Lello Zolla

Tuscia University, Viterbo, Latium, Italy

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Publications (253)797.34 Total impact

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    Clinical biochemistry 10/2015; DOI:10.1016/j.clinbiochem.2015.10.004 · 2.28 Impact Factor
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    ABSTRACT: Neurological disorders can be associated with protein glycosylation abnormalities. Rett syndrome is a devastating genetic brain disorder, mainly caused by de novo loss-of-function mutations in the methyl-CpG binding protein 2 (MECP2) gene. Although its pathogenesis appears to be closely associated with a redox imbalance, no information on glycosylation is available. Glycoprotein detection strategies (i.e., lectin-blotting) were applied to identify target glycosylation changes in the whole brain of Mecp2 mutant murine models of the disease. Remarkable glycosylation pattern changes for a peculiar 50kDa protein i.e., the N-linked brain nucleotide pyrophosphatase-5 were evidenced, with decreased N-glycosylation in the presymptomatic and symptomatic mutant mice. Glycosylation changes were rescued by selected brain Mecp2 reactivation. Our findings indicate that there is a causal link between the amount of Mecp2 and the N-glycosylation of NPP-5.
    Neuroscience Research 10/2015; DOI:10.1016/j.neures.2015.10.002 · 1.94 Impact Factor
  • Alessandro Lana · Lello Zolla ·
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    ABSTRACT: Background: Meat derives from muscle, but they are extremely different. The slaughtered muscle undergoes a number of biological changes during the maturation period, which is pivotal for the transformations that permit to obtain the final marketable product. Scope and approach: In this review a general process driving muscle-to-meat conversion is described, despite all the factors that can affect and diversify every individual process. We focus our attention on the switch from the normal, aerobic metabolism to the post-slaughter, anaerobic one, underlining all the consequences in terms of muscle reactions driving and influencing the transformation. The massive production of ROS is the pivotal event of the muscle-to-meat conversion, and muscle cells are stimulated to react as to cope with the oxidative stress. Despite the mobilization of defensive machineries, it soon becomes overwhelming and unsustainable: muscle cells are forced to die. Key findings and conclusions: ROS can induce both autophagy and apoptosis. Their role in muscle conversion is not completely clear, despite their differences have large influence on meat maturation and final product. A deeper understanding is pivotal on this argument as to better manage meat production.
    Trends in Food Science & Technology 10/2015; 46(2). DOI:10.1016/j.tifs.2015.10.001 · 4.65 Impact Factor
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    ABSTRACT: Short p63 isoform, ΔNp63, is crucial for epidermis formation, and it plays a pivotal role in controlling the turnover of basal keratinocytes by regulating the expression of a subset of genes involved in cell cycle and cell adhesion programs. The glycolytic enzyme hexokinase 2 (HK2) represents the first step of glucose utilization in cells. The family of HKs has four isoforms that differ mainly in their tissue and subcellular distribution. The preferential mitochondrial localization of HK2 at voltage-dependent anion channels provides access to ATP generated by oxidative phosphorylation and generates an ADP/ATP recycling mechanism to maintain high respiration rates and low electron leak. Here, we report that ΔNp63 depletion in human keratinocytes impairs mitochondrial basal respiration and increases mitochondrial membrane polarization and intracellular reactive oxygen species. We show ΔNp63-dependent regulation of HK2 expression, and we use ChIP, validated by p63-Chip sequencing genomewide profiling analysis, and luciferase assays to demonstrate the presence of one p63-specific responsive element within the 15th intronic region of the HK2 gene, providing evidence of a direct interaction. Our data support the notion of ΔNp63 as a master regulator in epithelial cells of a combined subset of molecular mechanisms, including cellular energy metabolism and respiration. The ΔNp63-HK2 axis is also present in epithelial cancer cells, suggesting that ΔNp63 could participate in cancer metabolic reprogramming.
