Search

Your search keyword '"Trabalzini, L."' showing total 138 results
Start Over Author "Trabalzini, L."
138 results on '"Trabalzini, L."'

6. Cerebral Cavernous Malformations: from disease mechanisms to novel therapeutic approaches

Author

Goitre, Luca, Moglia, Andrea, Trapani, Eliana, Marchi, S., Pinton, P., Delle Monache, S., Cianfruglia, L., Armeni, T., Principato, G., Antognelli, C., Talesa, V., Tognon, M., Fontanella, M., Baldini, E., Trabalzini, L., D. Y., Li, and Retta, Saverio Francesco

Subjects
Molecular Mechanisms of CCM Pathogenesis, Cerebral cavernous malformation (CCM), Cerebrovascular disease, KRIT1, Redox Biology, Oxidative stress
Published
2014

8. Role of KRIT1 in the pathogenesis of Cerebral Cavernous Malformations (CCM): from disease mechanisms toward pharmacological therapies

Author

Goitre, Luca, Cutano, V., Trapani, Eliana, Morina, A., Canzoneri, R., Gianoglio, S., Moglia, Andrea, Cianfruglia, L., Armeni, T., Delle Monache, S., Rudini, N., Dejana, E., Gallone, S., Fontanella, M., Baldini, E., Trabalzini, L., and Retta, Saverio Francesco

Subjects
Molecular Mechanisms of CCM Pathogenesis, Cerebral cavernous malformation (CCM), KRIT1, Cerebrovascular disease
Published
2013

9. Cerebral Cavernous Malformations: the CCM Italia research network offers new therapeutic perspectives

Author

Goitre, Luca, Cutano, V., Trapani, Eliana, Morina, A., Canzoneri, R., Pergolizzi, Barbara, Gianoglio, S., Moglia, Andrea, Cianfruglia, L., Armeni, T., Delle Monache, S., Tognon, M., Fontanella, M., Baldini, E., Trabalzini, L., and Retta, Saverio Francesco

Subjects
Molecular Mechanisms of CCM Pathogenesis, KRIT1, Cerebral Cavernous Malformation (CCM), Cerebrovascular disease
Published
2013

13. Methods to study the Ras2 protein activation state and the subcellular localization of Ras-GTP in saccharomyces cerevisiae

Author

Trabalzini, L, Retta, SF, Colombo, S, Martegani, E, COLOMBO, SONIA, MARTEGANI, ENZO, Trabalzini, L, Retta, SF, Colombo, S, Martegani, E, COLOMBO, SONIA, and MARTEGANI, ENZO

Abstract

Ras proteins were highly conserved during evolution. They function as a point of convergence for different signalling pathways in eukaryotes and are involved in a wide range of cellular responses (shift from gluconeogenic to fermentative growth, breakdown of storage carbohydrates, stress resistance, growth control and determination of life span, morphogenesis and development, and others). These proteins are members of the small GTPase superfamily, which are active in the GTP-bound form and inactive in the GDP-bound form. Given the importance of studies on the Ras protein activation state to understand the detailed mechanism of Ras-mediated signal transduction, we provide here a simple, sensitive, and reliable method, based on the high affinity interaction of Ras-GTP with the Ras binding domain (RBD) of Raf1, to measure the level of Ras2-GTP on total Ras2 in Saccharomyces cerevisiae. Moreover, to study the localization of Ras-GTP in vivo in single S. Cerevisiae cells, we expressed a probe consisting of a GFP fusion with a trimeric Ras Binding Domain of Raf1 (eGFP-RBD3), which was proven to be a useful live-cell biosensor for Ras-GTP in mammalian cells. © 2014 Springer Science+Business Media, LLC.

Published
2014

14. Yeast as a model for Ras signalling

Author

Trabalzini, L, Retta, SF, Tisi, R, Belotti, F, Martegani, E, TISI, RENATA ANITA, BELOTTI, FIORELLA, MARTEGANI, ENZO, Trabalzini, L, Retta, SF, Tisi, R, Belotti, F, Martegani, E, TISI, RENATA ANITA, BELOTTI, FIORELLA, and MARTEGANI, ENZO

