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Ricerca

Programma di Ricerca Fondazione Enrico Puccinelli

Vari programmi di ricerca si stanno svolgendo nell’ambito della Fondazione, ma attualmente l’attenzione è concentrata sulla presenza di un complesso contenente DNA e presente nel sangue circolante.

L’attuale programma intende stabilire la struttura di questo complesso, la sua formazione, come viene secreto dalle cellule e se può essere un sistema di comunicazione tra cellula e cellula penetrando nelle cellule vicine ed esprimendosi.

Questo studio ha due importanti applicazioni pratiche:

  1. Nella diagnostica prenatale
  2. Nel monitoraggio dei tumori.

Dopo la seconda settimana di gravidanza nel sangue materno si trova anche il complesso derivato dall’embrione ed è possibile diagnosticare alterazioni cromosomiche quali il mongolismo e malattie genetiche come la talassemia evitando l’amniocentesi.

Nei tumori si osservano variazioni quantitative e qualitative di questo DNA che tendono a scomparire dopo l’asportazione del tumore e se la chemioterapia ha successo, mentre riappaiono in caso di micro metastasi difficilmente rilevabili con le tecniche attuali o di insuccesso della chemioterapia.

Questa ricerca è attualmente finanziata con una donazione ricevuta dalla Fondazione

Titolo

Components of the cytosolic and released virtosomes from stimulated and non-stimulated human lymphocytes

Nome degli Autori

Samuela Cataldi and Mariapia Viola-Magni

Abstract

 http://www.sciencedirect.com/science/article/pii/S2405580816300449

Volume 6, July 2016, Pages 236–241

  • a Department of Pharmaceutical Science, University of Perugia, Perugia, Italy
  • b Fondazione Puccinelli, Italy
 Received 8 February 2016, Revised 7 April 2016, Accepted 13 April 2016, Available online 16 April 2016
doi:10.1016/j.bbrep.2016.04.006

Highlights

•Virtosomes are particles formed in the cytoplasm and released in the medium.
•Released virtosomes are transferred in other cells modifying their function.
•Virtosomes contain DNA, RNA, protein and lipids.
•The lipids composition is characterized by high level of sphingomyelin and low level of cholesterol.
•Virtosomes does not present a cell membrane.

Abstract

Abstract aim

This work intends to analyse the structure and the composition of virtosomes and their role.

Background

Virtosomes are newly synthesized DNA-RNA-lipoprotein complexes released from living cells in a regulated and energy-dependent manner.

Methods

Virtosome fractions were isolated by ultracentrifugation from human lymphocytes cytoplasm and from culture medium before and after stimulation with phitoemoagglutinin (PHA). The composition in DNA, RNA, protein and lipids was determined. The virtosomes present in the culture medium were put in contact with lymphocytes.

Results

Virtosome fractions released from non-stimulated lymphocytes are shown to reduce replication of stimulated lymphocytes and those from stimulated lymphocytes to increase multiplication of non-stimulated lymphocytes. Biochemical analyses of the virtosomal complexes have shown that those from stimulated lymphocytes have five proteins that are absent from non-stimulated virtosome fractions. A comparison of the cytosolic versus released virtosome fractions from non-stimulated lymphocytes indicated that there is a greater percentage of phospholipids in the released virtosomes with a corresponding decrease in the percentage of protein.

Conclusion

Although there is a presence of cholesterol in the virtosomes, the low levels of phosphatidylcholine and cholesterol, together with the low ratios of cholesterol: phospholipids leads to a confirmation of the apparent lack of a limiting membrane around the virtosomes.

General significance

Virtosomes are structural particles formed in the cytoplasm, released from the cells and capable to be transferred in other cells influencing their behaviour.

Graphical abstract

Abbreviations

  • PHA, phytohaemaglutinin;
  • PLs, phospholipids;
  • CHO, cholesterol;
  • PS, phosphatidylserine;
  • PI, phosphatidylinositol;
  • PC, phosphayidylcholine;
  • PE, phosphatidyiletanolamine;
  • SM, sphyngomyelin

Keywords

  • Virtosomes composition;
  • Lymphocytes proliferation;
  • Virtosome lipids

1. Introduction

A number of early investigators demonstrated that both stimulated and non-stimulated lymphocytes released DNA [1], [2], [3], [4], [5], [6], [7], [8] and [9]. Subsequently, Stroun and Anker showed the released DNA to be newly synthesized with 3H-thymidine labeling studies [3]. Furthermore, the DNA was associated with RNA [10]. Since both nucleic acids were resistant to nuclease activity, it was considered that they were protected by lipoprotein. The presence of protein was identified when RNAse activity affected RNA only after a prior treatment with either pronase or proteinase k [2] while that of lipids was identified from the complex's low density during upward sucrose density gradient centrifugation, freezing and thawing and the incorporation of radioactive phospholipid precursors [2]. Subsequent studies using radioactive precursors permitted the demonstration that the RNA, protein and associated phospholipids were (a) newly synthesized and (b) synthesized at about the same time. Similar results were obtained with other cell types [11] and [12]. This DNA/RNA-lipoprotein complex has an estimated size of ~5×105 Da [3] although the complex released from stimulated rat lymphocytes had a higher density than that released from non-stimulated rat lymphocytes [1]. The complex, termed a virtosome [13] is released in an apparently energy-dependent step [2], only from living cells [2] and [3] in a controlled manner [3]. Experiments employing radioactive precursors have shown that the DNA, RNA, phospholipid and proteins appear in the cytoplasm at about 3 h after commencing labeling and that the complex is released from cells 3–6 h later, depending on which cells were studied i.e. human, other mammalian, avian, amphibian and plant cells [1], [3], [12], [14], [15] and [16]. The complex does not appear to have a limiting membrane as shown by studies on the uptake and release of virtosomes between chick embryo fibroblasts [17] and on release from J774 cells and their uptake by non-stimulated lymphocytes [18]. Importantly, virtosomes released from one cell type can enter a different cell type resulting in a biological modification of the recipient cells e.g. transformation of NIH 3T3 cells on uptake of released mutant k-ras from SW480 cells [19], an allogenic T–B lymphocyte co-operation involving lymphocyte subsets from human donors with different allotypes [20] and [21] and DNA synthesis initiation in non-stimulated lymphocytes on uptake of virtosomes released by J774 and P497 tumour cells [18]. Thus, the virtosome appears to be a novel cytoplasmic component that may act as an inter-cellular messenger.

However, the full structure of the complex has not been ascertained. In the present study, experiments were designed (a) to identify the lipids and proteins associated with both the cytosolic and released complexes, (b) the comparative amounts of proteins, lipids, DNA and RNA in cytosolic and released virtosomes and (c) the nature of the proteins present in the released virtosomes from stimulated lymphocytes as opposed to those absent in non-stimulated lymphocytes. However, as a first step to ensure that the virtosomes released from stimulated and non-stimulated lymphocytes were biologically active, the released virtosomes were fractionated and tested for their biological activity, using a modification of the previously described method [17] and [18].

In addition to obtaining the overall content of DNA, RNA and phospholipids, the analysis of the individual phospholipids gave further confirmation for the absence of a classical membrane limiting the virtosome.

2. Material and methods

2.1. Lymphocyte separation

The lymphocytes were obtained from buffy coats kindly donated by the Immunotransfusion Laboratory (Ospedale Santa Maria della Misericordia, Perugia).

Blood samples were stratified on Ficoll-Plaque and centrifuged at 1600 rpm for 30 min The lymphocyte layer was collected and the cells resuspended in saline and sedimented by centrifugation at 1600 rpm for 30 min This treatment was repeated twice and the cells were counted using a Burker chamber. Dead cells (1.0–1.5%) were identified by trypan blue staining.

