Pietro Pucci

Professor of Biochemistry

Name Pietro
Surname Pucci
Institution Università degli Studi della Campania Luigi Vanvitelli
Telephone +39 081 674 318 (UniNa)
Telephone 2 +39 081 373 7896 (Ceinge)
E-Mail pucci@unina.it
Address Department of Chemical Sciences, Federico II University, Via Cintia 6, 80126, Naples, Italy
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Pietro Pucci


  • Retraction: The microRNA 15a/16-1 cluster down-regulates protein repair isoaspartyl methyltransferase in hepatoma cells: Implications for apoptosis regulation.

    Publication Date: 24/05/2019 on The Journal of biological chemistry
    by Sambri I, Capasso R, Pucci P, Perna AF, Ingrosso D
    DOI: 10.1074/jbc.RX119.009146
  • Evolution of an insect immune barrier through horizontal gene transfer mediated by a parasitic wasp.

    Publication Date: 05/03/2019 on PLoS genetics
    by Di Lelio I, Illiano A, Astarita F, Gianfranceschi L, Horner D, Varricchio P, Amoresano A, Pucci P, Pennacchio F, Caccia S
    DOI: 10.1371/journal.pgen.1007998

    Genome sequencing data have recently demonstrated that eukaryote evolution has been remarkably influenced by the acquisition of a large number of genes by horizontal gene transfer (HGT) across different kingdoms. However, in depth-studies on the physiological traits conferred by these accidental DNA acquisitions are largely lacking. Here we elucidate the functional role of Sl gasmin, a gene of a symbiotic virus of a parasitic wasp that has been transferred to an ancestor of the moth species Spodoptera littoralis and domesticated. This gene is highly expressed in circulating immune cells (haemocytes) of larval stages, where its transcription is rapidly boosted by injection of microorganisms into the body cavity. RNAi silencing of Sl gasmin generated a phenotype characterized by a precocious suppression of phagocytic activity by haemocytes, which was rescued when these immune cells were incubated in plasma samples of control larvae, containing high levels of the encoded protein. Proteomic analysis demonstrated that the protein Sl gasmin is released by haemocytes into the haemolymph, where it opsonizes the invading bacteria to promote their phagocytosis, both in vitro and in vivo. Our results show that important physiological traits do not necessarily originate from evolution of pre-existing genes, but can be acquired by HGT events, through unique pathways of symbiotic evolution. These findings indicate that insects can paradoxically acquire selective advantages with the help of their natural enemies.

  • A signalling cascade involving receptor-activated phospholipase A<sub>2</sub>, glycerophosphoinositol 4-phosphate, Shp1 and Src in the activation of cell motility.

    Publication Date: 01/03/2019 on Cell communication and signaling : CCS
    by Varone A, Mariggiò S, Patheja M, Maione V, Varriale A, Vessichelli M, Spano D, Formiggini F, Lo Monte M, Brancati N, Frucci M, Del Vecchio P, D'Auria S, Flagiello A, Iannuzzi C, Luini A, Pucci P, Banci L, Valente C, Corda D
    DOI: 10.1186/s12964-019-0329-3

    Shp1, a tyrosine-phosphatase-1 containing the Src-homology 2 (SH2) domain, is involved in inflammatory and immune reactions, where it regulates diverse signalling pathways, usually by limiting cell responses through dephosphorylation of target molecules. Moreover, Shp1 regulates actin dynamics. One Shp1 target is Src, which controls many cellular functions including actin dynamics. Src has been previously shown to be activated by a signalling cascade initiated by the cytosolic-phospholipase A (cPLA) metabolite glycerophosphoinositol 4-phosphate (GroPIns4P), which enhances actin polymerisation and motility. While the signalling cascade downstream Src has been fully defined, the mechanism by which GroPIns4P activates Src remains unknown.

  • The complex CBX7-PRMT1 has a critical role in regulating E-cadherin gene expression and cell migration.