Abstract

For centuries yeast species have been popular hosts for classical biotechnology processes, such as baking, brewing, and wine making, and more recently for recombinant proteins production, thanks to the advantages of unicellular organisms (i.e., ease of genetic manipulation and rapid growth) together with the ability to perform eukaryotic posttranslational modifications. Moreover, yeast cells have been used for few decades as a tool for identifying the genes and pathways involved in basic cellular processes such as the cell cycle, aging, and stress response.In the budding yeast S. cerevisiae the Ras/cAMP/PKA pathway is directly involved in the regulation of metabolism, cell growth, stress resistance, and proliferation in response to the availability of nutrients and in the adaptation to glucose, controlling cytosolic cAMP levels and consequently the cAMP-dependent protein kinase (PKA) activity.Moreover, Ras signalling has been identified in several pathogenic yeasts as a key controller for virulence, due to its involvement in yeast morphogenesis. Nowadays, yeasts are still useful for Ras-like proteins investigation, both as model organisms and as a test tube to study variants of heterologous Ras-like proteins.

Published
2014

21. Helicobacter pylori immunoproteomes in case reports of rosacea and chronic urticaria

Author

Mini R, Figura N, D'Ambrosio C, Braconi D, Bernardini G, Di Simplicio F, Lenzi C, Nuti R, Trabalzini L, Martelli P, Bovalini L, Scaloni A, and Santucci A

Abstract

Rosacea and chronic urticaria are two common skin disorders existing in idiopathic forms. A role of Helicobacter pylori bacterium infection in the aetiopathogenesis of rosacea or chronic urticaria has been suggested although still controversial. The aim of the present study was to establish a relationship between H. pylori infection and rosacea chronic urticaria by means of an immunoproteomic investigation. We analyzed immunoglobulin A (IgA)-, IgG-, and IgE-mediated immune-responses against H. pylori antigens and we identified some bacterial immunoresponsive proteins. A general IgA- and IgE-mediated immune response against antioxidative bacterial proteins was observed. A correlation between the bacterial occurrence and skin diseases pathogenesis is discussed.

Published
2005

25. Inactivation of Helicobacter pylori cagA gene affects motility

Author

Figura N, Trabalzini L, Mini R, Bernardini G, Scaloni A, Talamo F, Lusini P, Ferro E, Martelli P, and Santucci A.

Subjects
bacteria, bacterial infections and mycoses, digestive system, digestive system diseases
Abstract

The cytotoxin-associated protein CagA is a Helicobacter pylori immunodominant antigen whose gene resides in the cag pathogenicity island. Our purpose was to determine if the disruption or deletion of cagA gene could have an effect on the expression of other proteins at the proteome level. We analyzed two H. pylori strains, 328 and G27 wild-type, bearing the cag pathogenicity island, and their respective isogenic cagA(-) mutants. METHODS: The proteomes of two H. pylori strains (328 and its isogenic mutant SPM328_DeltacagA) were resolved by two-dimensional electrophoresis and the digitalized images obtained were analysed both quantitatively and qualitatively. Peculiar spots of each strain were identified by mass spectrometry or by Western blotting. RESULTS: The comparison between the proteome expression of an H. pylori cagA(+) strain and an isogenic mutant strain where the cagA gene was disrupted showed that, as well as the lack of expression of CagA, both flagellin A and flagellin B expressions were significantly decreased. The cagA(-) isogenic mutant was nonmotile. G27_DeltacagA, in which CagA was inactivated by gene deletion, was nonmotile as well respecting to motile G27 wild-type strain. Moreover, reintroduction of cagA in G27_DeltacagA restored motility. CONCLUSIONS: Our results suggest that CagA could quantitatively influence flaA and flaB transcription or their subsequent translation and/or correct folding.

Published
2004

29. Proteomic response to physiological fermentation stresses in a wild-type wine strain of saccharomyces cerevisiae

Author

Trabalzini L., Paffetti A., Scaloni A., Talamo F., Ferro E., Coratza G., Bovalini L., Lusini P., Martelli P., and Santucci A.

Abstract

We report a study on the adaptive response of a wild-type wine Saccharomyces cerevisiae strain, isolated from natural spontaneous grape must, to mild and progressive physiological stresses due to fermentation. We observed by two-dimensional electrophoresis how the yeast proteome changes during glucose exhaustion, before the cell enters its complete stationary phase. On the basis of their identification, the proteins representing the S. cerevisiae proteomic response to fermentation stresses were divided into three classes: repressed proteins, induced proteins and autoproteolysed proteins. In an overall view, the proteome adaptation of S. cerevisiae at the time of glucose exhaustion seems to be directed mainly against the effects of ethanol, causing both hyperosmolarity and oxidative responses. Stress-induced autoproteolysis is directed mainly towards specific isoforms of glycolytic enzymes. Through the use of a wild-type S. cerevisiae strain and PMSF, a specific inhibitor of vacuolar proteinase B, we could also distinguish the specific contributions of the vacuole and the proteasome to the autoproteolytic process.