2.2. Lymphocyte experiments

2.2.1. Growth of lymphocytes

This was evaluated by seeding the isolated lymphocytes in RPMI medium in 50 ml flasks, either with or without PHA, at a concentration of 100,000 ml−1. In some experiments, the lymphocytes were incubated in RPMI medium either with or without serum +PHA. Cell proliferation was estimated by cell counts every 24 h for 96 h.

After incubation for 96 h, the lymphocytes were recuperated by centrifugation at 600 g for 10 min, washed twice with RPMI medium in order to eliminate any serum and PHA after which they were ready for use in subsequent experimental procedures.

 

2.2.2. Released and cytosolic virtosome isolation

~350,000,000 lymphocytes were place in RPMI for 3 h and incubated at 37 °C for 3 h prior to centrifugation at 600 g for 10 min to sediment the cells. Cell death (<1.5%) was monitored by trypan blue.

The supernatant so obtained was further centrifuged at 10,000 g for 10 min to remove organelles and cell debris. The supernatant was further centrifuged at 120,000 g for 1 h to sediment any remaining debris. The virtosomes will have remained in the supernatant. The cells and the final supernatants were saved for the analysis of the virtosomes that remain in the supernatant.

The supernatant to be used for the analysis of DNA, RNA and protein (350–390 ml) was lyophilized. The powder obtained was resuspended in distilled water and dialysed overnight at 3–4 °C against diluted PBS to decrease the saline concentration.

Cytosolic virtosomes were isolated by gently homogenizing the cells in PBS (10 strokes with a plastic pestle) [18]. The suspension was treated as described (above) for the released virtosomes. The supernatant so obtained was lyophilized and dialysed as described above.

2.2.3. Analysis of the cytosolic and released virtosomes

Protein was determined with the colorimetric method Folin [22] using albumin as a standard. The DNA was determined by the method of diphenilamine (Burton [23], using DNA (the highly polymerized calf-thymus DNA-preparation-Sigma) at scalar quantities for quantification. The RNA was measured using the orcinolo method, Ribonucleic acid type IV from calf-liver-(from Sigma for quantitative evaluation) at scalar quantities for quantification [24].

Total lipids were extracted by the method of Folch et al. [25] and their concentration determined by measuring the amount of inorganic phosphorus using Fiske and Subbarow method [26].

2.2.4. Chromatographic separation and quantification of phospholipids

The supernatant was placed directly upon thin layer chromatography plates (Merk) and the phospholipids separated using chloroform: methanol: ammonia (65:25:4 v/v) and the spots identified with iodine.

The individual phospholipids were scraped from the plates, collected and the amount of inorganic phosphorus present was determined [26]. The single phospholipids were identified using a standard phospholipid solution as reference [27].

2.2.5. Cholesterol determination

After total lipid extraction, chromatographic plate separation of cholesterol was made using a solution of ethyl ether: petroleum ether: acetic acid (50:50:1 v/v) and cholesterol was identified using cholesterol as a standard reference. After removal from the chromatographic plate, the cholesterol amount was determined with 0.05% o-phtaldeyde in acetic and sulphuric acids [28].

2.2.6. Protein analysis

Proteins present in the culture medium supernatants derived from cultures of both stimulated and non-stimulated cells were concentrated by ultra-filtration with AMICON CENTRIKON, Millipore that excludes proteins of <5000 Da. The protein concentration was determined by the method of Bradford [29]. One hundred µg of the protein concentrate for each sample were analysed by bi-dimensional electrophoresis using a GE HEALTHCARE apparatus.

In bi-dimensional electrophoresis the first run is based on IEF, the pH range is 3–10, the direction is vertical from anode (+) to cathode (-), the second run is an SDS-Page, from cathode to anode is the direction and discriminates on the basis of molecular weight (the higher on top and the lower on back).

Each spot was analysed with a SPECTROMETER ESI TRAP, LCQ Deca XP plus THERMO ELECTRON and a MASCOT SEARCH system (Fig. 1).

The bands indicated with the letters are present in both samples, whereas that indicated with numbers are present only in stimulated lymphocytes.

Mono-dimensional electrophoresis was performed with a BIO RAD apparatus.

using 50 µg protein per lane for each sample. Spots were analysed by SPECTROMETER ESI TRAP, LCQ Deca XP plus THERMO ELECTRON and a MASCOT SEARCH. Only the bands indicated in with the numbers 1–5 in Fig. 2 were so analysed.

3. Results

3.1. Lymphocyte cultures

3.1.1. Stimulated v non-stimulated lymphocytes

As expected, the number of lymphocytes increased more rapidly after PHA stimulation rising from 100,000 ml−1 to ~1000,000 ml−1 by 96 h whilst non-

stimulated cells augmented by only ~680,000 cells ml−1 (Fig. 3).

3.1.2. Effect of virtosomes released from stimulated lymphocytes on non-stimulated lymphocytes

Whilst non-stimulated lymphocyte numbers increased from 100,000 ml−1 to 668,000 ml−1 cells, those cultured in the presence of the virtosome fraction from stimulated lymphocytes increased from 100,000 ml−1 to 821,000 ml−1 (Fig. 4).

 

3.1.3. Effect of virtosomes released from non-stimulated lymphocytes on stimulated lymphocytes

Little difference was observed between the cell number increase between non-stimulated lymphocytes and stimulated lymphocytes in the presence of virtosomes released from non-stimulated lymphocytes (Fig. 5).

3.2. Analysis of non-stimulated lymphocyte cytosolic and released virtosomal fractions

3.2.1. General analysis

The percentages of DNA, RNA, protein and phospholipids present in the two fractions are given in Table 1 and Table 2 (Table 3 and Table 4).

Table 1.

Composition of Virtosomes isolated from the supernatant.

Supernatant%γ/mg proteins
Proteins 27.44±4.20  
DNA 3.92±1.85 139±33
RNA 36.41±2.31 1345±204
PLs 32.21±3.69 1196±223

The same analysis was made on the virtosomes isolated from the cytoplasm (Table 2).

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Table 2.

Composition of Virtosomes isolated from the cytoplasm.

Cytoplasm%γ/mg proteins
Proteins 41.01%±1.91  
DNA 3.45%±0.39 95±10
RNA 35.09%±4.40 859±142
PLs 19.90%±2.16 484±42
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Table 3.

Comparison of the values calculated per mg of proteins.

 CytoplasmSupernatant
DNA 95±10 139±33
RNA 859±142 1345±204
PLs 484±42 1196±223

Comparison of the percentage values shows no significant differences in the

DNA and RNA content from the two fractions (Table 3 and Table 4). An increase in PLs is observed in the released fraction.

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Table 4.

Comparison of the percentage of virtosome composition.

 CytoplasmSupernatant
Proteins 41.01% 27.91%
DNA 3.45% 3.92%
RNA 35.09% 36.41%
PLs 19.90% 32.21%

However, the protein concentration is diminished and the phospholipid percentage increased in the released fraction.

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3.3. Phospholipids and cholesterol

There is an increase in both the SM and PS contents of the released fraction compared with the cytosolic fraction. The PC and PE percentages remain relatively unchanged whereas PI increases. Of interest is the similarity of the PC levels that are less than would be expected to be present in a standard membrane (Table 5 and Table 6) [30]Table 7.

 
Table 5.

PLs composition of virtosomes isolated from the supernatant.

 average%µg PLs values of 2 experiments
PS 14.78% PS: 0.15 µg → 14.56%PS: 0.15 µg → 15.0%
PI 16.25% PI: 0.16 µg → 16.0% PI: 0.17 µg → 16.50%
SM 27.57% SM: 0.27 µg → 27.0% SM: 0.29 µg → 28.15%
PC 20.69% PC: 0.21 µg → 21.0% PC: 0.21 µg → 20.38%
PE 20.69% PE: 0.21 µg → 21.0% PE: 0.21 µg → 20.38%

The same analysis, performed on virtosomes isolated from the cytoplasm, confirm the increase of SM and PI. The results of two experiments are very similar (Table 6).

