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CO-LOCALIZATION OF MUTANT P53 AND AMYLOID-LIKE PROTEIN AGGREGATES IN BREAST TUMORS
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Abstract
P53 isoneof themost important tumor suppressorproteins inhumancancers.Mutations in theTP53gene
are common features of malignant tumors and normally correlate to a more aggressive disease. In breast
cancer, these gene alterations are present in approximately 20% of cases and are characteristically of
missense type. In the present work we describeTP53mutations in breast cancer biopsies and investigate
whether wild and mutant p53 participate in protein aggregates formation in these breast cancer cases.
We analyzed 88 biopsies from patients residing in the metropolitan area of Rio de Janeiro, andperformed
TP53mutation screening using direct sequencing of exons 5–10. Seventeen mutations were detected, 12
of them were of missense type, 2 nonsenses, 2 deletions and 1 insertion. The presence ofTP53mutation
was highly statistically associated to tumor aggressiveness of IDC cases, indicatedhere by ElstonGrade III
(p<0.0001). Paraffin embedded breast cancer tissues were analyzed for the presence of p53 aggregates
through immunofluorescenceco-localizationassay, usinganti-aggregateprimaryantibodyA11, andanti-p53. Our results show that mutant p53 co-localizes with amyloid-like protein aggregates, depending on
mutation type, suggesting that mutant p53 may form aggregates in breast cancer cells,in vivo.
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