Results: The 1889c-shcFlip, but not the shcFlip-HaCat, showed sensitivity to TRAIL (tumor necrosis factor-related apoptosis-inducing ligand), accompanied by an overexpression of both the pro-apoptotic protein Noxa (p<10-4) and the anti-apoptotic proteins BIRC2, BIRC3 and XIAP compared to the non-transfected cells (p<10-4). Conclusion: cFLIP shRNA seems to induce apoptosis in the thymus carcinoma cell line. Simultaneously antiapoptotic proteins (AIPs) BIRC2, BIRC3 and XIAP were up regulated in order to protect the cell from apoptosis. Could these AIPs provide the way to escape the cell death? AIPs Selective inhibitions could represent a promising therapeutic approach for malignant thymic carcinomas. Objective: Nucleolin is a multifunctional DNA-, RNA-and protein-binding protein, involved in fundamental aspects of transcription, cell proliferation and growth. It is located in the nuclei/nucleolus, cytoplasm and on the cell surface. The present study aimed at optimizing the histological identification of nucleolin. Method: Mamary invasive ductal carcinoma 3 μm paraffin sections were pretreatead with pronase at room temperature (5-10 min) to epitope exposure. Biotinilated peptide against nucleolin was applied (1/1.5 mM dilutions), incubated at room temperature for 30 min/overnight at 4°C; after phosphate-buffered saline, peptide binding was identified by peroxidase-conjugated streptavidin and 3,3-diaminobenzidine tetrahydrochloride applied according to manufacturer's instructions before haematoxylin counterstaining. Results: Pretreatment for 5 min at 1.5 mM of biotinilated peptide showed only nuclear expression, as 1 mM/10 min pretreatment with overnight peptide incubation; positive cytoplasmic expression was obtained also after 30 min incubation/room temperature. At 1.5 mM concentration for 10 min epitope retrieval, cytoplasmic and nuclear positivity raised over 75 % expression, independently of peptide exposure (overnight/room temperature).