Author: "Assunta Pandolfi" - Searchworks@Jio Institute Digital Library Search Results

134 results on '"Assunta Pandolfi"'

101. Insulin resistance affects gene expression in endothelium

Author: Eugenio Martelli, Arnaldo Ippoliti, Claudia Consoli, Ottavia Porzio, Assunta Pandolfi, Massimo Federici, Diego Arcelli, Agostino Consoli, Renato Lauro, Rossella Menghini, Monica D’Adamo, and G. R. Pistolese
Subjects: medicine.medical_specialty, Umbilical Veins, Settore MED/09 - Medicina Interna, Endothelium, Cells, medicine.medical_treatment, Biology, Settore MED/22 - Chirurgia Vascolare, Settore MED/13 - Endocrinologia, Insulin resistance, Internal medicine, Hyperinsulinism, Gene expression, Genetic model, medicine, Hyperinsulinemia, Humans, Settore MED/49 - Scienze Tecniche Dietetiche Applicate, PI3K/AKT/mTOR pathway, Cells, Cultured, Adaptor Proteins, Signal Transducing, Cultured, Settore M-EDF/01 - Metodi e Didattiche delle Attivita' Motorie, Insulin, Gene Expression Profiling, Signal Transducing, Adaptor Proteins, Endothelial Cells, Settore MED/23 - Chirurgia Cardiaca, Insulin Receptor Substrate Proteins, Gene Expression Regulation, Insulin Resistance, medicine.disease, Insulin receptor, Endocrinology, medicine.anatomical_structure, biology.protein, Cardiology and Cardiovascular Medicine
Abstract: To the editor: We and others have found that either genetic insulin resistance or hyperinsulinemia may dampen insulin ability to activate the PI3-kinase/Akt pathway, leading to perturbation of endothelial nitric oxide synthase (eNOS) activation.1,2 However, little is known about insulin effects on transcription of antiatherogenic and proatherogenic genes in insulin resistant conditions. Therefore, we used a genetic model of vascular insulin resistance, primary human umbilical vein endothelial cells (HUVECs) naturally carrying the G972R Insulin Receptor Substrate-1 (IRS-1) variant,2 to investigate the effect of both genetic insulin resistance and hyperinsulinemia on transcription of atherosclerosis related genes. G972R IRS-1 variant reduces IRS-1 activation of the PI3-K/Akt pathway,3 and it has been associated to coronary artery disease and obesity.3,4 HUVECs carrying the wild-type (WT) or G972R IRS-1 variant were obtained as previously described.3 For the experiments, 3rd through 5th passage HUVEC-WT and 972 were incubated in serum free EGM-2 medium for 16 hours in the presence or absence of insulin 5×10−7 mol/L, to obtain a full effect of insulin on nitric oxide production.5 Total RNA was extracted from the HUVECs with Trizol reagent according to the manufacturer’s protocol. To profile gene expression pattern we made use of U133A Affymetrix DNA microarray containing a total number of 22283 probe sets corresponding to about 15 000 genes, using previously described methods.6 Gene expression profiling was obtained by …
Published: 2008

102. Decreased in vivo oxidative stress and decreased platelet activation following metformin treatment in newly diagnosed type 2 diabetic subjects