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Table 6.

PLs composition of virtosomes from the cytoplasm.

 Average%µg PLs values of 2 experiments
PS 12.5% PS: 0.15 µg → 14.42% PS: 0.09 µg → 10.58%
PI 23.11% PI: 0.20 µg → 19.23% PI: 0.23 µg → 27%
SM 19.23% SM: 0.18 µg → 17.30% SM: 0.18 µg → 21.17%
PC 22.58% PC: 0.25 µg → 24.0% PC: 0.18 µg → 21.17%
PE 22.5% PE: 0.26 µg → 25.0% PE: 0.17 µg → 20.0%

CHO was present but at a level, which when referred to the PLs levels, is very low. In the released fraction, the ratio of CHO: PLs is 0.29 whilst that for the cytosolic fraction is 0.19This results is confirmed by the ratio CHO/SM which is very different with respect to membrane and is more similar to the values find in the chromatin (Table 7).

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Table 7.

Values of CHO in relation to PLs and SM.

 SupernatantCytoplasm
CHO /PLs 0.29 0.19
CHO/SM 1.08 1.02
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3.4. Protein levels and composition

The difference in percentage of protein composition between cytosolic fraction and supernatant is mainly due to an increase in PLs than a real decrease in protein (Table 4) which concentration/ml remains practically constant.

The bi-dimensional electrophoretic separation of the proteins shows a large number of proteins of >5000 Da to be present in both released and cytosolic fractions (Fig. 1(a), (b)). These include human RAI1-retinoic acid-induced protein present in the non-stimulated lymphocyte fraction (spot 1 of Fig. 1(a)) and human NFRKB-nuclear factor related to kappa-B-binding protein present in the stimulated lymphocyte fraction (spot f of Fig. 1(b)).

The mono-dimensional electrophoretic gels (Fig. 2) also show a large number of proteins present in both the non-stimulated and stimulated lymphocyte fractions. Six human proteins, present in the fraction from stimulated lymphocytes, but absent from the non-stimulated lymphocyte fraction, include CHM2A-charged multi-vesicular body protein 2a (line 3), CLMP-CXADR-like membrane protein (line5), ZFAN4-AN1-type zinc finger protein 4 (line 4), ZN160-zinc finger protein 160 (line5), DYHC1-cytoplasmic dynein 1 heavy chain 1( Line 4) and PNPH-purine nucleoside phosphorylase (Line4).

Human proteins present in both non-stimulated and stimulated lymphocyte fractions include ACTB-cytoplasmic 1 actin (Line1), ACTA-aortic smooth muscle actin (line2), POTEE-POTE Ankyrin domain family member E (line2), POTEF-POTE Ankyrin domain family member F(line2), FETUA-alpha-2-HS-glycoprotein and UBE4B-ubiquitin conjugation factor E4B(line5).

4. Discussion

The incubation of non-stimulated lymphocytes in the culture medium containing virtosomes from stimulated lymphocytes resulted in an increase in their level of multiplication (Fig. 4). No effect was seen when the stimulated lymphocytes were incubated in the culture medium from non-stimulated lymphocytes (Fig. 5). This response was in agreement with the data from earlier experiments [18] when DNA synthesis was increased in non-stimulated lymphocytes by virtosome preparations from tumour cells while DNA synthesis was inhibited by the virtosome preparations from non-stimulated lymphocytes and hepatocytes.

Hence, it was of interest to analyse the virtosome fractions from non-stimulated and stimulated lymphocyte populations to determine their composition and to note any differences. Similarly, a comparison of cytosolic and released virtosome fractions would indicate any differences between them. In addition, it would help to determine whether or not a standard limiting membrane was present since earlier studies had indicated that there was no such membrane [16] and [18].

Earlier workers had demonstrated that the virtosomes form in the cytosol and are released into the external medium after formation [13]. Hence, a biochemical analysis was performed on the cytosolic and released virtosome fractions from non-stimulated lymphocytes. The major differences concern the percentage increase in PLs contents with a lower percentage of proteins in the supernatant virtosomes (Table 4). Nevertheless, there is little difference between the percentage contents of the single PLs, the major change being an increase of 8% in the SM content and a decrease in PI with minor change of PC and PE. If compare the percentages of single PLs with that present in the nuclear membrane, chromatin and nuclear matrix [30] it is clear that they do not correspond to any of these structures especially for the large amount of SM and the low percentage of PC. This specific aspect excludes the possibility that the material analysed in the supernatant may be derived from membranes nuclear matrix or chromatin of dead cells.

This conclusion is also confirmed by the similarity with the PLs found in the cytoplasm, thus in agreement with the hypothesis that virtosomes are formed inside of the cells and thereafter excluded. The high percentage of SM is similar to that found in the chromatin and may have a possible role in transcription by protecting RNA from degradation. Previous experiments have demonstrated that chromatin SM protects RNA from RNase digestion [31].

The presence of CHO confirms the previous difference with values very low with respect to membranes. The only affinity is the value of CHO/SM which is similar to that found in the chromatin. The role of CHO is crucial for membrane biogenesis, but also for trafficking and signalling and is indispensable for cell migration and invasion. In this case it may have a role in favouring the invasion of cells by the virtosomes [32] and [33].

Earlier studies [16] and [18] have indicated that the virtosomes do not appear to have a standard limiting membrane. This is reinforced by the low amount of PC (Table 5 and Table 6). Furthermore, the ratios of CHO: PLs are too low for the presence of a standard membrane. In the released fraction, the ratio is 0.29 whilst that for the cytosolic fraction is 0.19. This compares with a ratio of almost 1.0 for standard membranes. The comparison of the values expressed in percentages show a decrease of proteins in the released virtosomes with respect to that isolated from the cytoplasm with an increase in percentage of PLs. The protein decrease implies that they are formed inside the cells and released thereafter.

In order to confirm this supposition and to explain the difference of the effect of virtosomes from stimulated lymphocytes and that from nonstimulated on the lymphocytes, we have analysed the proteins of the supernatant.

Only the lanes which indicate possible differences were analysed. Bi- and uni-dimensional gel electrophoresis of the proteins showed a large number of proteins of >5000 Da to be present in the fractions measured (Fig. 1 and Fig. 2).

A small number of the proteins have been identified including five proteins present in the stimulated lymphocyte released virtosome fraction that are absent from the supernatant of the control.

Bidimensional electrophoresis showed the presence of NF-kB (nuclear factor related to kappa B–binding protein) which is involved in transcriptional regulation, DNA replication and probably DNA repair [34].

Monodimensional electrophoresis has permitted the identification of many proteins. Some of which are common to both stimulated and non-stimulated cells and some that are specific to one or other of the two groups of lymphocytes. Actin and Ankyrin are common and perhaps may function to anchor of structure.

 

Concerning the proteins present only on virtosomes released from stimulated lymphocytes, the most important are, the ZNF160 zinc finger protein 160 involved in transcriptional regulation [35], the DYHC1 dynein, cytoplasmic 1, heavy chain 1 potential transmembrane proteins that may play a role in either the transport between the endoplasmic reticulum and the Golgi complex or organization of the Golgi in cells. The dynein-dynactin complex is necessary for protein transport, positioning of cell compartments, mobility of structures within the cell and many other cell processes [36]. The PNPH purine nucleoside phosphorylase has a central role in purine metabolism [37].

In conclusion, on the basis of these results, we can exclude the possibility that the isolated particles are due to dead cell fragments, since they have specific characters which correspond to those found in the cytoplasm and so confirm earlier findings that the complexes are not released by dead cells [15]. The composition change in relation to function such that the virtosomes are capable of influencing other cells.

Aknowledgements

We wish to thank the ISVET financial support as donation to Fondazione “Enrico Puccinelli” ONLUS and Prof. Peter Brian Gahan for the suggestion in developing this research and for revising the manuscript.