    Publication Date: 28/02/2019 on Biochimica et biophysica acta. Gene regulatory mechanisms
    by Federico A, Sepe R, Cozzolino F, Piccolo C, Iannone C, Iacobucci I, Pucci P, Monti M, Fusco A
    DOI: 10.1016/j.bbagrm.2019.02.006

    The Chromobox protein homolog 7 (CBX7) belongs to the Polycomb Group (PcG) family, and, as part of the Polycomb repressive complex (PRC1), contributes to maintain transcriptional gene repression. Loss of CBX7 expression has been reported in several human malignant neoplasias, where it often correlates with an advanced cancer state and poor survival, proposing CBX7 as a candidate tumor-suppressor gene in cancer progression. Indeed, CBX7 is able to positively or negatively regulate the expression of genes involved in cell proliferation and cancer progression, such as E-cadherin, cyclin E, osteopontin, EGR1. To understand the molecular mechanisms that underlie the involvement of CBX7 in cancer progression, we designed a functional proteomic experiment based on CHIP-MS to identify novel CBX7 protein partners. Among the identified CBX7-interacting proteins we focused our attention on the Protein Arginine Methyltransferase 1 (PRMT1) whose critical role in epithelial-mesenchymal transition (EMT), cancer cell migration and invasion has been already reported. We confirmed the interaction between CBX7 and PRMT1 and demonstrated that this interaction is crucial for PRMT1 enzymatic activity both in vitro and in vivo and for the regulation of E-cadherin expression, an important hallmark of EMT. These results suggest a general mechanism by which CBX7 interacting with histone modification enzymes like HDAC2 and PRMT1 enhances E-cadherin expression. Therefore, disruption of this equilibrium may induce impairment of E-cadherin expression and increased cell migration eventually leading to EMT and, then, cancer progression.

  • Lanthionine and Other Relevant Sulfur Amino Acid Metabolites: Detection of Prospective Uremic Toxins in Serum by Multiple Reaction Monitoring Tandem Mass Spectrometry.

    Publication Date: 01/01/2019 on Methods in molecular biology (Clifton, N.J.)
    by Perna AF, Pane F, Sepe N, Fontanarosa C, Pinto G, Zacchia M, Trepiccione F, Anishchenko E, Ingrosso D, Pucci P, Amoresano A
    DOI: 10.1007/978-1-4939-9528-8_2

    In the context of the vascular effects of hydrogen sulfide (HS), it is known that this gaseous endogenous biological modulator of inflammation, oxidative stress, etc. is a potent vasodilator. Chronic renal failure, a common disease affecting the aging population, is characterized by low levels of HS in plasma and tissues, which could mediate their typical hypertensive pattern, along with other abnormalities. Lanthionine and homolanthionine, natural non-proteinogenic amino acids, are formed as side products of HS production. Also in consideration of the intrinsic difficulties in HS measuring, these compounds have been proposed as reliable and stable markers of HS synthesis. However, in the setting of chronic renal failure patients on hemodialysis, they represent typical retention products (without ruling out the possibility of an increased intestinal synthesis) and prospective novel uremic toxins. Here, a method utilizing liquid chromatography-electrospray tandem mass spectrometry (LC-MS/MS) in multiple reaction monitoring ion mode has been developed and evaluated for the determination of these key HS metabolites in plasma, by using a triple quadrupole mass spectrometer.

  • TRIM8-driven transcriptomic profile of neural stem cells identified glioma-related nodal genes and pathways.

    Publication Date: 05/12/2018 on Biochimica et biophysica acta. General subjects
    by Venuto S, Castellana S, Monti M, Appolloni I, Fusilli C, Fusco C, Pucci P, Malatesta P, Mazza T, Merla G, Micale L
    DOI: 10.1016/j.bbagen.2018.12.001

    We recently reported TRIM8, encoding an E3 ubiquitin ligase, as a gene aberrantly expressed in glioblastoma whose expression suppresses cell growth and induces a significant reduction of clonogenic potential in glioblastoma cell lines.

  • Genome-wide mapping of 8-oxo-7,8-dihydro-2'-deoxyguanosine reveals accumulation of oxidatively-generated damage at DNA replication origins within transcribed long genes of mammalian cells.

    Publication Date: 20/11/2018 on Nucleic acids research
    by Amente S, Di Palo G, Scala G, Castrignanò T, Gorini F, Cocozza S, Moresano A, Pucci P, Ma B, Stepanov I, Lania L, Pelicci PG, Dellino GI, Majello B
    DOI: 10.1093/nar/gky1152

    8-Oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG) is one of the major DNA modifications and a potent pre-mutagenic lesion prone to mispair with 2'-deoxyadenosine (dA). Several thousand residues of 8-oxodG are constitutively generated in the genome of mammalian cells, but their genomic distribution has not yet been fully characterized. Here, by using OxiDIP-Seq, a highly sensitive methodology that uses immuno-precipitation with efficient anti-8-oxodG antibodies combined with high-throughput sequencing, we report the genome-wide distribution of 8-oxodG in human non-tumorigenic epithelial breast cells (MCF10A), and mouse embryonic fibroblasts (MEFs). OxiDIP-Seq revealed sites of 8-oxodG accumulation overlapping with γH2AX ChIP-Seq signals within the gene body of transcribed long genes, particularly at the DNA replication origins contained therein. We propose that the presence of persistent single-stranded DNA, as a consequence of transcription-replication clashes at these sites, determines local vulnerability to DNA oxidation and/or its slow repair. This oxidatively-generated damage, likely in combination with other kinds of lesion, might contribute to the formation of DNA double strand breaks and activation of DNA damage response.