Author: Agostino Consoli, Giovanni Ciabattoni, Giovanni Davì, Antonio Nicolucci, Noemi Michetti, Patrizia Di Fulvio, Assunta Pandolfi, Elena A. De Filippis, Tonino Bucciarelli, and Gloria Formoso
Subjects: Blood Glucose, Male, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Type 2 diabetes, medicine.disease_cause, Endocrinology, Internal medicine, Diabetes mellitus, Internal Medicine, medicine, Humans, Hypoglycemic Agents, Insulin, Gliclazide, Platelet activation, Aged, Glucose tolerance test, medicine.diagnostic_test, C-Peptide, business.industry, Glucose Tolerance Test, Middle Aged, medicine.disease, Platelet Activation, Metformin, Oxidative Stress, Diabetes Mellitus, Type 2, Female, business, Oxidative stress, medicine.drug
Abstract: Background In type 2 diabetes, metformin reduces cardiovascular risk beyond the effect of glycaemic control. Since oxidative stress and the consequent enhanced platelet activation contribute to accelerated atherosclerosis in diabetes, we hypothesized that metformin could reduce oxidative stress in this condition. Methods We randomized 26 newly diagnosed type 2 diabetic subjects to assume either metformin (M, n = 13) or gliclazide (G, n = 13) for 12 weeks. Drugs were titrated as needed to achieve good glycaemic control. Before and after treatment, we determined blood glucose, insulin, HbA1c, vitamin A and E levels and 8-iso-PGF2α and 11-dehydro-thromboxane B2 urinary excretion, an in vivo oxidative stress and a thromboxane-dependent platelet activation marker, respectively. Results Notwithstanding a comparable improvement in metabolic control, 8-iso-PGF2α (M from 708 ± 32 to 589 ± 45 pg/mg cr, p < 0.001; G from 646 ± 80 to 665 ± 79, pg/mg cr, p = ns) and 11-dehydro-thromboxane B2 (M from 2190 ± 196 to 1753 ± 150 pg/mg cr, p < 0.05; G from 2048 ± 202 to 1923 ± 223, pg/mg cr, p = ns) urinary excretion decreased after metformin but not after gliclazide treatment. After metformin, vitamin A and E levels significantly increased while they remained unchanged after gliclazide. Conclusions These data suggest that metformin could improve oxidative stress, preserve antioxidant function and restrain platelet activation in type 2 diabetes. Copyright © 2007 John Wiley & Sons, Ltd.
Published: 2007

103. Chronic hyperglicemia and nitric oxide bioavailability play a pivotal role in pro-atherogenic vascular modifications

Author: Assunta Pandolfi and Elena A. De Filippis
Subjects: medicine.medical_specialty, Vascular smooth muscle, Endothelium, Endocrinology, Diabetes and Metabolism, Review, Biology, medicine.disease, biology.organism_classification, Nitric oxide, Endothelial stem cell, chemistry.chemical_compound, Endocrinology, medicine.anatomical_structure, Downregulation and upregulation, chemistry, Enos, Internal medicine, Diabetes mellitus, Genetics, medicine, cardiovascular system, Endothelial dysfunction
Abstract: Diabetes is associated with accelerated atherosclerosis and macrovascular complications are a major cause of morbidity and mortality in this disease. Although our understanding of vascular pathology has lately greatly improved, the mechanism(s) underlying enhanced atherosclerosis in diabetes remain unclear. Endothelial cell dysfunction is emerging as a key component in the pathophysiology of cardiovascular abnormalities associated with diabetes. Although it has been established that endothelium plays a critical role in overall homeostasis of the vessels, vascular smooth muscle cells (vSMC) in the arterial intima have a relevant part in the development of atherosclerosis in diabetes. However, high glucose induced alterations in vSMC behaviour are not fully characterized. Several studies have reported that impaired nitric oxide (NO) synthesis and/or actions are often present in diabetes and endothelial dysfunction. Furthermore, although endothelial cells are by far the main site of vascular NO synthesis, vSMC do express nitric oxyde synthases (NOSs) and NO synthesis in vSMC might be important in vessel's function. Although it is known that vSMC contribute to vascular pathology in diabetes by their change from a quiescent state to an activated proliferative and migratory phenotype (termed phenotypic modulation), whether this altered phenotypic modulation might also involve alterations in the nitrergic systems is still controversial. Our recent data indicate that, in vivo, chronic hyperglycemia might induce an increased number of vSMC proliferative clones which persist in culture and are associated with increased eNOS expression and activity. However, upregulation of eNOS and increased NO synthesis occur in the presence of a marked concomitant increase of O(2-) production. Since NO bioavailabilty might not be increased in high glucose stimulated vSMC, it is tempting to hypothesize that the proliferative phenotype observed in cells from diabetic rats is associated with a redox imbalance responsible quenching and/or trapping of NO, with the consequent loss of its biological activity. This might provide new insight on the mechanisms responsible for accelerated atherosclerosis in diabetes.
Published: 2007