Appendix A. Supplementary materials

Supplementary data

Supplementary data

 

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14.            Biagetti M., Serenelli G., Loukopoulou Z., Tognellini T., Viola Magni M.P., ''Incorporazione di Bromodeossiuridina in cellule di Friend indotte a differenziarsi''. Il Ruolo della Biologia nella Diagnostica del 2000, 359-365, 1995.

 

15.            Serenelli G. (in coll. con Frascarelli M., Loukopoulou Z, Viola Magni M.P., Tognellini R.: ''PCNA/Cyclin Expression in Differentiated Human Erythroleukemic Cells''., Europ. J. Histochem,. 39/3, 54, 1995.

 

16.              Serenelli G. (in coll. con Frascarelli M., Tognellini R., Viola-Magni M.P.): ''Effetti della Cloramina T sulla Proliferazione e Differenziazione di Cellule Eritroleucemiche di Friend (FLC)''. Atti VIII Congresso Internazionale ECBA, Isola Capo Rizzuto (Kr), 28 settembre-1 ottobre, 78, 1995.

 

17.            Serenelli G., Loukopoulou Z., Frascarelli M., Tognellini R.: ''Citomorfometria di Cellule di Friend coltivate in liquido di coltura di grani di Kefir''. Atti 2° Congr. Naz. Sici, 109, 1995.

 

18.            Serenelli G., Loukopoulou Z., Frascarelli M., Petturiti G., Tognellini R.: ''PCNA (Proliferating Cellular Nuclear Antigen)/Cyclin in Friend cells Cultivated in Liquid Kefir-grain-medium (LK)''. Int. J. Oncol. 7, 991, 1995

 

19.            Servillo G., Della Fazia M.A., Pettirossi V., Bartoli D., Ayroldi E., Viola-Magni M.P., ''Expression of the CD44 in the Liver and in the Hepatoma Cells. ECBO 95'', Heidelberg, Germany, 5-8 April 1995.

 

20.            Servillo G., Pettirossi V., Della Fazia M.A., Piobbico D., Ayroldi E., and Viola Magni M.P., ''Espressione del CD 44 in fegato rigenerante''. Convegno Congiunto ABCD, AGI, SIBBM, SIMGMB Montesilvano Lido, 2-5 Ottobre 1995, 45, 1995.

 

21.            Albi E., Micheli M., Viola Magni M.P. “ Phospholipds and Nuclear RNA”. Cell Biol. Intern. 20,6,407-412, 1996.

 

22.            Biagetti M., Bruschi F., Magni F., Viola Magni M.P.: Protein Synthesis in Rat Myocardium after Different Times of Storage in the Cold. An in vitro Study. Riv. It. Biol. Med., 16, 134-141, 1996

 

23.            Patricolo M., Paolocci N., Zangari A., Antonica A., Rossi L., Magni F., Viola-Magni M.P., Caione P., Lais A., Rivosecchi M. ‘’ Resezione epatica fetale nel coniglio: Confronto istologico della rigenerazione tissutale del feto e dell’adulto’’., Minerva Chir, 51, 1996.

 

24.            Serenelli G., Petturiti G., Frascarelli M., Viola Magni M.P., Tognellini R. "Role of Oxidative Agents in Human Erythroleukemic Cell Differentiation". Atti 1st International Conference on Oncology: Research Cell Growth and Oncogenesis, 74, 1996.

 

25.           Serenelli G., Frascarelli M., Petturiti G., Viola Magni M.P., Changes in DNA -Feulgen/nucleus Content in Murine Erythroleukemic Cells (FLC) Cultivated in Presence of Chloramine T. Int. J. Oncol., Suppl. 9, 840, 1996.

 

26.            Lais A., Frascarelli M., Paolocci N., Ciprandi G., Viola Magni M.P., Ferro F., Caione P. ‘’Isolation, Maintenance and Growth of Cultured Urothelial Cells in vitro. Preliminary Paper.’’, European Soc. Paediatric Urology, London, 22-24 March 1996.

 

27.            Albi E., Tomassoni M.L., Viola-Magni M.P. "La Fluidità della Membrana Nucleare", Società Italiana di Biochimica Gruppo Membrane e Bioenergetica & Gruppo Italiano di Bioenergetica e Biomembrane.,  Congresso Congiunto, Assisi, 27-29 Maggio, 1996.

 

28.            Albi E., Micheli M., and Viola Magni M.P. "La Sfingomielinasi Cromatinica in Rigenerazione Epatica" XXIII Congresso Nazionale Società Italiana di Patologia, Milano 23-26 Giugno 1996.

 

29.            Albi E., Tomassoni M.L., Viola Magni M.P. "La Fluidità della Membrana Nucleare in Rigenerazione Epatica, XIII Congresso Nazionale della Società Italiana di Patologia, Milano 23-26 giugno 1996.

 

30.            Della Fazia M.A., Servillo G., Penna L., Piobbico D., Foulkes N.S., Sassone-Corsi P., Viola Magni M.P., ‘’Espressione e Funzione del Gene CREM in fegato rigenerante, 1996, XIII Congresso Nazionale della Società Italiana di Patologia, Milano 23-26 giugno, 137, 1996

 

31.            Servillo G., Pettirossi V., Della Fazia M.A., Bartoli D., Castelli M., Ayroldi E., and Viola-Magni M.P.’’ Differente Espressione del CD44 durante la Rigenerazione Epatica.’’, Att. XXIII Congresso Nazionale, Soc. It. Pat., Milano, 23-26 giugno 1996, 136, 1996.

 

32.            Servillo G., Pettirossi V., Della Fazia M.A., Bartoli D., Castelli M. Ayroldi E., Viola Magni M.P. "Differente espressione del CD44 durante la rigenerazione epatica", XXIII Congresso Nazionaledella Società Italiana di Patologia., Milano 23-26 giugno 1996.

 

33.            Della Fazia M.A. Servillo G., Penna L., Piobbico D., Foulkes N.S., Sassone-Corsi P., Viola Magni M. "Espressione e funzione del gene CREM in fegato rigenerante", XXIII Congresso Nazionaledella Società Italiana di Patologia. , Milano 23-26 giugno 1996.

 

34.           Albi E., and Viola-Magni M.P. "Neutral Sphingomyelinase in Rat Liver Chromatin" 37th International Conference on the Biochemistry of Lipids, Antwerp 4/7 September 1996.

 

35.             Caione P., Frascarelli M., Paolocci N., Ciprandi G., Viola Magni M.P., Ferro F., Capozza N., Matarazzo E., Lais A. "Coltura di Urotelio Autologo: Ricerca Sperimentale". 32 ° Congresso Internazionale della Società Italiana di Chirurgia Pediatrica, Torino, 25-28 Settembre 1996, 101, 1996.

 

36.             Albi E., Tomassoni M.L., Viola-Magni M.P. "Fluidità della Membrana Nucleare ed Attività Nucleosidetrifosfatasica" Convegno Congiunto ABCD-AGI-SIBBM., Riccione,2-5 Ottobre, 1996.

 

37.             Albi E., Micheli M., Viola- Magni M.P. "Double-Stranded RNA e Fosfolipidi" Convegno Congiunto ABCD-AGI-SIBBM, Riccione, 2-5 Ottobre, 1996.

 

38.            Servillo G. Penna L., Viola Magni M., Foulkes N.S., Della Fazia M.A., Sassone-Corsi P. "CREM nella rigenerazione epatica"., Convegno congiunto ABCD AGI SIBBM SIMGBM. , Riccione (RN) 2-5 ottobre 1996.

 

39.             Serenelli G., Frascarelli M., Petturiti G., Viola Magni M.P. "Effetto Protettivo della Vitamina E sulla Differenziazione di Cellule Eritroleucemiche Umane Trattate con un Derivato Organico del Cloro ad Effetto Ossidante". , Atti IX Congresso Internazionale ECBA,  Grado (Go), 10-13 ottobre 1996, 93, 1996.

