Different Phenotypes in Human Prostate Cancer: α6 or α3 Integrin in Cell-extracellular Adhesion Sites

• DOI: 10.1038/sj.neo.7900223
• Publication Date: 2002-09-05T18:49:51Z
• Authors: Monika Schmelz; Anne E. Cress; Katherine M. Scott; Friederike Burger; Haiyan Cui; Karim Sallam; Kathy M. McDaniel; Bruce L. Dalkin; Raymond B. Nagle
• Keywords: Male; 0301 basic medicine; Integrins; Integrin alpha3; Biopsy; Integrin alpha6; 03 medical and health sciences; Antigens, CD; Cell Adhesion; Humans; RC254-282; Alleles; Binding Sites; Microscopy, Confocal; Neoplasms. Tumors. Oncology. Including cancer and carcinogens; Prostatic Neoplasms; α6/α3 integrin; Prostate-Specific Antigen; prostate cancer; focal adhesion proteins; Phosphoproteins; Immunohistochemistry; CD 151; 3. Good health; Cytoskeletal Proteins; Phenotype; Microscopy, Fluorescence; Mutation; Paxillin

The distribution of alpha6/alpha3 integrin in adhesion complexes at the basal membrane human normal and cancer prostate glands was analyzed 135 biopsies from 61 patients. levels polarized expression tumor were determined by quantitative immunohistochemistry. compared with Gleason sum score, pathological stage, preoperative serum prostate-specific antigen (PSA). associations assessed statistical methods. Eighty percent tumors expressed alpha6 or alpha3 20% integrin-negative. but not PSA, associated expression. Low score correlated increased expression, high low negative Three phenotypes distinguished based on differential Type I coexpressed both subunits, type II exclusively integrin, III only. Fifteen cases further examined for codistribution vinculin, paxillin, CD 151 frozen serial sections using confocal laser scanning microscopy. integrins, CD151, vinculin present within glands. In carcinoma, colocalized 151, paxillin. phenotype I, subunit did colocalize alpha indicating existence two different complexes. Human display their cell surface alpha6beta1 and/or alpha3beta1 integrins. identified, suggesting a reorganization structures cancer.