104. Possible role for nitric oxide dysregulation in critical illness myopathy

Author: Pamela Di Tomo, Antonio Di Muzio, Marta Pace, Antonino Uncini, Michele Ragno, Assunta Pandolfi, and Margherita Capasso
Subjects: Adult, Male, medicine.medical_specialty, Critical Illness Myopathy, Nitric Oxide Synthase Type III, Physiology, NOS1, Critical Illness, Nitric Oxide Synthase Type II, Enzyme-Linked Immunosorbent Assay, Nitric Oxide Synthase Type I, Biology, Nitric oxide, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Downregulation and upregulation, Muscular Diseases, Physiology (medical), Internal medicine, Peroxynitrous Acid, Myosin, medicine, Humans, Muscle, Skeletal, Aged, Sarcolemma, Nitrotyrosine, Middle Aged, Endocrinology, Biochemistry, chemistry, Gene Expression Regulation, Female, Neurology (clinical), Nitric Oxide Synthase, Peroxynitrite
Abstract: Muscle fiber inexcitability and myosin loss underlie weakness in critical illness myopathy (CIM). Nitric oxide (NO) takes part in the maintenance of muscle fiber resting potential and, in pathological conditions accompanied by oxidative stress, may damage proteins through peroxynitrite generation. Sepsis and other conditions associated with CIM may differentially affect expression of NO synthases (NOSs), so that both downregulation and upregulation with excessive peroxynitrite production can be hypothesized. In six patients with CIM we studied NOS1, NOS2, and NOS3 protein expression by immunohistochemistry and Western blot. To investigate peroxynitrite production, we performed immunohistochemistry for nitrotyrosine and measured nitrotyrosine levels by enzyme-linked immunosorbent assay. In three patients, sarcolemmal staining for NOS1 was selectively absent. In the others, it was absent in atrophic fibers and absent or reduced in non-atrophic fibers. Total NOS1 protein content was reduced by 41% in patients compared to controls, whereas no significant changes were found in levels and localization of NOS2, NOS3, and nitrotyrosine. Further studies are warranted to determine whether NOS1 loss plays a role in the pathophysiology of CIM, possibly reducing the release of NO at the sarcolemma and affecting muscle fiber excitability. Muscle Nerve, 2007
Published: 2007

105. The prominent role of p38 mitogen-activated protein kinase in insulin-mediated enhancement of VCAM-1 expression in endothelial cells

Author: R. De Caterina, Agostino Consoli, Rosalinda Madonna, Marika Massaro, and Assunta Pandolfi
Subjects: insulin, medicine.medical_treatment, Immunoblotting, Immunology, Vascular Cell Adhesion Molecule-1, Electrophoretic Mobility Shift Assay, Transfection, p38 Mitogen-Activated Protein Kinases, Cell Line, 03 medical and health sciences, 0302 clinical medicine, Insulin resistance, NF-KappaB Inhibitor alpha, Downregulation and upregulation, insulin resistance, medicine, Humans, Hypoglycemic Agents, Immunology and Allergy, ASK1, Enzyme Inhibitors, Phosphorylation, Pharmacology, diabetes, Akt/PKB signaling pathway, Chemistry, Kinase, Insulin, NF-kappa B, Endothelial Cells, Flow Cytometry, medicine.disease, Immunohistochemistry, Up-Regulation, Cell biology, Vascular endothelial growth factor A, MAP kinases, 030220 oncology & carcinogenesis, I-kappa B Proteins, Signal transduction, atherosclerosis, insulin, insulin resistance, MAP kinases, atherosclerosis, diabetes, 030215 immunology
Abstract: Insulin levels are a marker for cardiovascular events, but the link between hyperinsulinemia and atherosclerosis is poorly understood. We previously showed that insulin increases monocyte-endothelial interactions and the endothelial expression of the pro-atherogenic vascular cell adhesion molecule-1 (VCAM-1). The aim of this study is to examine molecular mechanisms involved in the effect of insulin on VCAM-1 expression. Human umbilical vein endothelial cells (HUVEC) were incubated with insulin (0–24 h) ± inhibitors of signaling pathways potentially involved. At pathophysiological concentrations (10−9-10−7 M), insulin selectively induced VCAM-1 expression. The p38mitogen activated protein(MAP) kinase inhibitors SB203580 and SB202190, and partially the c-Jun NH2-terminal kinase (JNK) inhibitor SP600127, decreased insulin effect on VCAM-1. Gene silencing by small interfering RNA significantly reduced the expression of p38MAP kinase, and this was accompanied by suppression of insulin-stimulated VCAM-1 expression. Treatment with insulin also led to the activation of NF-κB and induction of IκB-α phosphorylation, thus accounting for NF-κB translocation into the nucleus. Co-treatment of HUVEC with insulin and SB202190 strongly reverted the stimulatory effect of insulin on NF-κB activation, thus establishing a link between NF-κB activation and p38MAPkinase-mediated induction of VCAM-1 by insulin. In conclusion, pathophysiological insulin concentrations increase VCAM-1 expression and activate NF-κB. This mostly occurs through stimulation of p38MAP kinase.
Published: 2007