 

40.            Albi E., Micheli M., Viola Magni M.P.”Choline Base Exchange Activity in Rat Hepatocyte  Nuclei”. Cell Biol. Intern .,21, 217-221, 1997.

 

41.          Albi E., Tomassoni M.L., Viola-Magni M.P. "Effect of lipid composition on rat liver nuclear membrane fluidity" Cell Biochem. and Funct, 15, 181-190, 1997

 

42.            Albi, E. and Viola Magni, M.P. "Chromatin neutral spingomyelinase and its role in hepatic regeneration. Biochim. Biophys. Res. Commun., 236, 29-33, 1997.

 

43.            Albi E., and Viola Magni, M.P. “Sphyngomyelin synthesis in rat liver chromatin” Chemistry Physic of Lipids, 88, 121, 1997.

 

44.            Tomassoni M.L., Albi E., Viola Magni,M.P. “Effect of sphyngomyelinase treatment on nuclear membrane” Chemistry Physic of Lipids, 88, 147, 1997

 

45.            Serenelli, G., Frascarelli, M., Petturiti, G., Viola-Magni, M.P., Tognellini, R., '' Changes in CD44 expression in erythroleukemic cells during DMSO-induced differentiation''. Int. J. Oncol. , Suppl. 11,., 877-940, 1997.

 

46.            Servillo G., Penna L., Foulkes N. S., Viola Magni M., Della Fazia M.A. and Sassone-Corsi P. “Cyclic AMP signalling pathway and cellular proliferation: Induction of CREM during liver regeneration.” Oncogene. 1997; 14 1601-1606.

 

47.             Beccari T., Appolloni M.G., Costanzi E., Stinchi S., Stirling J.L., Della Fazia M.A., Servillo G., Viola M. and Orlacchio A.: "Lysosomial a-D-Mannosidase of in mouse tissue characteristics of the isoenzymes and cloning and expression a full length cDNA"., Biochemical Journal., 327, 45-49 , 1997.

 

48.             Tomassoni M.L., Albi E., Viola Magni M.P. "Influenza della Fluidità della Membrana Nucleare nella Regolazione del Trasporto Nucleocitoplasmatico". Congresso Congiunto Gruppo Italiano di Bioenergetica e Biomembrana e Gruppo Membrane e Bioenergetica della SIB, Riccia (Campobasso), 17-19 Giugno 1997.

 

49.             Albi E.; Viola Magni M.P.; “Sphingomyelin synthesis in rat liver chromatin” 38th International Conference on the Biochemistry of Lipids, Assisi, Italy, September, 16-19, 1997.

 

50.             Micheli,M., Albi,E., Scassellati,C., Antolini,F., and Viola Magni,M.P. "Partial Purification of an Intranuclear Alkaline Sphingomyelinase" 42° Congresso nazionale della Società Italiana di Biochimica" Ancona, 24-27 settembre 1997.

 

51.             Servillo G., Bartoli D., Giacomucci A., Viola Magni M. e Della Fazia M.A.: "Isolamento e caratterizzazione di un gene neoespresso in rigenerazione epatica". Convegno congiunto ABCD-SIBBM-SIMGBM Montesilvano lido (PE) 30 settembre 3 ottobre 1997.

 

52.             Micheli,M., Albi,E., Viola Magni,P.M. “Attività sfingomielinasica e fosfolipasica-C fosfatidilcolina dipendente legata al double-stranded RNA nucleare” , Convegno congiunto ABCD-SIBBM-SIMGBM.,  Montesilvano lido, 30 Settembre-3 Ottobre 1997.

 

53.            Della Fazia M.A., Piobbico D., Castelli M., Viola Magni M. e Servillo G.: "Studio di liver annexin like (LAL-1) in fegato rigenerante’’., Convegno congiunto ABCD-SIBBM-SIMGBM , Montesilvano lido (PE) 30 settembre 3 ottobre 1997.

 

54.            Servillo G., Bartoli D., Giacomucci A., Viola Magni M.P. e Della Fazia M.A.: "Isolamento e caratterizzazione di un gene neoespresso in rigenerazione epatica". Convegno congiunto ABCD-SIBBM-SIMGBM, Montesilvano lido (PE) 30 settembre 3 ottobre 1997.

 

55.            Della Fazia M.A., Piobbico D., Castelli M., Viola Magni M. e Servillo G.: "Studio di liver annexin like (LAL-1) in fegato rigenerante. Convegno congiunto ABCD-SIBBM-SIMGBM Montesilvano lido (PE) 30 settembre 3 ottobre 1997.

 

56.            Albi,E., Peloso,I., Viola Magni,M.P. “Metabolismo sfingomielina-colesterolo nella cromatina di fegato di ratto” Convegno congiunto ABCD-SIBBM-SIMGBM. Montesilvano lido, 30 Settembre-3 Ottobre 1997

 

57.             Albi,E., Serenelli,G., and Viola Magni,M.P. "Erythroleukemic Cells: Neutral Sphingomyelinase and Differentiation" Biomedicina '97 Firenze, 26-28 novembre 1997

 

58.             Micheli M., Albi E., Leray, C., and Viola Magni, M.P. “Nuclear Sphinsomyelin Protects RNA from RNAse Action” FEBS, 431, 443-447, 1998.

 

59.             Albi,E., and Viola Magni, M.P. "Neutral Sphingomyelinase and Phosphatidylcholine-dependent phospholipase C in rat hepatocyte chromatin" Chemistry and Physic of Lipids,  94, 160, 1998.

 

60.            Peloso, I., Albi, E. and Viola Magni, M.P. "Presence of cholesterol in rat liver chromatin and nuclear matrix" Chemistry and Physic of Lipids, 94, 160, 1998.

 

61.            Della Fazia,M.A, Piobbico, D.,.Castelli ,M. , Micheli, M., Viola-Magn, M.P., Servillo, G., ‘’ 2LAL-1: nuovo gene “Annexin like” in rigenerazione epatica”. XXIV Congresso Nazionale della Società Italiana di Patologia., Siena 24-27 giugno 1998.,  Abstract book,  16, 1998.

 

62.           Servillo G., Bartoli D., Brancorsini S., , Giacomucci, A, Viola Magni,M.P.,. Della Fazia, M.A, : “Isolamento e caratterizzazione di un gene neoespresso in rigenerazione epatica”. XXIV Congresso Nazionale della Società Italiana di Patologia. , Siena 24-27 giugno 1998.

 

63.            Albi,E., Peloso,I., Cataldi,S., Viola Magni ,M.P. "La Fosfolipasi C-Fosafatidilcolina-Dipendente e la Fosfatidilcolina-Sintasi Cromatiniche nella Rigenerazione Epatica" XXIV Congresso Nazionale della Società Italiana di Patologia Siena, 24-27 Giugno 1998

 

64.           Rossi,G., Albi,E., Viola Magni,M.P. "La fosfolipasi C fosfatidilinositolo-dipendente nella cromatina di fegato di ratto" XXIV Congresso Nazionale della Società Italiana di Patologia Siena, 24-27 Giugno 1998

 

65.            Servillo G., Della Fazia M. A. and Sassone-Corsi P. "Transcription Factor CREM Regulates the Timing of Hepatocytes Proliferation upon Liver Regeneration" EMBL Transcription meeting August 22-26, 1998

 

66.           Cataldi,S., Albi,E., Viola Magni,M.P. "I Plasmalogeni Intranucleari" Convegno congiunto ABCD-AGI-SIBBM-SIMGBM Montesilvano, 1-4-ottobre 1998.

 

67.            Servillo G., Castelli M., Bartoli D., Brancorsini S., Piobbico D., Viola Magni M., Della Fazia M.A.: “Un nuovo gene a 4 domini LXXLL in rigenerazione epatica”., Convegno congiunto ABCD, AGI, SIBM, SIMGBM, Montesilvano Lido (PE), 1-4 ottobre 1998, Abstract Book , 167, 1998.

