title: Expression of alpha 3 beta 1 integrin receptor and its ligands in human lung tumors.
abstract: Increasing experimental evidence demonstrates that malignant transformation is associated with changes in the repertoire of expression of the integrin family of molecules, which mediate cell-matrix and cell-cell interactions. We have analyzed immunohistochemically and immunochemically the expression of VLA-3 integrin and its known ligands, namely, laminin (LM), fibronectin (FN), collagen type IV (Coll IV), nicein (NIC), and entactin/nidogen (ENT), in lung tumors of various histological types. alpha 3 beta 1 was detectable in normal bronchial epithelium and along basement membranes of alveolar walls. In non-small cell lung carcinomas (NSCLC) the integrin was expressed in 82% of the cases, independently of histological type and degree of differentiation of the tumors. On the other hand, only 13% of the small cell lung carcinomas (SCLC) displayed a weak and heterogeneous distribution of the alpha 3 beta 1 complex. Our findings were confirmed immunochemically using long-term tumor cell lines. While the expression of both alpha 3 beta 1 and ligands LM, FN, Coll IV, and Ent correlated in NSCLC with the presence of basement membranes, FN was the only ligand detectable in the stroma of SCLCs. A selective loss of nicein in basement membranes was demonstrated in NSCLC indicating an impairment of expression of this glycoprotein following malignant transformation.
authors.affiliation: Department of Immunology, Regina Elena Cancer Institute, Rome, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Bartolazzi
authors.forename: C
authors.initials: C
authors.lastname: Cerboni
authors.forename: G
authors.initials: G
authors.lastname: Flamini
authors.forename: A
authors.initials: A
authors.lastname: Bigotti
authors.forename: L
authors.initials: L
authors.lastname: Lauriola
authors.forename: P G
authors.initials: PG
authors.lastname: Natali
mesh_terms: D000230:Adenocarcinoma / Q000378:metabolism*; D000911:Antibodies, Monoclonal; D001485:Basement Membrane / Q000378:metabolism; D002289:Carcinoma, Non-Small-Cell Lung / Q000378:metabolism*; D018288:Carcinoma, Small Cell / Q000378:metabolism*; D002294:Carcinoma, Squamous Cell / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007797:Laminin / Q000378:metabolism; D008024:Ligands; D008168:Lung / Q000378:metabolism*; D008175:Lung Neoplasms / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D016029:Receptors, Very Late Antigen / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D000097794:Kalinin
chemical_list: D000911:Antibodies, Monoclonal; D015815:Cell Adhesion Molecules; D003094:Collagen; D005353:Fibronectins; D007797:Laminin; D008024:Ligands; D008562:Membrane Glycoproteins; D016029:Receptors, Very Late Antigen; D000097794:Kalinin; C029967:nidogen