    Proceedings of the National Academy of Sciences 09/2015; 112(37). DOI:10.1073/pnas.1508871112 · 9.67 Impact Factor
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    ABSTRACT: Caspase proteases are responsible for the regulated disassembly of the cell into apoptotic bodies during mammalian apoptosis. Structural homologues of the caspase family (called metacaspases) are involved in programmed cell death in single-cell eukaryotes, yet the molecular mechanisms that contribute to death are currently undefined. Recent evidence revealed that a programmed cell death process is induced by acetic acid (AA-PCD) in Saccharomyces cerevisiae both in the presence and absence of metacaspase encoding gene YCA1. Here, we report an unexpected role for the yeast metacaspase in protein quality and metabolite control. By using an "omics" approach, we focused our attention on proteins and metabolites differentially modulated en route to AA-PCD either in wild type or YCA1-lacking cells. Quantitative proteomic and metabolomic analyses of wild type and Δyca1 cells identified significant alterations in carbohydrate catabolism, lipid metabolism, proteolysis and stress-response, highlighting the main roles of metacaspase in AA-PCD. Finally, deletion of YCA1 led to AA-PCD pathway through the activation of ceramides, whereas in the presence of the gene yeast cells underwent an AA-PCD pathway characterized by the shift of the main glycolytic pathway to the pentose phosphate pathway and a proteolytic mechanism to cope with oxidative stress. The yeast metacaspase regulates both proteolytic activities through the ubiquitin-proteasome system and ceramide metabolism as revealed by proteome and metabolome profiling of YCA1-knock-out cells during acetic-acid induced programmed cell death. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Proteomics 08/2015; DOI:10.1016/j.jprot.2015.08.003 · 3.89 Impact Factor
  • Mohsen Janmohammadi · Lello Zolla · Sara Rinalducci ·
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    ABSTRACT: Low temperature (LT) is one of several important environmental stresses influencing plant performance and distribution. Adaptation to LT is a highly dynamic stress-response phenomenon and involves complex cross-talk between different regulatory levels. Although plants differ in their sensitivity to LT, in temperate species low nonfreezing temperatures cause noticeable alterations in various biochemical and physiological processes that can potentially improve freezing tolerance. This adaptation is associated with changes in the expression pattern of genes and their protein products. Proteins are the major players in most cellular events and are directly involved in plant LT responses, thereby proteome analysis could help uncover additional novel proteins associated with LT tolerance. Proteomics is recommended as an appropriate strategy for complementing transcriptome level changes and characterizing translational and post-translational regulations. In this review, we considered alterations in the expression and accumulation of proteins in response to LT stress in the three major cereal crops produced worldwide (wheat, barley, and rice). LT stress down-regulates many photosynthesis-related proteins. On the contrary, pathways/protein sets that are up-regulated by LT include carbohydrate metabolism (ATP formation), ROS scavenging, redox adjustment, cell wall remodelling, cytoskeletal rearrangements, cryoprotection, defence/detoxification. These modifications are common adaptation reactions also observed in the plant model Arabidopsis, thus representing key potential biomarkers and critical intervention points for improving LT tolerance of crop plants in cold regions with short summers. We believe that an assessment of the proteome within a broad time frame and during the different phenological stages may disclose the molecular mechanisms related to the developmental regulation of LT tolerance and facilitate the progress of genetically engineered stress-resistant plant varieties. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Phytochemistry 06/2015; 117:76-89. DOI:10.1016/j.phytochem.2015.06.003 · 2.55 Impact Factor
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    ABSTRACT: Meat derives from a muscle that undergoes a great number of biochemical and physiological changes. The anoxic condition established from the moment of animal sacrifice forces muscle cells to a sort of reaction, resulting in methodical programmed cell death to avoid necrosis. The duality autophagy and/or apoptosis is at the centre of the scientific debate about the biological processes driving the muscle to meat conversion. Here we report an omic time course overview carried on proteome, phosphoproteome and metabolome of Piedmontese Longissimus thoracis muscle searching for clues helping us to extricate through the dilemma. The survey depicts a progressive physiological impairing and our evidences push towards the apoptotic behavior: proteomic time course trend of annexin A2, RKIP, HSPB6, αB crystalline, adenylate kinase, DJ-1, 31 kDa actin fragment; the 0-1 days increased phosphorylation of myosin 2 and synaptopodin; the metabolomic time course trend of key metabolic indicators, like GSH/GSSG ratio, taurine and nitrotyrosine. The employed techniques provide strong indications about the likely apoptotic behavior of aging meat in muscle-to-meat conversion process. Our work underlines compelling evidences of the apoptotic behavior of Piedmontese beef muscle cells undergoing the muscle-to-meat process, whereas no autophagic clues are inferred from this omic investigation. Copyright © 2015. Published by Elsevier B.V.