 

68.            Serenelli,G., Albi,E., Viola Magni, M.P. “Camelia sinensis Kuntze, un antiossidante naturale, effetti sul metabolismo fosfolipidico in cellule eritroleucemiche di Friend” XI Congresso Internazionale Ordine Nazionale dei Biologi Napoli 15-18 Ottobre 1998

 

69.             Albi,E., Serenelli,G., and Viola Magni,M.P. "Changes in Nuclear Phosphatidylcholine-Dependent Phospholipase C activity in Erythroleukemic Cell Induced to Differentiate" Biomedicina '98 Florence, 25-27 November 1998

 

70.              Tomassoni, ML, Amori, D, Magni MV. "Changes of nuclear membrane lipid composition affect RNA nucleocytoplasmic transport." Biochem Biophys Res Comm,  258, 476-481, 1999.

 

71.              Albi,E., and Viola Magni,M.P. “Phosphatidylcholine-Dependent Phospholipase C in Rat Liver Chromatin” Biochem.Biophys.Res.Commun. 265, 640-643, 1999.

 

72.              Tomassoni, M.L., Amori, D., Leray, C., Micheli, M., Viola-Magni, M.P., '' Biophysical and biochemical characteristics of nuclear membrane isolated from rat hepatoma cell line Reuber H 35''.Biochemie-An International Journal of Biochemistry and Molecular Biology, Suppl. 6, s 140,1999.

 

73.              Albi E., Peloso I, Viola Magni MP. "Nuclear membrane sphingomyeline-Cholesterol changes in rat liver after hepatectomy". Biochim. Biophys. Res. Commun. 262, 692-695, 1999

 

74.             Albi,E., Viola Magni,M.P. “Sphingomyelin-Synthase in Rat Liver Nuclear Membrane and Chromatin” FEBS Letters 460, 369-372, 1999

 

75.              Albi,E., Peloso,I., Viola Magni,M.P. “Effect of oxysterols on intranuclear lipids” 40th International Conference of the Biochemistry of Lipids Graz, Austria September 1999. Chemistry and Physic of Lipids 101, 2, 1999.

 

76.              Della Fazia M.A., Castelli M., Bartoli D., Brancorsini S., Piobbico D., Banelli E., Viola Magni M., Servillo G.: “Espressione e caratterizzazione di un nuovo gene ubiquitin-like espresso in rigenerazione epatica”. 1° Convegno FISV. Riva del Garda (TN), 2-6 ottobre 1999. Abstract Book pag. 172.

 

77.              Panarelli,P., Albi,E., and Viola Magni,M.P. “Presence of antiphosphatidylinositol antibodies in deep venous thrombosis patients affected by nervous system vascular damage” Biomedicina 99” November 24-29, 1999, Firenze

 

78.              Serenelli,G., Albi,E., Viola Magni,M.P. “Chromatin Neutral Sphingomyelinase in Friend Leukemia Cells Treated with Medicinal Infusion of Camellia sinensis Kuntze” Biomedicina 99” November 24-29, 1999, Firenze

 

79.              Albi,E., Pieroni,S., Sartori,C., Viola Magni, M.P. “Effetto del ciprofibrato sulla sfingomielinasi neutra cromatinica” XXV Congresso Nazionale della Società Italiana di Patologia  Giugno 7-10, 2000, Bari

 

80.              Albi,E., Cataldi,S., Lazzarini,R., Peloso,I., Viola Magni,M.P.  “Modificazioni del colesterolo cromatinico in rigenerazione epatica” XXV Congresso Nazionale della Società Italiana di Patologia  Giugno 7-10, 2000, Bari

 

81.              Della Fazia M.A., Castelli M., Bartoli D., Brancorsini S., Pettirossi V. Piobbico D., Ubaldi M.., Viola Magni M., Servillo G.: “Studio di un nuovo gene Ubiquitin-like espresso in rigenerazione epatica”. XXV Congresso Nazionale della Società Italiana di Patologia, Bari, 7-10 giugno 2000, Abstract Book pag. 57.

 

82.              Della Fazia M.A., Brancorsini S., Renna L.A., Castelli M., Bartoli D., Pettirossi V. Piobbico D., Viola Magni M., Servillo G.: “Analisi molecolare e cellulare di un nuovo gene 4/4 isolato da fegato rigenerante”. XXV Congresso Nazionale della Società Italiana di Patologia, Bari, 7-10 giugno 2000, Abstract Book pag. 83.

 

83.              Della Fazia M.A., Pettirossi V., Ayroldi E., Riccardi C., Viola Magni M. and Servillo G. “CD44 and cellular proliferation: differential expression of isoform during liver regeneration”.J. Hepat. 2001, 34: 555-561.

 

84.              Caso,V., Panarelli,P., Paciaroni,M., Albi,E., Magni,V., Parnetti,L., Gallai,V. “A new assay for antiphospholipid antibodies in patient with ischemic stroke” XXXII Congress of the Italian Neurological Society. Neurological Sciences Supplement vol. 22 September 2001

 

85.              Albi,E., Cataldi,S., Maraldi,N., Rossi,G., Viola Magni, M.P., Zini, N. “Chromatin phosphatidylinositol-dependent phospholipase C in cell proliferation” XVIII Conferenza Nazionale di Citometria Ottobre 2-5 2001 Chioggia (Venezia)

 

86.              Albi,E., Scassellati,C., Fakan,S., Viola Magni,M.P. “Electron microscopy cytochemical study of the localization of the chromatin sphingomyelin” XVIII Conferenza Nazionale di Citometria Ottobre 2-5 2001 Chioggia (Venezia)

 

87.              Albi,E., Cataldi,S., Lazzarini,R, Rossi,G., Viola Magni,MP.“The chromatin cholesterol during rat liver regeneration” 7th European Meeting on hepatocarcinogenesis. October 12-15, 2001 Castiadas (Sardinia)

 

88.              Della Fazia M.A., Castelli M., Bartoli D., Brancorsini S., Pettirossi V. Piobbico D., Viola Magni M., Servillo G.: “A novel gene during liver regeneration: characterization and functional analysis” 7th European Metting on Hepatocarcinogenesis. Castadias , Italy 12-15 October 2001, Abstract Book pag. 56.

 

89.              Albi,E., Viola Magni,M.P. “The presence and the role of chromatin cholesterol in rat liver regeneration” Journal of Hepatology 36, 395-400, 2002.

 

90.              Caso,V., Panarelli,P., Albi,E., Viola-Magni,M.P., Parnetti,L., Gallai,V.“Phospholipid autoantibodies: time for a new immuno-assay?” Clin Exp Hypertens. 24: 511-516, 2002.

 

91.              Della Fazia M.A., Piobbico D., Bartoli D., Castelli M., Brancorsini S., Viola Magni M. and Servillo G. “ lal-1: a differentially expressed novel gene during proliferation in liver regeneration and in hepatoma cells” Genes to cells, 2002, 7, 1183-1190.

 

92.              Albi,E., Lazzarini,R., Rossi,G., Borio,T., Viola Magni,M.P. “A Phospholipid intranuclear clock regulates the cell fate” Cell Signaling, Transcription and Translation as Therapeutic Targets. Luxembourg, January 30 to February 2nd 2002

 

93.              Cataldi,S, Viola Magni,MP., Albi,E. “Nuclear cholesterol-sphingomyelin relationship in tumor growth” Cell Signaling, Transcription and Translation as Therapeutic Targets. Luxembourg, January 30 to February 2nd 2002

 

94.              Albi, E., Serenelli, G., Rossi, G., Cataldi, S., Borio, T., Lazzarini, R. Viola Magni, M.P.  Can the nuclear sphingomyelin regulate the fate of the cell? First Meeting “Sphingolipid Club” Perugia, 24-25 maggio 2002

 

95.              Albi, E., Rossi, G., Cataldi, S., Borio, T., Lazzarini, R., Viola Magni, M.P. Intranuclear lipid signalling. International Conference on the Bioscience of Lipids ICBL Graz, September 11-14, Chemistry and Physic of Lipids 118,1-2, 2002.