Published
2003

43. Haemorheological and endothelial-dependent alterations in heart failure after ACE inhibitor, calcium antagonist and β blocker.

Author

Turchetti, V., Bellini, M.A., Boschi, L., Postorino, G., Pallassini, A., Richichi, M.G., Trabalzini, L., Guerrini, M., and Forconi, S.

Subjects
HEART failure, HEMORHEOLOGY, HEART dilatation
Abstract

The aim of our study was to evaluate endothelium-dependent dilatation induced by an ACE-inhibitor, calcium antagonist and β blocker in patients suffering from heart failure (NYHA class II and III). We studied 34 patients (19M, 15F, mean age 76.96 ± 8.82) in pharmacological wash-out for at least one week, divided into 3 groups: Group A (15 patients, 9M and 6F) taking ramipril (5 mg/die); Group B (10 patients, 6M and 4F) taking amlodipine (10 mg/die), Group C: (9 patients, 4M and 5F) taking carvedilole (25 mg/die). The groups were homologous for NYHA class and instrumental echographic parameters (mean EF = 22.5 ± 6.7 and mean sAPP 38.4 ± 8.7). At the beginning and after 3 weeks of therapy, we performed a clinical and instrumental assessment; we studied endothelial function by determination of L-arginine and L-citrulline (amino acids of the nitric oxide metabolic pathway), the L-citrulline/L-arginine ratio (an index of NOS activity) and VCAM-1 (endothelial dysfunction index); haemorheological parameters (blood viscosity, plasma fibrinogen and erythrocyte morphology); coagulative/fibrinolytic parameters (PT, aPTT, fibrinogen and PAI-1). The results show that L-citrulline and L-arginine increase, while VCAM-1 decreases. The L-citrulline/L-arginine ratio increases in a statistically significant way. This trend is maintained in each group. These results demonstrate that the drugs used induce an improvement of endothelium-dependent dilatation. In addition, there is progressive haemorheological and fibrinolytic improvement, with a reduction of PAI-1 and blood viscosity. [ABSTRACT FROM AUTHOR]

Published
2002

44. Spontaneous echo-contrast as an in vivo indicator of rheological imbalance in dilatative cardiomyopathy.

Author

Turchetti, V., Bellini, M.A., Ricci, D., Lapi, A., Donati, G., Boschi, L., Trabalzini, L., Guerrini, M., and Forconi, S.

Subjects
CARDIOMYOPATHIES, RHEOLOGY (Biology)
Abstract

The aim of this study was to evaluate coagulative and hemorheologic assessment in patients with dilatative cardiomyopathy with or without spontaneous echo contrast (SEC). We studied 45 patients, 35 males and 10 females (mean age 72.1 ± 9.2). We measured whole blood viscosity, plasmatic fibrinogen, prothrombin time (PT), activated partial thromboplastin time (aPTT), D-dimer and red cell morphology with Zipursky-Forconi method. Transthoracic and transesophageal echocardiography was performed in all patients to evaluate the presence of SEC in left atrium. We divided all the patients into two groups: the 1st group of 20 patients with SEC and Atrial Fibrillation (AF) in 80% of cases, and the 2nd group of 25 patients without SEC and AF in 31%. Our results show that in patients with SEC there is a statistically significant increase of whole blood viscosity and plasma fibrinogen in comparison with patients without SEC. Red cell morphology in all patients demonstrates a reversed EMI. D-Dimer, was out of the normal range in about ⅓ of the patients in both groups. An analysis of our results points out that in patients with SEC and AF, with a major risk factor for cardioembolic stroke, we have alterations of hemorheologic assessment with an increase of whole blood viscosity and fibrinogen that seems to be caused by an increase of red cells aggregability favoured by fibrinogen. Our conclusions are that SEC in patients with dilatative cardiomyopathy and AF is an important in vivo indicator of hemorheologic imbalance and an important marker for cardioembolic risk stroke evaluation. [ABSTRACT FROM AUTHOR]

Published
2001

45. Blood viscosity and red cell morphology in subjects suffering from cirrhosis before and after treatment with S-Adenosyl-L-Methionine (SAM).

Author

Turchetti, V., Bellini, M.A., Leoncini, F., Petri, F., Trabalzini, L., Guerrini, M., and Forconi, S.