    Journal of proteomics 05/2015; 125. DOI:10.1016/j.jprot.2015.04.023 · 3.89 Impact Factor
  • Sara Rinalducci · Lello Zolla ·
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    ABSTRACT: The mechanisms responsible for the reduced lifespan of transfused red blood cells (RBCs) and platelets (PLTs) are still under investigation, however one explanation refers to the detrimental biochemical changes occurring during ex vivo storage of these blood products. A myriad of historical and more recent studies has contributed to advance our understanding of storage lesion. Without any doubts, proteomics had great impact on transfusion medicine by profiling the storage-dependent changes in the total detectable protein pool of both RBCs and PLTs. This review article focuses on the role of oxidative/nitrosative stress in developing RBC and PLT storage lesions, with a special glance at its biochemistry and cross-talk with phosphorylative signal transduction. In this sense, we enlighten the potential contribution of new branches of proteomics in identifying novel points of intervention for the improvement of blood product quality. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Transfusion and Apheresis Science 04/2015; 52(3). DOI:10.1016/j.transci.2015.04.005 · 0.77 Impact Factor
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    ABSTRACT: Piedmontese meat tenderness becomes higher by extending the ageing period after slaughter up to 44 days. Classical physical analysis only partially explain this evidence, so in order to discover the reason of the potential beneficial effects of prolonged ageing, we performed omic analysis in the Longissimus thoracis muscle by examining main biochemical changes through mass spectrometry-based metabolomics and proteomics. We observed a progressive decline in myofibrillar structural integrity (underpinning meat tenderness) and impaired energy metabolism. Markers of autophagic responses (e.g. serine and glutathione metabolism) and nitrogen metabolism (urea cycle intermediates) accumulated until the end of the assayed period. Key metabolites such as glutamate, a mediator of the appreciated umami taste of the meat, were found to constantly accumulate until day 44. Finally, statistical analyses revealed that glutamate, serine and arginine could serve as good predictors of ultimate meat quality parameters, even though further studies are mandatory.
    Food Chemistry 04/2015; 172(731):741. DOI:10.1016/j.foodchem.2014.09.146 · 3.39 Impact Factor
  • Valeria Pallotta · Sara Rinalducci · Lello Zolla ·
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    ABSTRACT: BACKGROUND Refrigerated storage of red blood cell (RBC) units promotes the progressive accumulation of the so-called storage lesions, a widespread series of alterations to morphology, metabolism, and proteome integrity of stored RBCs. However, while storage lesions targeting the RBC membrane fraction have been widely documented, the cytosolic fraction is as yet an underinvestigated cause of the technical inconveniences related to the high abundance of hemoglobin.STUDY DESIGN AND METHODS By exploiting a recently ideated preparative two-dimensional clear native electrophoresis, followed by mass spectrometry analysis, we could monitor the changes of soluble multiprotein complexes (MPCs) in RBCs after 0, 21, and 35 days of storage under standard blood banking conditions.RESULTSData indicate a substantial storage-dependent alteration of RBC MPCs, particularly of those involved in energy and redox metabolism, confirming previous evidence about the progressive dysregulation of these pathways in long-stored units.CONCLUSION The use of native gel–based proteomics to investigate MPCs present in the RBC cytosolic fraction proved to be a powerful tool. Results collected represent a preliminary advance in the knowledge of the key role of native cytosolic MPCs in context of RBC storage lesion. Multiprotein organization and interacting partners of some key enzymes have been found to change during storage duration, suggesting that future studies will be needed to assess whether such alterations could influence their activity and efficiency.
    Transfusion 03/2015; 55(8). DOI:10.1111/trf.13079 · 3.23 Impact Factor
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    ABSTRACT: The yeast Saccharomyces cerevisiae expresses one member of metacaspase Cys protease family, encoded by YCA1 gene. Combination of proteomics and metabolomics data showed YCA1 deletion down-regulated glycolysis, TCA cycle and alcoholic fermentation as compared with WT cells. Δyca1 cells also showed a down-regulation of the pentose phosphate pathway and an accumulation of pyruvate, correlated with higher levels of certain amino acids found in these cells. Accordingly, there is a decrease in protein biosynthesis, and up-regulation of specific stress response protein like Ahp1p, which possibly provides these cells with a better protection against stress. Moreover, in agreement with the down-regulation of protein biosynthesis machinery in Δyca1 cells, we have found that regulation of transcription, co-translational protein folding and protein targeting to different subcellular locations were also down-regulated. Metabolomics analysis of the nucleotide content showed a significant reduction in Δyca1 cells in comparison with the WT, except for GTP content which remained unchanged. Thus, our combined proteome/metabolome approach added a new dimension to the non-apoptotic function of yeast metacaspase, which can specifically affect cell metabolism through as yet unknown mechanisms and possibly stress-response pathways, like HOG and cell wall integrity pathways. Certainly, YCA1 deletion may induce compensatory changes in stress response proteins offering a better protection against apoptosis to Δyca1 cells rather than a loss in a pro-apoptotic YCA1-associated activity.