 

96.              Albi,E., Cataldi,S., Viola Magni,M.P. L’inibizione della sfingomielinasi nucleare rallenta la crescita tumorale. 26° Congresso Nazionale Società Italiana di Patologia, Catania 29 settembre-2 ottobre 2002.

 

97.              Albi,E., Rossi,G., Borio,T., Tringali A.R, Tringali S., Lazzarini,R., Viola Magni,M.P. La sfingomielina e la fosfatidilcolina intranucleari regolano la funzione cellulare. 26° Congresso Nazionale Società Italiana di Patologia, Catania 29 settembre-2 ottobre 2002.

 

98.              Della Fazia M.A., Castelli M., Bartoli D., Pettirossi V., Piobbico D., Pieroni S., Viola Magni M. Servillo G.: “Un nuovo gene coinvolto in rigenerazione epatica: cambiamenti molecolari durante la proliferazione cellulare” 26° congresso nazionale SIP. Catania,  29 sett. – 2 ott. 2002, Abstract Book pag. 118-119

 

99.              Panarelli,P., Viola-Magni,M.P., and Albi E. “Antiphosphatidylinositol antibody in deep venous thrombosis patients” Int.J. Immunopath. Pharm. 2003, 16: 61-6.

 

100.         Albi,E., Cataldi,S., Rossi,G., and Viola Magni,M.P. A possible role of cholesterol-sphingomyelin/phosphatidylcholine in nuclear matrix during rat liver regeneration. J. Hepatology 2003, 38: 623-8.

 

101.         Albi,E., Pieroni,S., Viola Magni,M.P., and Sartori,CChromatin sphingomyelin changes in cell proliferation and/or apoptosis induced by ciprofibrate. J. Cell Physiol. 2003, 196:354-61

 

102.         Valeria Caso, Lucilla Parnetti, Paolo Panarelli, Maria Pia Viola Magni, MD, Virgilio Gallai, Elisabetta Albi Selection of Thrombogenetic Antiphospholipid Antibodies In Cerebrovascular Disease Patients J.Neurol 2003, 250: 593-7.

 

103.         Albi,E., Rossi,G., Maraldi,N.M., Viola Magni,M.P., Cataldi,S., Solimando, L., Zini,N. Involvement of nuclear Phosphatidylinositol-dependent Phospholipases C in cell cycle progression  during rat liver J. Cell Physiol. 2003, 197: 181-188.

 

104.         Albi,E., and Viola Magni,M.P. “The metabolism of nuclear phospholipids in cell function regulation” Recent Res Develop Biophys Biochem 2003, 3:45-63.

 

105.         Albi,E., and Viola Magni,M.P. “Chromatin associated sphingomyelin: metabolism in relation to cell function” Cell Biochem Funct. 2003, 21(3):211-215.

 

106.         Elisabetta Albi, Remo Lazzarini and Mariapia Viola Magni “Reverse Sphingomyelin-Synthase in Rat Liver Chromatin” FEBS Letters 2003, 549(1-3):152-156

 

107.         Albi,E., Cataldi,S., Colombaioni,L., Mazzoni, F., Viola Magni, M.P., Vaccoli, V., Garcia-Gil M. Serum deprivation activates the sphingomyelin metabolism in neuronal cell nuclei. Second Meeting “Sphingolipid Club” Sale Marasino, 3-4 giugno 2003

 

108.         Albi,E., Cataldi,S., Lazzarini, R., Rossi, G., Tringali, A.R., Tringali, S., Viola Magni, MP. The sphingomyelinase activity regulates the cholesterol level in the nucleus. Second Meeting “Sphingolipid Club” Sale Marasino, 3-4 giugno 2003

 

109.         Perrella, G., Cataldi, S., Toller,M., Meli, A., Del Terra, E., Casani, S., Ranaldi, F., and Albi,E. “Sphingomyelin metabolism modifications in response to the effect of the UV and cosmic (stratospheric) radiation. Second Meeting “Sphingolipid Club” Sale Marasino, 3-4 giugno 2003

 

110.         Albi,E., Cataldi,S., Lazzarini, R., Rossi, G., Viola Magni, MP. Intranuclear sphingomyelin and transcription. 2nd International “Charleston Ceramide Conference”. Como, Italy, June 4-7, 2003

 

111.         Elisabetta Albi, Samuela Cataldi, Mariapia Viola Magni and Claudia Sartori “Plasmalogens  in rat liver chromatin: new molecules involved in cell proliferation” J. Cell Physiol, 2004, 201(3):439-46.

 

112.         Albi E and Viola Magni MP “The role of intranuclear lipids” Biology of the Cell, 2004, 96(8):657-67

 

113.         La Porta C.A.M., Cataldi S., Lazzarini, R, Viola Magni, MP. Albi E. Effect of Protein kinase C delta on nuclear sphingomyelin metabolism. Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

114.         Albi E, Cataldi S, Bartoccini E,Mazzoni F, Voccoli V, Viola Magni M,  Lazzarini R, and Garcia-Gil M. Sphingomyelin metabolism changes after serum deprivation in neuronal cell nuclei. Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

115.         Rossi G., Viola Magni MP, Albi E.Double strand RNA and sphingomyelin. Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

116.         Villani M., Cascianelli G., Tosti M., Viola Magni MP, Albi E. Lipid rafts in hepatocyte nuclei. Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

117.         Tringali Sabina, Tringali Anna Rita, Viola Magni MP, Albi E. Dexametasone reduces cell growth via nuclear sphingomyelin metabolism Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

118.         Pugliese L., Bernardini I., Viola Magni MP, Albi E. Cholesterol/sphingomyelin relationships in oncohaematologic patients Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004.

 

119.         Perrella G., Cataldi S., Toller M., Meli A., Ranaldi F., Viola Magni M.P. and Albi E. Sphingomyelin metabolism modifications in response to the effect of high neutron energy. Third Meeting “Sphingolipid Club” Firenze, 18-19 giugno 2004

 

120.         Pugliese L., Bernardini I., Viola Magni MP., Albi E. Anti-Sphingomyelin Antibodies in Oncologic Patients. 4th Meeting of the Sphingolipid Club Bertinoro 9-11 giugno 2005.

 

121.         Cascianelli G., Villani M., Tosti M., Viola Magni MP, Albi E.Sphingomyelin and Stat 3 in Nuclear Lipid Rafts . 4th Meeting of the Sphingolipid Club Bertinoro 9-11 giugno 2005.

 

122.         Bartoccini E1,Mazzoni F 2, Viola Magni M1, Garcia-Gil M2 and Albi E1 Effect of vitamin D3 on embryonic hippocampal cells via neutral sphingomyelinase. 4th Meeting of the Sphingolipid Club Bertinoro 9-11 giugno 2005.

 

123.         Tringali Anna Rita, Tringali Sabina, Viola Magni M.P., Albi E. Effect of Dexamethasone on cellular and nuclear Sphingomyelin-synthase. 4th Meeting of the Sphingolipid Club Bertinoro 9-11 giugno 2005.

 

124.         Elisabetta Albi, Samuela Cataldi, Elisa Bartoccini, Mariapia Viola Magni, Francesca Marini, Francesca Mazzoni, Giuseppe Rainaldi, Monica Evangelisti, Mercedes Garcia-Gil “Nuclear sphingomyelin pathway in serum deprivation-induced apoptosis of embryonic hippocampal cells” J Cell Physiol, 2005, 206:189-95.