Subjects
BLOOD, VISCOSITY, LIVER cells
Abstract

Alterations of fluidity of the hepatocytic membrane and of the transport related systems are the basis of the cholesteatic syndrome and favour the tissue accumulation of cytotoxic metabolites. S-Adenosyl-L-Methionine (SAM) is a natural molecule which acts as a giver of methylic groups and as an enzymatic activator in several enzymatic actions of transmethylase and of transulphuration and plays a key role in biochemical processes of hepatic cell. The aim of our study was to evaluate the effects of SAM on the restoration of the membrane fluidity and on the hepatic function in general. In studying the fluidity of the cell membrane we evaluated some hemorheological parameters (total blood viscosity and red cell morphology). Fluidity of the red cell membrane is one of the most important elements of red cell rheology. We studied 15 patients (Group A) suffering from micro- and macro-nodular cirrhosis verified through hepatic biopsy, with alcoholic or post-viral causes. We evaluated the values of: blood viscosity (with a cone-plate rheometer by Carri-med), haematocrit, plasma fibrinogen and the erythrocytic morphology at the optical microscope with the Zipursky-Forconi method before and after 7 days of therapy with SAM iv. Data were compared with those of a similar group (Group B) treated with traditional therapy only (hyposodic and hypoprotein diet supplemented with multivitamin preparations, vitamin K in particular, if necessary, and potassium sparing diuretics). We also measured biliary salts, alkaline phosphatase, transaminase and gamma-GT. In the first group we observed a statistically significant reduction of blood viscosity, haematocrit didn't change significantly; biliary salts reduced in a statistically significant way. Evaluation of red cell morphology showed in all cases a pathological percentage (> 15%) of echinocytes and knizocytes which reduced to a mean of 5% after SAM therapy. We observed no further modifications of the other hemorheological parameters.... [ABSTRACT FROM AUTHOR]

Published
2000

47. Identification of a novel RalGDS-related protein as a candidate effector for Ras and Rap1.

Author

Peterson, S N, Trabalzini, L, Brtva, T R, Fischer, T, Altschuler, D L, Martelli, P, Lapetina, E G, Der, C J, and White, G C

Abstract

Although Ras and Rap1 share interaction with common candidate effector proteins, Rap1 lacks the transforming activity exhibited by Ras proteins. It has been speculated that Rap antagonizes Ras transformation through the formation of nonproductive complexes with critical Ras effector targets. To understand further the distinct biological functions of these two closely related proteins, we searched for Rap1b-binding proteins by yeast two-hybrid screening. We identified multiple clones that encode the COOH-terminal sequences of a protein that shares sequence identity with RalGDS and RGL, which we have designated RGL2. A 158-amino acid COOH-terminal fragment of RGL2 (RGL2 C-158) bound to Ras superfamily proteins which shared identical effector domain sequences with Rap1 (Ha-Ras, R-Ras, and TC21). RGL2 C-158 binding was impaired by effector domain mutations in Rap1b and Ha-Ras. Furthermore, RGL2 C-158 bound exclusively to the GTP-, but not the GDP-bound form of Ha-Ras. Finally, coexpression of RGL2 C-158 impaired oncogenic Ras activation of transcription from a Ras-responsive promoter element and focus-forming activity in NIH 3T3 cells. We conclude that RGL2 may be an effector for Ras and/or Rap proteins.

Published
1996

48. Proteome of H. pylori strains with different cagA structural type isolated from patients with gastric carcinoma and controls.

Author

Figura, N., Santucci, A., Trabalzini, L., Paffetti, A., Valassina, M., Valentini, M., Martelli, P., Lusini, P., Roviello, F., Vindigni, C., and Marrelli, D.

