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Maria Fiammetta Romano

Prof. Maria Fiammetta Romano

Università FEDERICO II di Napoli

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I am an MD, specialist in Oncology and Immunology, and I serve as a professor of Human Biochemistry at the School of Medicine, Federico II University of Naples, Italy. My research contributed to the biochemical and molecular characterization of the signal transduction pathways that are altered in cancer and responsible for resistance to conventional therapies, with particular regard to the NF-kappaB transcription factors. In the last decade, my research has provided significant contributions to the elucidation of the role of FK506 binding proteins (FKBP) in cancer. FKBP51 serves as a scaffold and isomerase in IKK kinase complex assembly. Its inhibition hampers the activation of NF-kappa-B transcription factors and increases sensitivity to chemo and radiotherapy in melanoma and leukemia. FKBP51 is abundantly expressed in melanoma and supports tumor growth, invasion, autophagy, and resistance to apoptosis. Its expression is correlated with the aggressiveness and metastatic potential of the tumor. FKBP51 is particularly abundant in melanoma-cancer stem cells. The cross-talk between melanoma and immune cells generates a spliced FKBP51 isoform that acts as a PD-L1 cochaperone and is associated with immune evasion. FKBP51s plays a role in M2 macrophage polarization and marks CD163 macrophages of glioblastoma patients.

Research Keywords & Expertise

Apoptosis
PBMC
PD-L1
NF-kB signaling pathwa...
Macrophage biomarkers

Fingerprints

7%
Apoptosis
5%
PBMC
5%
PD-L1

Short Biography

I am an MD, specialist in Oncology and Immunology, and I serve as a professor of Human Biochemistry at the School of Medicine, Federico II University of Naples, Italy. My research contributed to the biochemical and molecular characterization of the signal transduction pathways that are altered in cancer and responsible for resistance to conventional therapies, with particular regard to the NF-kappaB transcription factors. In the last decade, my research has provided significant contributions to the elucidation of the role of FK506 binding proteins (FKBP) in cancer. FKBP51 serves as a scaffold and isomerase in IKK kinase complex assembly. Its inhibition hampers the activation of NF-kappa-B transcription factors and increases sensitivity to chemo and radiotherapy in melanoma and leukemia. FKBP51 is abundantly expressed in melanoma and supports tumor growth, invasion, autophagy, and resistance to apoptosis. Its expression is correlated with the aggressiveness and metastatic potential of the tumor. FKBP51 is particularly abundant in melanoma-cancer stem cells. The cross-talk between melanoma and immune cells generates a spliced FKBP51 isoform that acts as a PD-L1 cochaperone and is associated with immune evasion. FKBP51s plays a role in M2 macrophage polarization and marks CD163 macrophages of glioblastoma patients.