    Molecular BioSystems 02/2015; 11(6). DOI:10.1039/C4MB00660G · 3.21 Impact Factor
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    ABSTRACT: One of the hallmarks of blood bank stored red blood cells (RBCs) is the irreversible transition from a discoid to a spherocyte-like morphology withmembrane perturbation and cytoskeleton disorders. Therefore, identification of the storage-associated modifications in the protein–protein interactions between the cytoskeleton and the lipid bilayer may contribute to enlighten the molecular mechanisms involved in the alterations ofmechanical properties of stored RBCs. Here we report the results obtained analyzing RBCs after 0, 21 and 35 days of storage under standard blood banking conditions by label free mass spectrometry (MS)-based experiments. We could quantitatively measure changes in the phosphorylation level of crucial phosphopeptides belonging to β-spectrin, ankyrin-1, α-adducin, dematin, glycophorin A and glycophorin C proteins. Data have been validated by both western blotting and pseudo-Multiple Reaction Monitoring (MRM). Although each phosphopeptide showed a distinctive trend, a sharp increase in the phosphorylation level during the storage duration was observed. Phosphopeptide mapping and structural modeling analysis indicated that the phosphorylated residues localize in protein functional domains fundamental for the maintenance of membrane structural integrity. Along with previous morphological evidence acquired by electron microscopy, our results seem to indicate that 21-day storage may represent a key point for the molecular processes leading to the erythrocyte deformability reduction observed during blood storage. These findings could therefore be helpful in understanding and preventing the morphology-linked mechanisms responsible for the post-transfusion survival of preserved RBCs.
    Journal of Mass Spectrometry 02/2015; 50(2):326-335. DOI:10.1002/jms.3531 · 2.38 Impact Factor
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    ABSTRACT: In the present study, we performed an integrated proteomics (2DE) and metabolomics (HPLC-MS) investigation to determine the molecular mechanisms underlying cadmium (Cd) tolerance in the halophyte Cakile maritima. Recent physiological reports have documented how C. maritima could accumulate high doses of Cd in roots and shoots, while appearing to be naturally equipped to cope with it, since mild or heavy Cd stress did not alter physiological parameters, including mineral uptake, pigment contents, other than transpiration, water use efficiency and variation of net CO2 assimilation. In the present study, metabolomics and proteomics results highlighted the Cd-dependent up-regulation of thiol compound anabolism, including glutathione and phytochelatin homeostasis, especially in response to elevated Cd stress (100 µM), which allows an intracellular chelation of Cd and its compartmentalization into vacuole. Altered energy metabolism at the triose phosphate level was accompanied by altered accumulation of Calvin cycle intermediates and photorespiration byproducts at high (100 µM), albeit not at mild (25 µM), CdCl2 stress, suggesting that elevated doses of Cd might promote photorespiration. Metabolomics results confirmed proteomics and previous physiological evidence, also suggesting that osmoprotectants betaine and proline, together with plant hormones methyl jasmonate and salicylic acid might be involved in mediating responses to Cd-induced stress. Taken together, from the present study we conclude that C. maritima might represent an ideal candidate for phytoremediation interventions in Cd-contaminated soils.
