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37 results on '"Ghigo, Dario Antonio"'

4. Doxorubicin-antioxidant multitarget drugs

Author

Chegaev, Konstantin, Riganti, Chiara, Rolando, Barbara, Lazzarato, Loretta, Gazzano, Elena, Guglielmo, Stefano, Ghigo, Dario Antonio, Fruttero, Roberta, and Gasco, Alberto

Published
2013

5. Genome-wide expression analysis identified defects in cell growth, proliferation and viability in SCA28 lymphoblastoid cell lines

Author

Mancini, Cecilia, Roncaglia, P, Brussino, Alessandro, Stevanin, G, LO BUONO, Nicola, Krmac, H, Maltecca, F, Gazzano, Elena, Bartoletti Stella, A., Calvaruso, M. A., Iommarini, L., Cagnoli, Claudia, Forlani, S, Le Ber, I, Durr, A, Brice, A, Ghigo, Dario Antonio, Casari, G, Porcelli, Am, Funaro, Ada, Gasparre, G, Gustincich, S, and Brusco, Alfredo

Published
2013

6. Identification of pathogenic mechanisms of Spinocerebellar Ataxia, type 28 (SCA28)

Author

Mancini, Cecilia, Roncaglia, P, LO BUONO, Nicola, Gazzano, Elena, Bartoletti Stella, A, Mariani, E, Calvaruso, M, Iommarini, L, Brussino, Alessandro, Cagnoli, C., Krmac, H, Stevanin, G, Forlani, S, Funaro, Ada, Durr, A, Porcelli, A, Ghigo, Dario Antonio, Gasparre, G, Gustincich, S, and Brusco, Alfredo

Published
2012

12. Artemisinin induces doxorubicin resistance in human colon cancer cells via calcium-dependent activation of HIF-1α and P-glycoprotein overexpression

Author

Riganti, Chiara, Doublier, Sophie Michelle, Viarisio, D, Miraglia, Erica, Pescarmona, Gianpiero, Ghigo, Dario Antonio, and Bosia, Amalia

Subjects
Antimetabolites, Antineoplastic, calmodulin-dependent kinase II, HIF-1α, P-glycoprotein, Hypoxia-Inducible Factor 1, alpha Subunit, Research Papers, Artemisinins, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Antimalarials, Protein Transport, artemisinin, Doxorubicin, Drug Resistance, Neoplasm, sesquiterpene lactones, Cell Line, Tumor, doxorubicin, colon cancer cells, calcium, Colonic Neoplasms, Humans, Calcium, ATP Binding Cassette Transporter, Subfamily B, Member 1, Phosphorylation, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Sesquiterpenes
Abstract

Artemisinin is an antimalarial drug exerting pleiotropic effects, such as the inhibition of the transcription factor nuclear factor-kappa B and of the sarcoplasmic/endoplasmic reticulum Ca(++)-ATPase (SERCA) of P. falciparum. As the sesquiterpene lactone thapsigargin, a known inhibitor of mammalian SERCA, enhances the expression of P-glycoprotein (Pgp) by increasing the intracellular Ca(++) ([Ca(++)](i)) level, we investigated whether artemisinin and its structural homologue parthenolide could inhibit SERCA in human colon carcinoma HT29 cells and induce a resistance to doxorubicin.HT29 cells were incubated with artemisinin or parthenolide and assessed for SERCA activity, [Ca(++)](i) levels, Pgp expression, doxorubicin accumulation and toxicity, and translocation of the hypoxia-inducible factor, HIF-1alpha.Artemisinin and parthenolide, like the specific SERCA inhibitors thapsigargin and cyclopiazonic acid, reduced the activity of SERCA. They also increased intracellular calcium concentration ([Ca(++)](i)) and Pgp expression and decreased doxorubicin accumulation and cytotoxicity. The intracellular Ca(++) chelator, 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid, and the inhibitor of calmodulin-dependent kinase II (CaMKII) KN93 prevented these effects. CaMKII is known to promote the phosphorylation and the activation of HIF-1alpha, which may induce Pgp. In HT29 cells, artemisinin and parthenolide induced the phosphorylation of HIF-1alpha, which was inhibited by KN93.Our results suggest that artemisinin and parthenolide may act as SERCA inhibitors and, like other SERCA inhibitors, induce resistance to doxorubicin in human colon cancer cells, via the CaMKII-dependent activation of HIF-1alpha and the induction of Pgp.