 

125.         Elisabetta Albi, Caterina AM LaPorta , Samuela Cataldi, Mariapia Viola Magni “Nuclear sphingomyelin-synthase and protein kinase C delta in  melanoma cells” Arch. Biochem Biophys, 2005, 438:156-61.

 

126.         Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V., Piobbico D., Viola-Magni M. and Servillo G.“HOPS: a novel cAMP-dependent shuttling protein involved in protein synthesis regulation” J. Cell Sci. 2005, 118, 3185-3194  (IF. 7.250)

 

286     Rossi G, Magni MV, Albi E. Sphingomyelin-cholesterol and double stranded RNA relationship in the intranuclear complex. Arch Biochem Biophys. 2007;459:27–32

 

287     Pugliese L, Bernardini I, Pacifico E, Viola-Magni M, Albi E. Antiphospholipid antibodies in patients with cancer. Int J Immunopathol Pharmacol. 2006 Oct-Dec;19(4):879-88.

 

 

 

288     Pugliese L, Bernardini I, Viola-Magni MP, Albi E. Low levels of serum cholesterol/phospholipids are associated with the antiphospholipid antibodies in monoclonal gammopathy. Int J Immunopathol Pharmacol. 2006 Apr-Jun;19(2):331-7.

 

289     Albi E, Viola Magni MP. Sphingomyelin: a small-big molecule in the nucleus. Rec Res Dev Biophys Biochem. 2006; 661:211–227.

 

 

290   Rossi G., Viola-Magni M.,  Albi E. Sphingomyelin-cholesterol and double strended RNA relationship in the intranuclear complex. Achives of Biochemistry and Biophysics Volume 459, issue 1, 1 march 2007, 27-32.

 

 

 

291     Rossi G, Viola Magni M, Albi E. Signal transducer and activator of transcription 3 and sphingomyelin metabolism in intranuclear complex during cell proliferation.Arch Biochem Biophys. 2007 Aug 1;464(1):138-43. Epub 2007 Apr 24.

 

 

 

292     Bernardini I., Bartoccini E., Viola Magni M., Albi E. 2007. Nuclear Lipids and Cell Fate. Dynamic Cell Biol. 1, 42-47 Global Science Books. Print ISSN 1749-0561

 

 

 

293     Albi E, Lazzarini R, Viola Magni M. Phosphatidylcholine/sphingomyelin metabolism crosstalk inside the nucleus. Biochem J. 2008 Mar 1;410(2):381-9.

 

 

 

294     Cascianelli G, Villani M, Tosti M, Marini F, Bartoccini E, Magni MV, Albi E. Lipid microdomains in cell nucleus. Mol Biol Cell. 2008 Dec;19(12):5289-95.

 

 

 

295           Albi E, Cataldi S, Rossi G, Viola Magni M, Toller M, Casani S, Perrella G. The nuclear ceramide/diacylglycerol balance depends on the physiological state of thyroid cells and changes during UV-C radiation-induced apoptosis. Arch Biochem Biophys. 2008 Oct 1;478(1):52-8.  

 

 

 

296     Stefania Pieroni,1, Maria Agnese Della Fazia,1, Marilena Castelli,1 Danilo Piobbico,1 Daniela Bartoli,1 Cinzia Brunacci1, Marina Maria Bellet,1 Mariapia Viola-Magni1 and Giuseppe Servillo1,* HOPS is an essential constituent of centrosome assembly. Cell Cycle 7:10, 1462-1466; 15 May 2008

 

 

 

297     Brunacci C, Piobbico D, Bartoli D, Castelli M, Pieroni S, Bellet MM, Viola-Magni M, Della Fazia MA, Servillo G. Identification and characterization of a novel peptide interacting with cAMP-responsive elements binding and cAMP-responsive elements modulator in mouse liver. Liver Int. 2010 Mar;30(3):388-95. Epub 2009 Nov 24.

 

 

 

298     Marini F, Bartoccini E, Cascianelli G, Voccoli V, Baviglia MG, Magni MV, Garcia-Gil M, Albi E. Effect of 1alpha,25-dihydroxyvitamin D3 in embryonic hippocampal cells. Hippocampus. 2010 Jun;20(6):696-705.

 

 

 

299                      Scassellati C, Albi E, Cmarko D, Tiberi C, Cmarkova J, Bouchet-Marquis C, Verschure PJ, Driel R, Magni MV, Fakan S. Intranuclear sphingomyelin is associated with transcriptionally active chromatin and plays a role in nuclear integrity. Biol Cell. 2010 Apr 1;102(6):361-75.

 

 

 

300                      Bruschi F, Dundar M, Gahan PB, Gartland K, Szente M, Viola-Magni MP, Akbarova Y. Biotechnology worldwide and the 'European Biotechnology Thematic Network' Association (EBTNA). Curr Opin Biotechnol. 2011 Sep;22 Suppl 1:S7-14. Epub 2011 Jun 15

 

301                      M. Viola-Magni and P.B. Gahan (2012). Possible Roles of Nuclear Lipids in Liver Regeneration, Liver Regeneration, PhD. Pedro Baptista (Ed.), ISBN: 978-953-51-0622-7, InTech, Available from: http://www.intechopen.com/books/liver-regeneration/role-of-chromatin-lipids-in-liver-regeneration.

 

 

 

302           Biotechnology worldwide and the “European Biotechnology Thematic Association(EBTNA) (2011). Current opinion in biotechnology  22S 7-14

 

 

 

303    M.P. Viola-Magni1, S. Cataldi 1, P.B. Gahan, M. Stroun ( 2012)The cholesterol presence in virtosomes        Journal of Biotechnology 161S  5–12

 

 

 

304       M.P. Viola Magni, S. Cataldi , P.L. Orvietani,F.Susta, L. Binaglia, M. Stroun2, P. B.Gahan1 (2013)The protein composition of virtosomes isolated from non stimulated and stimulated lymphocytes. Current Opinion in Biotechnology 24 S21–S27

 

 

 

305      M P Viola Magni, S. Cataldi, M Stroum and. PB Gahan: Virtosomes-intracellular messengers?( 2014 ) J. Biotech. Biomater 3,5

 

 

306     Viola-Magni M.P., Cataldi S, StrounM. Gahan P.B.,. Virtosomes- intracellular messengers? Biotechnology 5° Congress Omics group Valencia 2014

 

307     S. Cataldi, M.P. Viola-Magni The expression of Hox genes, zen (GB 51301) ANT and UBX during the development of honey bee,(Apis mellifera)2014 in pubblicazione

 

 

 

308      Viola-Magni M.P. and Cataldi S. Biological markers for bladder cancer , J. of Biotechnology  2014  vol 185, supp.,11.

 

309     Novel technologies and their applications in biotechnology

 

Yusuf Deeni, T. Beccari,M.Dundar,Jill S Gartland,M.Maffia ; M.Viola-Magni,     K.M.A.Gartland 2014. European Journal of Biotechnology and Bioscience,2(6),13-19

 

 

 

310       Yusuf Deeni, T. Beccari,M.Dundar,Jill S Gartland,M.Maffia ; M.Viola-Magni, K.M.A.Gartland. Trends Reshaping Biotechnology. http://hplusmagzine.com 2015/03/12/8

 

 

 

311       T.Beccari,M.R.Ceccarini,M.Codini and MpViola-Magni

 

DNA sequencing technology:the clinical potential   Libro

 

 

 

312      MP Viola-Magni The biology of micro RNA and its role in pathology. J. Biotech 2015. Doi.org/10.1016/j.jbiotec.2015.06.004

 

 

 

313      Kevan M:A:Gartland,T.Beccari,F.Bruschi; M.Dundar,M.P. Viola-Magni,Jill S.Gartland
Innovation in Biotechnology, J. Biotech 2015. Doi.org/ 10.1016/j.jbiotec.2015.06.002

 

 

 

 

 

 

 

 

 

 

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