACKGROUND
  The contribution of stromal laminin chain expression to malignant potential, tumour stroma reorganization and vessel formation in oral squamous cell carcinoma (OSCC) is not fully understood. Therefore, the expression of the laminin chains alpha2, alpha3, alpha4, alpha5 and gamma2 in the stromal compartment/vascular structures in OSCC was analysed.
  
  
  METHODS
  Frozen tissue of OSCC (9x G1, 24x G2, 8x G3) and normal (2x)/hyperplastic (11x) oral mucosa was subjected to laminin chain and alpha-smooth muscle actin (ASMA) immunohistochemistry. Results were correlated to tumour grade. The relation of laminin chain positive vessels to total vessel number was assessed by immunofluorescence double labelling with CD31.
  
  
  RESULTS
  Stromal laminin alpha2 chain significantly decreases and alpha3, alpha4, alpha5 and gamma2 chains and also ASMA significantly increase with rising grade. The amount of stromal alpha3, alpha4 and gamma2 chains significantly increased with rising ASMA positivity. There is a significant decrease in alpha3 chain positive vessels with neoplastic transformation.
  
  
  CONCLUSIONS
  Mediated by myofibroblasts, OSCC development is associated with a stromal up-regulation of laminin isoforms possibly contributing to a migration promoting microenvironment. A vascular basement membrane reorganization concerning alpha3 and gamma2 chain laminins during tumour angioneogenesis is suggested.
authors.affiliation: Department of Internal Medicine I, University Hospital of Jena, Jena, Germany.
authors.forename: Marcus
authors.initials: M
authors.lastname: Franz
authors.forename: Anke
authors.initials: A
authors.lastname: Wolheim
authors.forename: Petra
authors.initials: P
authors.lastname: Richter
authors.forename: Claudia
authors.initials: C
authors.lastname: Umbreit
authors.forename: Regine
authors.initials: R
authors.lastname: Dahse
authors.forename: Oliver
authors.initials: O
authors.lastname: Driemel
authors.forename: Peter
authors.initials: P
authors.lastname: Hyckel
authors.forename: Ismo
authors.initials: I
authors.lastname: Virtanen
authors.forename: Hartwig
authors.initials: H
authors.lastname: Kosmehl
authors.forename: Alexander
authors.initials: A
authors.lastname: Berndt
mesh_terms: D000199:Actins / Q000032:analysis; D001485:Basement Membrane / Q000473:pathology; D002471:Cell Transformation, Neoplastic / Q000473:pathology; D003238:Connective Tissue / Q000098:blood supply / Q000473:pathology; D042783:Endothelial Cells / Q000473:pathology; D004730:Endothelium, Vascular / Q000473:pathology; D005347:Fibroblasts / Q000473:pathology*; D005455:Fluorescent Antibody Technique; D006801:Humans; D006965:Hyperplasia; D007797:Laminin / Q000032:analysis*; D009061:Mouth Mucosa / Q000098:blood supply / Q000473:pathology*; D009062:Mouth Neoplasms / Q000098:blood supply / Q000473:pathology*; D009389:Neovascularization, Pathologic / Q000473:pathology*; D019408:Platelet Endothelial Cell Adhesion Molecule-1 / Q000032:analysis; D015854:Up-Regulation
chemical_list: D000199:Actins; C501369:LAMA4 protein, human; C400567:LAMC2 protein, human; D007797:Laminin; D019408:Platelet Endothelial Cell Adhesion Molecule-1; C102645:laminin alpha 2; C097043:laminin alpha5; C095567:laminin alpha 3