FRAXE-associated mental retardation protein (FMR2) is an RNA-binding protein with high affinity for G-quartet RNA forming structure. Promotion of cell proliferation by the proto-oncogene DEK enhances oral squamous cell carcinogenesis through field cancerization. Nakashima, T., Tomita, H., Hirata, A., Ishida, K., Hisamatsu, K., Hatano, Y. DEK promotes HPV-positive and -negative head and neck cancer cell proliferation. Future directions and treatment strategies for head and neck squamous cell carcinomas. Wise-Draper, T.M., Draper, D.J., Gutkind, J.S., Molinolo, A.A., Wikenheiser-Brokamp, K.A., Wells, S.I. Role of the DEK oncogene in the development of squamous cell carcinoma. Ishida, K., Nakashima, T., Shibata, T., Hara, A., Tomita, H. The Complexity of DEK Signaling in Cancer Progression. Control of tumorigenesis and chemoresistance by the DEK oncogene. The DEK protein-an abundant and ubiquitous constituent of mammalian chromatin. Waldmann, T., Scholten, I., Kappes, F., Hu, H.G., Knippers, R. DEK-AFF2 Carcinoma of the Sinonasal Region and Skull Base: Detailed Clinicopathologic Characterization of a Distinctive Entity. Rooper LM, Agaimy A, Dickson BC, Dueber JC, Eberhart CG, Gagan J, et al. DEK-AFF2 fusion-associated papillary squamous cell carcinoma of the sinonasal tract: clinicopathologic characterization of seven cases with deceptively bland morphology. Kuo, Y.J., Lewis, J.S., Jr, Zhai C., Chen, Y.A., Chernock, R.D., Hsieh, M.S. Nonkeratinizing Squamous Cell Carcinoma of the Sinonasal Tract With DEK-AFF2: Further Solidifying an Emerging Entity. Middle ear and temporal bone nonkeratinizing squamous cell carcinomas with DEK-AFF2 fusion: an emerging entity. Todorovic, E., Truong, T., Eskander, A., Lin, V., Swanson, D., Dickson, B.C. Immunogenic neoantigens derived from gene fusions stimulate T cell responses. Yang, W., Lee, K.W., Srivastava, R.M., Kuo, F., Krishna, C., Chowell, D. Accordingly, AFF2 IHC is a highly sensitive and specific ancillary marker that distinguishes DEK-AFF2 carcinoma from the other sinonasal tumors with overlapping morphological features and may be an especially useful alternative for decalcified specimens. The nuclear expression of AFF2 IHC showed 100% sensitivity and specificity for DEK::AFF2 carcinoma. All DEK FISH-negative sinonasal tumors were negative for nuclear AFF2 expression. It was thus considered a failure of the IHC rather than a truly negative case and was excluded from the statistical analysis. The one case that was negative for AFF2 IHC in the tumor cells also lacked expression in the internal positive control. Sixteen of the 17 DEK::AFF2 carcinomas showed nuclear AFF2 expression in ā„30% of tumor cells, including one decalcified case that failed FISH and RT-PCR confirmation. Seventeen DEK::AFF2 carcinomas, including 11 cases with predominantly low-grade morphology and one showing glandular differentiation, as well as 78 DEK FISH-negative sinonasal tumors were evaluated by AFF2 immunohistochemistry (IHC). We then optimized an immunohistochemical assay with an anti-AFF2 C-terminus antibody for ancillary diagnosis. The gene expression of AFF2 was significantly higher in the fusion-positive cases compared to the wild-type tumors ( pā<ā0.001), while DEK was not. We first analyzed publicly available RNA sequencing data of sinonasal tumors from the national center for biotechnology information (NCBI) sequence read archive and identified 3 DEK::AFF2 carcinomas out of 28 sinonasal tumors. This current study aimed to validate an immunohistochemical assay for AFF2 C-terminus as an ancillary marker. The confirmation of this gene fusion has thus far relied solely on next-generation sequencing, fluorescence in situ hybridization (FISH), or reverse transcription polymerase chain reaction (RT-PCR). The tumor is typically characterized by papillary proliferation of non-keratinizing squamous epithelial cells with monotonous cytologic features, which may mimic other sinonasal tumors. DEK::AFF2 carcinoma of the sinonasal tract is an emerging entity.
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