title: A study of the extracellular matrix in salivary gland tumors.
abstract: BACKGROUND
  Epithelial-mesenchymal interactions constitute fundamental phenomena in the development and maintenance of the characteristic branching pattern seen in salivary glands. This study was undertaken to discuss the extracellular matrix (ECM) role in morphogenesis and cellular differentiation of salivary gland tumors originating from the intercalated duct.
  
  
  METHODS
  The ECM components, laminin (LN), type IV collagen, fibronectin (FN), and tenascin (TN) were revealed using a streptoavidin-biotin immunohistochemical technique and analyzed in 34 cases of salivary gland tumors: pleomorphic adenoma (PA); myoepithelioma; basal cell adenoma (BCA); polymorphous low grade adenocarcinoma (PLGA); and adenoid cystic carcinoma (ACC).
  
  
  RESULTS
  LN and type IV collagen were present in all tumors, confining well-organized duct-like structures, separating them from the stroma, or surrounding cell clusters. In PA and myoepithelioma, the basement membrane (BM) fragmentation was observed through LN and type IV collagen staining around each individual spindle-shaped cell, which was strictly related to the cell modification. Interestingly, BM interruption could not be seen in the malign tumors, however, was frequently augmented in some cases. LN, type IV collagen, and FN were also found in the stroma of all tumors studied, except for the pseudocystic spaces of ACC, which were only delimited by replicated LN and type IV collagen. TN exhibited a variable expression, being more intense in solid ACC.
  
  
  CONCLUSIONS
  LN and type IV collagen were always present around morphologically well-differentiated duct-like structures in all tumors studied. BM interruption could not be seen in the malign tumors, on the contrary BM production was evident, which is probably related to invasion. FN was present in the stroma of all tumors, but TN was mostly observed in less differentiated and higher degree of malignancy tumors, such as solid ACC.
authors.affiliation: Department of Oral Pathology, School of Dentistry, Braz Cubas University, São Paulo, Brazil. rraitz@acpd.org.br
authors.forename: R
authors.initials: R
authors.lastname: Raitz
authors.forename: M D
authors.initials: MD
authors.lastname: Martins
authors.forename: V C
authors.initials: VC
authors.lastname: Araújo
mesh_terms: D000230:Adenocarcinoma / Q000378:metabolism / Q000473:pathology; D000236:Adenoma / Q000378:metabolism / Q000473:pathology; D008949:Adenoma, Pleomorphic / Q000378:metabolism / Q000473:pathology; D001485:Basement Membrane / Q000378:metabolism / Q000473:pathology*; D024141:Collagen Type IV / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism / Q000473:pathology*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D007797:Laminin / Q000378:metabolism; D009208:Myoepithelioma / Q000378:metabolism / Q000473:pathology; D012468:Salivary Gland Neoplasms / Q000378:metabolism / Q000473:pathology*; D019063:Tenascin / Q000378:metabolism
chemical_list: D024141:Collagen Type IV; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D007797:Laminin; D019063:Tenascin