Published
2009

29. NO donor and biological properties of different benzofuroxans

Author

Medana, Claudio, DI STILO, Antonella, Visentin, Sonia, Fruttero, Roberta, Gasco, Alberto, Ghigo, Dario Antonio, and Bosia, Amalia

Subjects
Male, Benzoxazoles, Dose-Response Relationship, Drug, In Vitro Techniques, Nitric Oxide, Rats, Vasodilation, Norepinephrine, Structure-Activity Relationship, Cytosol, Guanylate Cyclase, Tumor Cells, Cultured, Animals, Nitric Oxide Donors, Rats, Wistar, nitric oxide - NO - benzofuroxans - NO donors, Cyclic GMP, Aorta
Abstract

To investigate the effect of benzofusion on NO donor properties and related biological activities of the furoxan system. The biological properties considered were the ability to increase the cytosolic levels of cGMP in C6 cells and vasodilation.NO donor properties were investigated either in the presence or the absence of cysteine by using the Griess reaction, chemiluminescence, and gas chromatography. Increase of cytosolic cGMP levels were evaluated by radioimmunoassay. Vasodilating activity was assessed on rat aorta strips precontracted with noradrenaline, in the presence and the absence of oxyhemoglobin (HbO2) and methylene blue (MB), respectively.Benzofuroxan and its methyl and cyano derivatives were unable to release NO under the experimental conditions. Generally these compounds displayed feeble vasodilating properties and were able to weakly stimulate soluble guanylate cyclase (sGC). By contrast, benzodifuroxan and benzotrifuroxan were able to produce both NO* and its reduced form NO- , the nitroxyl anion. They displayed potent vasodilating properties and were able to increase cytosolic levels of cGMP in a concentration-dependent manner.The simple benzofuroxans considered here are devoid of the capability to release NO, they weakly stimulate sGC as well as manifest feeble vasodilating properties by a mechanism that does not involve a thiol-induced NO production. By contrast, benzodifuroxan and benzotrifuroxan behave as typical NO donor furoxans.

Published
1999

30. Follicular fluid proteins stimulate nitric oxide (NO) synthesis in human sperm: a possible role for NO in acrosomal reaction

Author

Revelli, Alberto, Soldati, G., Costamagna, C., Pellerey, O., Aldieri, Elisabetta, Massobrio, Marco, Bosia, Amalia, and Ghigo, Dario Antonio

Subjects
Male, omega-N-Methylarginine, Acrosome Reaction, Nitric Oxide, Spermatozoa, Body Fluids, Canavanine, Ovarian Follicle, Fertilization, Citrulline, Humans, Female, Enzyme Inhibitors, Nitric Oxide Synthase
Abstract

Nitric oxide (NO) is a free radical involved in the regulation of several functions of the male genitourinary system. It is produced by neurons and the endothelium and epithelia of reproductive system; it mediates penile erection and regulates sperm motility, viability, and metabolism. Here we show that human spermatozoa exhibit a detectable NO synthase (NOS) activity, measured both as ability of the intact sperm and cell lysate to convert L-[3H]arginine into L-[3H]citrulline and as 24 h accumulation of extracellular nitrite in intact sperm suspensions. NOS activity (identified as an endothelial isoform) was inhibited by L-canavanine and N(G)-monomethyl-L-arginine, and nitrite accumulation was inhibited by the NO scavenger hemoglobin; both enzyme activity and nitrite production were increased by a 24 h incubation of spermatozoa with protein-enriched extracts of human follicular fluid (PFF); a significant increase of citrulline synthesis was observed only after a 4 h incubation with 40% PFF, a time period during which acrosomal reactivity was significantly increased. PFF-induced acrosomal reaction was inhibited by L-canavanine and hemoglobin, and the NO donors sodium nitroprusside (SNP), S-nitroso-N-acetyl-penicillamine (SNAP), and DETA NONOate were able to increase the percentage of reacted spermatozoa. Our results suggest that NO synthesized by human sperm may play a role in follicular fluid-induced acrosomal reaction.

Published
1999

36. [Changes in erythrocyte deformability following changes in oxido-reductive metabolism in diabetes mellitus]

Author

Ghigo, Dario Antonio, Bosia, Amalia, Pagani, A., Pescarmona, Gianpiero, Pagano, G., and Lenti, G.

Subjects
Adult, Osmotic Fragility, Erythrocytes, Diabetes Mellitus, Humans, Sorbitol, Ultrafiltration, Middle Aged, Glutathione, Oxidation-Reduction, NADP, Aged
Abstract

The enhanced sorbitol synthesis in diabetic red blood cells can lead to a depletion of NADPH and, by limiting the amount of GSH produced in the glutathione-reductase step, can make the cell more susceptible to oxidant injury. Diabetic red blood cells have a shortened life span, as shown by the increase of creatine level. The osmotic resistance of diabetic erythrocytes was measured and the erythrocyte flexibility was studied using a filtration method in which the cells were forced, at a constant flow rate, through a polycarbonate membrane with 5-mu pores. The increased osmotic resistance and the impaired flexibility shown by diabetic red blood cells can be induced in normal cells by a treatment with SH-reagents (diamide). This points to a redox state-mediated decrease in deformability and survival of diabetic erythrocytes.

Published
1983

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