De Lima Araujo L.H.,Brazilian National Cancer Institute INCA CPQ |
Pinto L.W.,Institute Pesquisa Clinica Evandro Chagas |
Schluckebier L.F.,Brazilian National Cancer Institute INCA CPQ |
De Moraes J.L.,Brazilian National Cancer Institute INCA CPQ |
And 4 more authors.
Medical Oncology | Year: 2012
Some proteins, canonically not associated with amyloid diseases, can aggregate into amyloid-like fibrils under special conditions. Our group hypothesized that stressful cancer microenvironment might induce the formation of insoluble deposits of p53 mutant protein. A cohort of 28 non-small cell lung cancer (NSCLC) patients was used to test the aforementioned hypothesis. Tumor specimens were assessed for TP53 mutations using DNA sequencing and for amyloid formation by Congo red staining. TP53 mutations were present in 57% of patients, whereas no amyloid deposits were detected in tissue sections under polarized light microscopy. Mutant p53 proteins are not associated with the appearance of amyloid-like fibrils in NSCLC samples, and DNA sequencing remains the standard method to detect such abnormality. © Springer Science+Business Media, LLC 2011. Source