    Molecular BioSystems 01/2015; 11(4). DOI:10.1039/C4MB00567H · 3.21 Impact Factor
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    ABSTRACT: Nibrin (also named NBN or NBS1) is a component of the MRE11/RAD50/NBN complex, which is involved in early steps of DNA double strand breaks sensing and repair. Mutations within the NBN gene are responsible for the Nijmegen breakage syndrome (NBS). The 90% of NBS patients are homozygous for the 657del5 mutation, which determines the synthesis of two truncated proteins of 26 kDa (p26) and 70 kDa (p70). Here, HEK293 cells have been exploited to transiently express either the full-length NBN protein or the p26 or p70 fragments, followed by affinity chromatography enrichment of the eluates. The application of an unsupervised proteomics approach, based upon SDS-PAGE separation and shotgun digestion of protein bands followed by MS/MS protein identification, indicates the occurrence of previously unreported protein interacting partners of the full-length NBN protein and the p26 fragment containing the FHA/BRCT1 domains, especially after cell irradiation. In particular, results obtained shed light on new possible roles of NBN and of the p26 fragment in ROS scavenging, in the DNA damage response, and in protein folding and degradation. In particular, here we show that p26 interacts with PARP1 after irradiation, and this interaction exerts an inhibitory effect on PARP1 activity as measured by NAD+ levels. Furthermore, the p26-PARP1 interaction seems to be responsible for the persistence of ROS, and in turn of DSBs, at 24 h from IR. Since some of the newly identified interactors of the p26 and p70 fragments have not been found to interact with the full-length NBN, these interactions may somehow contribute to the key biological phenomena underpinning NBS.
    PLoS ONE 12/2014; 9(12):e114651. DOI:10.1371/journal.pone.0114651 · 3.23 Impact Factor
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    ABSTRACT: Nelumbo nucifera (Gaertn.) or lotus, is an aquatic plant native to India, and presently consumed as food mainly in China and Japan. Lotus is also widely used in Indian and Chinese traditional medicine. Extracts from different parts of the lotus plant have been reported to show diverse biological activities – antioxidant, free radical scavenging, anti-inflammatory and immunomodulatory. Despite this, little work has been done in isolating and identifying proteins responsible for these activities, or yet importantly to establish a lotus proteome. The aim of our group is to develop a proteome catalogue of the lotus plant, starting with its seed, the nutrient rich food source. In this present study, the seed endosperm – most abundant and nutrient storage tissue – was targeted for protein extraction by testing five different extraction protocols, followed by their proteomic analyses using complementary 1DE and 2DE approaches in conjunction with tandem mass spectrometry. The inventory of 66 non-redundant proteins obtained by 1DE-MS and the 30 obtained by 2DE-MS provides the first catalogue of the lotus seed endosperm, where the most abundant protein functions were in categories of metabolic activities related to carbohydrate metabolism and nutrient storage.This article is protected by copyright. All rights reserved
    Proteomics 12/2014; 15(10). DOI:10.1002/pmic.201400406 · 3.81 Impact Factor
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    ABSTRACT: Heat-shock protein (Hsp)10 is the co-chaperone for Hsp60 inside mitochondria, but it also resides outside the organelle. Variations in its levels and intracellular distribution have been documented in pathological conditions, e.g. cancer and chronic obstructive pulmonary disease (COPD). Here, we show that Hsp10 in COPD undergoes changes at the molecular and subcellular levels in bronchial cells from human specimens and derived cell lines, intact or subjected to stress induced by cigarette smoke extract (CSE). Noteworthy findings are: (i) Hsp10 occurred in nuclei of epithelial and lamina propria cells of bronchial mucosa from non-smokers and smokers; (ii) human bronchial epithelial (16HBE) and lung fibroblast (HFL-1) cells, in vitro, showed Hsp10 in the nucleus, before and after CSE exposure; (iii) CSE stimulation did not increase the levels of Hsp10 but did elicit qualitative changes as indicated by molecular weight and isoelectric point shifts; and (iv) Hsp10 nuclear levels increased after CSE stimulation in HFL-1, indicating cytosol to nucleus migration, and although Hsp10 did not bind DNA, it bound a DNA-associated protein.
    Open Biology 10/2014; 4(10). DOI:10.1098/rsob.140125 · 5.78 Impact Factor
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    Dataset: LIPIDOMICS

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    ABSTRACT: In this work we evaluated Cd-phytoextraction ability of the halophyte Cakile maritima comparatively to the glycophyte Brassica juncea commonly recommended for phytoextraction. Seedlings were grown in nutrient solution added with 0–100 ␮M Cd for 21 days. Cd impaired growth in B. juncea but had no sig-nificant impact on C. maritima. The halophyte C. maritima maintained also higher photosynthetic activity than the glycophyte B. juncea. Cd decreased leaf chlorophyll (Chl) and carotenoids concentrations as well as PSII efficiency (F v /F m , F v /F 0 an PSII) in B. juncea while it increased intercellular CO 2 concentration in this species. Shoot Cd content was higher in the halophyte C. maritima reaching 1365 ␮g g −1 dw at 100 ␮M while it was 548 ␮g g −1 dw in B. juncea at the same dose. The translocation factor (TF) was higher for C. maritima than for B. juncea at all external Cd doses. It is concluded that the halophyte C. maritima could be considered as a promising plant material for Cd-phytoextraction.