Subjects
HELICOBACTER pylori, STOMACH cancer, PROTEOMICS
Abstract

Background: The infection by H. pylori (HP) strains with different structural types of the cagA gene, may determine different risk of gastric carcinoma (GC) development. As post-genomic approach to the study of H. priori is restricted to only a few strains, we carried out a comparative proteome analysis of HP with different cagA structural types, isolated from patients with different pathologies. Methods: The characteristics of the six strains studied and the patients' pathologies are reported in the table. Strains were grown simultaneously and protein extracts were submitted to two-dimensional polyacrylamide gel electrophoresis. Immobiline strips covering a pH range of 3-10 were used for isoelectrofocusing, while a polyacrytamide gel separating proteins in the Mr range of 200-8 kDa was used for the second dimension. The digitalized images of the silver stained gels were qualitatively and quantitatively analyzed by Melanie II 2d-PAGE software (Bio-Rad). Spot intensities were obtained in pixel units and normalized to the total absorbance of the gel. Increasing/decreasing indexes (fold change) were calculated as the ratio of spot intensity (relative volumes). Identification of protein spots was performed by N-terminal microsequencing, gel matching and immunoblotting. Results: We observed: a) a high variability in the expression of proteins; b) sharing of virulence determinants, such as UreB, Cag26, CagA, catalase, UreA, TagD, 26K antigen, HSPs, NapA, etc.; c) a maximal expression of CagA by GC strains, independently of the structural cagA type; d) a quantitatively different expression of CagA in strains from diffuse and intestinal GC; e) a decreased expression of proteins other than CagA in the cagA isogenic mutant. Discussion: the increased CagA expression by GC strains may be used for diagnostic/prognostic purposes. The role of proteins expressed by different cagA structural types is uncertain. [ABSTRACT FROM AUTHOR]

Published
2002

49. Yeast as a model for Ras signalling

Author

Fiorella Belotti, Renata Tisi, Enzo Martegani, Trabalzini, L, Retta, SF, Tisi, R, Belotti, F, and Martegani, E

Subjects
Candida albican, Cell growth, ved/biology, ved/biology.organism_classification_rank.species, pseudohyphal growth, Morphogenesis, Saccharomyces cerevisiae, Cell cycle, Biology, BIO/11 - BIOLOGIA MOLECOLARE, Yeast, Cell biology, mating, Signal transduction, Protein kinase A, Model organism, Gene
Abstract

For centuries yeast species have been popular hosts for classical biotechnology processes, such as baking, brewing, and wine making, and more recently for recombinant proteins production, thanks to the advantages of unicellular organisms (i.e., ease of genetic manipulation and rapid growth) together with the ability to perform eukaryotic posttranslational modifications. Moreover, yeast cells have been used for few decades as a tool for identifying the genes and pathways involved in basic cellular processes such as the cell cycle, aging, and stress response. In the budding yeast S. cerevisiae the Ras/cAMP/PKA pathway is directly involved in the regulation of metabolism, cell growth, stress resistance, and proliferation in response to the availability of nutrients and in the adaptation to glucose, controlling cytosolic cAMP levels and consequently the cAMP-dependent protein kinase (PKA) activity. Moreover, Ras signalling has been identified in several pathogenic yeasts as a key controller for virulence, due to its involvement in yeast morphogenesis. Nowadays, yeasts are still useful for Ras-like proteins investigation, both as model organisms and as a test tube to study variants of heterologous Ras-like proteins.

Published
2014

50. Methods to Study the Ras2 Protein Activation State and the Subcellular Localization of Ras-GTP in Saccharomyces cerevisiae

Author

Enzo Martegani, Sonia Colombo, Trabalzini, L, Retta, SF, Colombo, S, and Martegani, E

Subjects
Fluorescence microscopy, biology, cAMP/PKA pathway, Saccharomyces cerevisiae, BIO/11 - BIOLOGIA MOLECOLARE, biology.organism_classification, Subcellular localization, Yeast, Transport protein, Cell biology, Small G protein, Protein structure, Biochemistry, Active Ra, Small GTPase, Ras2, Signal transduction, Nutrient, Binding domain
Abstract

Ras proteins were highly conserved during evolution. They function as a point of convergence for different signalling pathways in eukaryotes and are involved in a wide range of cellular responses (shift from gluconeogenic to fermentative growth, breakdown of storage carbohydrates, stress resistance, growth control and determination of life span, morphogenesis and development, and others). These proteins are members of the small GTPase superfamily, which are active in the GTP-bound form and inactive in the GDP-bound form. Given the importance of studies on the Ras protein activation state to understand the detailed mechanism of Ras-mediated signal transduction, we provide here a simple, sensitive, and reliable method, based on the high affinity interaction of Ras-GTP with the Ras binding domain (RBD) of Raf1, to measure the level of Ras2-GTP on total Ras2 in Saccharomyces cerevisiae. Moreover, to study the localization of Ras-GTP in vivo in single S. Cerevisiae cells, we expressed a probe consisting of a GFP fusion with a trimeric Ras Binding Domain of Raf1 (eGFP-RBD3), which was proven to be a useful live-cell biosensor for Ras-GTP in mammalian cells. © 2014 Springer Science+Business Media, LLC.

Published
2013
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results