title: VLA2 integrin expression in breast carcinomas evaluated by automated and quantitative immunohistochemistry.
abstract: VLA2 is thought to be involved in the metastatic process in malignant tumours, in particular in carcinomatous cell adhesion to vessel basement membrane. VLA2 expression was immunohistochemically investigated in 204 breast carcinomas. Frozen tissue sections were probed with monoclonal anti-VLA2 using automated (Ventana ES 320 System) and quantitative (SAMBA 2005 image processor) immunoperoxidase. A positive anti-VLA2 immunoreaction was observed in 48 tumours (23.5%), within epithelial carcinomatous cells. The VLA2-positive surface in tumours varied from 3% to 20% (mean 8.75, S.D. 7.17) and was correlated with histoprognostic indicators and tumour expression of various antigens detected using the same method as that for VLA2. The results show that VLA2 immunoexpression was independent of the tumour size, grade, type and aneuploidy, and of the nodal status. VLA2 significantly correlated with ELAM, VCAM, VLA3 and P-glycoprotein (P-gp) (P < 0.01) and inversely correlated with cathepsin D (P < 0.001), but was independent of Ki67/MIB1, p53, bcl-2, c-erbB-2, E cadherin, CD44v, CD31, oestrogen and progesterone receptors' (ER, PR) antigenic sites and pS2. The exact role, if any, of VLA2 in tumour cell dissemination remains to be elucidated and the clinical relevance of VLA2 immunodetection in breast carcinomas requires further investigation of the correlation between VLA2 immunocytochemical expression and patients' outcome and response to chemotherapy.
authors.affiliation: Department of Pathology, Faculté de Médecine Timore (IFR Immunologie et Cancérologie), Hôpital Nord, Marseille, France.
authors.forename: C
authors.initials: C
authors.lastname: Charpin
authors.forename: S
authors.initials: S
authors.lastname: Garcia
authors.forename: D
authors.initials: D
authors.lastname: Bergeret
authors.forename: L
authors.initials: L
authors.lastname: Andrac
authors.forename: N
authors.initials: N
authors.lastname: Horschowski
authors.forename: R
authors.initials: R
authors.lastname: Choux
authors.forename: M N
authors.initials: MN
authors.lastname: Lavaut
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D014408:Biomarkers, Tumor / Q000096:biosynthesis*; D001943:Breast Neoplasms / Q000378:metabolism*; D015820:Cadherins / Q000096:biosynthesis; D002402:Cathepsin D / Q000096:biosynthesis; D002448:Cell Adhesion / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D019040:E-Selectin / Q000096:biosynthesis; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D039201:Integrin alpha3beta1; D016023:Integrins / Q000096:biosynthesis*; D019394:Ki-67 Antigen / Q000096:biosynthesis; D008875:Middle Aged; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D019408:Platelet Endothelial Cell Adhesion Molecule-1 / Q000096:biosynthesis; D011233:Precipitin Tests; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000096:biosynthesis; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000096:biosynthesis; D038981:Receptors, Collagen; D016159:Tumor Suppressor Protein p53 / Q000096:biosynthesis; D019010:Vascular Cell Adhesion Molecule-1 / Q000096:biosynthesis
chemical_list: D014408:Biomarkers, Tumor; D015820:Cadherins; D002402:Cathepsin D; D019040:E-Selectin; D039201:Integrin alpha3beta1; D016023:Integrins; D019394:Ki-67 Antigen; D009363:Neoplasm Proteins; D019408:Platelet Endothelial Cell Adhesion Molecule-1; D019253:Proto-Oncogene Proteins c-bcl-2; D018719:Erb-b2 Receptor Tyrosine Kinases; D038981:Receptors, Collagen; D016159:Tumor Suppressor Protein p53; D019010:Vascular Cell Adhesion Molecule-1