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Prof. Anastasia De Luca
University of Rome "Tor Vergata", Department of Biology, Via della Ricerca Scientifica 1, 00133 Rome, Italy
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Academic Career Length
20Years (2007-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications4 May 2009 in Angewandte Chemie International Edition
Journal Article
WAWee Han Ang
Wee Han AngLPLorien J. Parker
Lorien J. Parker
ALAnastasia De Luca
Anastasia De LucaLJLucienne Juillerat‐Jeanneret
Lucienne Juillerat‐Jeanneret
CMCraig Morton
Craig MortonPDPaul Dyson
Paul Dyson +2
29 November 2007 in ChemMedChem
Journal Article
WAWee Han Ang
Wee Han AngALAnastasia De Luca
Anastasia De LucaCCCatherine Chapuis‐Bernasconi
Catherine Chapuis‐Bernasconi
LJLucienne Juillerat‐Jeanneret
Lucienne Juillerat‐Jeanneret
MBMario Lo Bello
Mario Lo BelloPDPaul Dyson
Paul Dyson9 October 2009 in Biochemistry
Journal Article
RFRaffaele Fabrini
Raffaele Fabrini
ALAnastasia De Luca
Anastasia De Luca
Lorenzo StellaGMGiampiero Mei
Giampiero Mei
BOBarbara Orioni
Barbara Orioni
Giorgio Ricci +3
20 June 2019 in Proceedings of the National Academy of Sciences
Journal Article
ALAnastasia De Luca
Anastasia De LucaLPLorien J. Parker
Lorien J. Parker
WAWee Han Ang
Wee Han Ang
Carlo RodolfoVGValentina Gabbarini
Valentina GabbariniPDPaul Dyson
Paul Dyson +7
Cisplatin [ cis- diamminedichloroplatinum(II) ( cis -DDP)] is one of the most successful anticancer agents effective against a wide range of solid tumors. However, its use is restricted by side effects and/or by intrinsic or acquired drug resistance. Here, we probed the role of glutathione transferase (GST) P1-1, an antiapoptotic protein often overexpressed in drug-resistant tumors, as a cis -DDP–binding protein. Our results show that cis -DDP is not a substrate for the glutathione (GSH) transferase activity of GST P1-1. Instead, GST P1-1 sequesters and inactivates cisplatin with the aid of 2 solvent-accessible cysteines, resulting in protein subunits cross-linking, while maintaining its GSH-conjugation activity. Furthermore, it is well known that GST P1-1 binding to the c-Jun N-terminal kinase (JNK) inhibits JNK phosphorylation, which is required for downstream apoptosis signaling. Thus, in turn, GST P1-1 overexpression and Pt-induced subunit cross-linking could modulate JNK apoptotic signaling, further confirming the role of GST P1-1 as an antiapoptotic protein.
14 November 2011 in Biochemical Journal
Journal Article
ALAnastasia De Luca
Anastasia De LucaNMNoemi Moroni
Noemi Moroni
ASAnnalucia Serafino
Annalucia SerafinoAPAlessandra Primavera
Alessandra Primavera
PAPastore Anna
Pastore AnnaMBMario Lo Bello
Mario Lo Bello +7
Acquired drug resistance was found to be suppressed in the doxorubicin-resistant breast cancer cell line MCF7/Dx after pre-treatment with GSNO (nitrosoglutathione). The effect was accompanied by enhanced protein glutathionylation and accumulation of doxorubicin in the nucleus. Among the glutathionylated proteins, we identified three members of the histone family; this is, to our knowledge, the first time that histone glutathionylation has been reported. Formation of the potential NO donor dinitrosyl–diglutathionyl–iron complex, bound to GSTP1-1 (glutathione transferase P1-1), was observed in both MCF7/Dx cells and drug-sensitive MCF7 cells to a similar extent. In contrast, histone glutathionylation was found to be markedly increased in the resistant MCF7/Dx cells, which also showed a 14-fold higher amount of GSTP1-1 and increased glutathione concentration compared with MCF7 cells. These results suggest that the increased cytotoxic effect of combined doxorubicin and GSNO treatment involves the glutathionylation of histones through a mechanism that requires high glutathione levels and increased expression of GSTP1-1. Owing to the critical role of histones in the regulation of gene expression, the implication of this finding may go beyond the phenomenon of doxorubicin resistance.
1 September 2019 in Journal of Trace Elements in Medicine and Biology
Journal Article
ALAnastasia De Luca
Anastasia De LucaABAnna Barile
Anna BarileMAMario Arciello
Mario ArcielloLRLUISA ROSSI
LUISA ROSSIAbout Me
Name: Anastasia De Luca.
Place and Date of Birth: Rome, 24. August 1982.
EDUCATION:
November 2009: Ph.D. in Cellular Molecular Biology at the University of Rome Tor Vergata.
September 2006: Master's degree cum Laude in Medical Biotechnology at the University of Rome Tor Vergata.
July 2004: Bachelor's degree cum Laude in Medical Biotechnology at the University of Rome Tor Vergata.
July 2001: Senior high school degree, Immanuel Kant, Rome.
EXPERIENCE:
April 2008–July 2008: Fellowship at the Ecole Polytechnique Federale de Lausanne.
November 2009–December 2010: Fellowship at the Istituto Dermopatico dell’Immacolata (Rome) in Experimental Immunology.
January 2011–May 2016: Fellowship in Biochemistry (Univ. of Rome Tor Vergata).
June 2016–June 2018: Fellowship in Cell Biology Lab (Univ of Rome Tor Vergata).
December 2018–November 2021: Fellowship in Botany/Clinical Biochemistry (Univ of Rome Tor Vergata).
December 2021–Today: Assistant Professor in Clinical Biochemistry (Department of Biology, Univ. of Rome Tor Vergata).
AWARDS:
July 2007: "Raeli Foundation" for the Best Graduates.
2015, 2017, and 2021: Umberto Veronesi Fellowships.
Research projects:
GSTP1-1 in the reversal of drug resistance in breast cancer cell lines.
The interaction between GSTP1-1, JNK, and TRAF2 (on the in vitro recombinant proteins or cell lines).
The role of FMRP in tumorigenesis.
The copper-dependent modulation of cancer metastatization.