  • The extreme hyper-reactivity of Cys94 in lysozyme avoids its amorphous aggregation.

    Publication Date: 30/10/2018 on Scientific reports
    by Bocedi A, Cattani G, Martelli C, Cozzolino F, Castagnola M, Pucci P, Ricci G
    DOI: 10.1038/s41598-018-34439-y

    Many proteins provided with disulfide bridges in the native state undergo amorphous irreversible aggregation when these bonds are not formed. Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent. In fact, when the reduced protein assembles into a molten globule state, its cysteines acquire strong hyper-reactivity towards natural disulfides. The most reactive residue, Cys94, reacts with oxidized glutathione (GSSG) 3000 times faster than an unperturbed protein cysteine. A low pK of its sulfhydryl group (6.6/7.1) and a productive complex with GSSG (K = 0.3 mM), causes a fast glutathionylation of this residue (t = 3 s) and a complete inhibition of the protein aggregation. Other six cysteines display 70 times higher reactivity toward GSSG. The discovery of extreme hyper-reactivity in cysteines only devoted to structural roles opens new research fields for Alzheimer's and Parkinson diseases.

  • A hypothesis of sudden body fluid vaporization in the 79 AD victims of Vesuvius.

    Publication Date: 26/09/2018 on PloS one
    by Petrone P, Pucci P, Vergara A, Amoresano A, Birolo L, Pane F, Sirano F, Niola M, Buccelli C, Graziano V
    DOI: 10.1371/journal.pone.0203210

    In AD 79 the town of Herculaneum was suddenly hit and overwhelmed by volcanic ash-avalanches that killed all its remaining residents, as also occurred in Pompeii and other settlements as far as 20 kilometers from Vesuvius. New investigations on the victims' skeletons unearthed from the ash deposit filling 12 waterfront chambers have now revealed widespread preservation of atypical red and black mineral residues encrusting the bones, which also impregnate the ash filling the intracranial cavity and the ash-bed encasing the skeletons. Here we show the unique detection of large amounts of iron and iron oxides from such residues, as revealed by inductively coupled plasma mass spectrometry and Raman microspectroscopy, thought to be the final products of heme iron upon thermal decomposition. The extraordinarily rare preservation of significant putative evidence of hemoprotein thermal degradation from the eruption victims strongly suggests the rapid vaporization of body fluids and soft tissues of people at death due to exposure to extreme heat.

  • Multiple Reaction Monitoring Tandem Mass Spectrometry Approach for the Identification of Biological Fluids at Crime Scene Investigations.

    Publication Date: 01/05/2018 on Analytical chemistry
    by Illiano A, Arpino V, Pinto G, Berti A, Verdoliva V, Peluso G, Pucci P, Amoresano A
    DOI: 10.1021/acs.analchem.7b04742

    Knowledge of the nature of biofluids at a crime scene is just as important as DNA test to link the nature of the biofluid, the criminal act, and the dynamics of the crime. Identification of methods currently used for each biological fluid (blood, semen, saliva, urine) suffer from several limitations including instability of assayed biomolecules, and low selectivity and specificity; as an example of the latter issue, it is not possible to discriminate between alpha-amylase 1 (present in saliva) and alpha-amylase 2 (present in semen and vaginal secretion. In this context, the aim of the work has been to provide a predictive protein signature characteristic of each biofluid by the recognition of specific peptides unique for each protein in a single analysis. A panel of four protein biomarkers for blood, four for saliva, five for semen, and two for urine has been monitored has been monitored by using a single multiple reaction monitoring (MRM)-based method targeting concomitantly 46 different peptides. Then, The optimized method allows four biological matrices to be identified when present on their own or in 50:50 mixture with another biofluid. Finally, a valid strategy combining both DNA analysis and liquid chromatographic-tandem mass spectrometric multiple reaction monitoring (LC-MS-MRM) identification of biofluids on the same sample has been demonstrated to be particularly effective in forensic investigation of real trace evidence collected at a crime scene.