    Ecological Engineering 10/2014; 71:623-627. DOI:10.1016/j.ecoleng.2014.08.013 · 2.58 Impact Factor
  • Sara Rinalducci · Cristina Marrocco · Lello Zolla ·
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    ABSTRACT: Background Red blood cell (RBC) glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme normally inhibited upon binding to the membrane-spanning protein Band 3, but active when free in the cytosol. Accumulating evidence in other cells indicates that oxidative thiol modifications in cytosolic GAPDH drive this molecule into functional avenues that deviate from glycolysis. This study aimed to investigate the role of GAPDH in oxidative stress–dependent metabolic modulations occurring in SAGM-stored RBCs, to increase the knowledge of the molecular mechanisms affecting RBC survival and viability under blood banking conditions.Study Design and Methods Membranes and cytosol from CPD SAGM-stored RBCs were subjected to Western blotting with anti-GAPDH at 0, 7, 14, 21, 28, 35, and 42 days of preservation. Immunoreactive bands were excised, digested with trypsin, and analyzed by mass spectrometry for the presence of oxidative posttranslational modifications. GAPDH enzymatic activity was also measured in the cytosolic fraction during storage.ResultsAt 21 days of storage, we demonstrated that cytosolic GAPDH undergoes temporary inactivation due to the formation of an intramolecular disulfide bond between the active-site Cys-152 and nearby Cys-156, a mechanism to rerouting glucose flux toward the pentose phosphate pathway. In addition, an increase in the membrane-bound GAPDH was detected in long-stored RBCs.Conclusion Reversible inhibition or activation of cytosolic GAPDH may represent a protective strategy against oxidative stress to favor NADPH production in stored RBCs.
    Transfusion 10/2014; 55(3). DOI:10.1111/trf.12855 · 3.23 Impact Factor
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    ABSTRACT: The "New discipline for blood transfusion activities and national production of blood derivatives" (Italian Parliament, October 21st, 2005) brought about a significant update of all regulatory aspects concerning transfusion medicine activities in Italy, including the establishment of a nationally co-ordinated blood system consistent with the autonomy of regional authorities1. The aim was to identify homogeneous standards of quality and safety nationwide1. In this setting, the newly born Italian National Blood Centre was to be responsible for all technical and scientific aspects related to transfusion medicine issues, including (i) blood and blood product self-sufficiency; (ii) blood quality and safety; (iii) appropriate utilisation of blood resources; (iv) accreditation and funding of transfusion medicine activities; (v) a national blood information system; (vi) technology nnnassessment; (vii) external quality assessment; (viii) a national haemovigilance network; (ix) control of medical products deriving from human plasma; (x) inspections and controls of the plasma-derivative industry; (xi) education and scientific research in transfusion medicine, and (xii) promotion of voluntary, non-remunerated, responsible and periodic blood donation1.
    Blood transfusion = Trasfusione del sangue 09/2014; 13(1). DOI:10.2450/2014.0053-14 · 2.37 Impact Factor

Publication Stats

4k Citations
797.34 Total Impact Points


  • 1994-2015
    • Tuscia University
      • Department of Biological and Ecological Sciences DEB
      Viterbo, Latium, Italy
  • 2009
    • Universität des Saarlandes
      • Fachbereich Chemie
      Saarbrücken, Saarland, Germany
  • 1977-2009
    • The American University of Rome
      Roma, Latium, Italy
    • Università degli Studi del Sannio
      Benevento, Campania, Italy
  • 2004
    • Viterbo University
      Largo, Florida, United States
  • 1990-1993
    • University of Camerino
      • Dipartimento di Scienze Chimiche
      Camerino, The Marches, Italy
  • 1985-1986
    • Sapienza University of Rome
      • Department of Biochemical Sciences "Alessandro Rossi Fanelli
      Roma, Latium, Italy
  • 1984
    • University of Rome Tor Vergata
      • Dipartimento di Biologia
      Roma, Latium, Italy
  • 1983
    • Roche Institute of Molecular Biology
      Nutley, New Jersey, United States
  • 1981
    • The American Society for Biochemistry and Molecular Biology
      RMG, Georgia, United States