106. Osteogenic differentiation of amniotic fluid mesenchymal stromal cells and their bone regeneration potential

Author: Assunta Pandolfi and Caterina Pipino
Subjects: Pathology, medicine.medical_specialty, Histology, business.industry, Mesenchymal stem cell, Clinical uses of mesenchymal stem cells, Amniotic stem cells, Review, Cell Biology, Regenerative medicine, medicine.anatomical_structure, Genetics, Cancer research, medicine, Bone marrow, Stem cell, Bone regeneration, business, Molecular Biology, Genetics (clinical), Stem cell transplantation for articular cartilage repair
Abstract: In orthopedics, tissue engineering approach using stem cells is a valid line of treatment for patients with bone defects. In this context, mesenchymal stromal cells of various origins have been extensively studied and continue to be a matter of debate. Although mesenchymal stromal cells from bone marrow are already clinically applied, recent evidence suggests that one may use mesenchymal stromal cells from extra-embryonic tissues, such as amniotic fluid, as an innovative and advantageous resource for bone regeneration. The use of cells from amniotic fluid does not raise ethical problems and provides a sufficient number of cells without invasive procedures. Furthermore, they do not develop into teratomas when transplanted, a consequence observed with pluripotent stem cells. In addition, their multipotent differentiation ability, low immunogenicity, and anti-inflammatory properties make them ideal candidates for bone regenerative medicine. We here present an overview of the features of amniotic fluid mesenchymal stromal cells and their potential in the osteogenic differentiation process. We have examined the papers actually available on this regard, with particular interest in the strategies applied to improve in vitro osteogenesis. Importantly, a detailed understanding of the behavior of amniotic fluid mesenchymal stromal cells and their osteogenic ability is desirable considering a feasible application in bone regenerative medicine.
Published: 2015
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107. An increased osteoprotegerin serum release characterizes the early onset of diabetes mellitus and may contribute to endothelial cell dysfunction

Author: Riccardo Candido, Assunta Pandolfi, Claudio Celeghini, Federica Corallini, Bruno Fabris, Agostino Consoli, Paola Secchiero, Silvano Capitani, Giorgio Zauli, Secchiero, P., Corallini, F., Pandolfi, A., Consoli, A., Candido, R., Fabris, Bruno, Celeghini, Claudio, Capitani, S., and Zauli, G.
Subjects: musculoskeletal diseases, Blood Glucose, Male, medicine.medical_specialty, Time Factors, Endothelium, Peripheral blood mononuclear cell, Pathology and Forensic Medicine, Diabetes Mellitus, Experimental, NO, Mice, Apolipoproteins E, Osteoprotegerin, Internal medicine, Diabetes mellitus, Medicine, Animals, Humans, Endothelial dysfunction, Aorta, Aged, biology, business.industry, diabetes mellitu, RANK Ligand, osteoprotegerin, diabetes mellitus, endothelial cells, Type 2 Diabetes Mellitus, Middle Aged, medicine.disease, Endothelial stem cell, Mice, Inbred C57BL, medicine.anatomical_structure, Endocrinology, Glucose, Diabetes Mellitus, Type 2, RANKL, biology.protein, Cytokines, Female, Endothelium, Vascular, business, Signal Transduction, Regular Articles
Abstract: Serum osteoprotegerin (OPG) is significantly increased in diabetic patients, prompting expanded investigation of the correlation between OPG production/release and glycemic levels. Serum levels of OPG, but not of its cognate ligand receptor activator of nuclear factor-kappaB ligand (RANKL), were significantly increased in type 2 diabetes mellitus patients compared with healthy blood donors. Serum OPG was also significantly elevated in a subgroup of recently diagnosed diabetic patients (within 2 years). The relationship between serum OPG and diabetes mellitus onset was next investigated in apoE-null and littermate mice. Serum OPG increased early after diabetes induction in both mouse strains and showed a positive correlation with blood glucose levels and an inverse correlation with the levels of free (OPG-unbound) RANKL. The in vitro addition of tumor necrosis factor-alpha to human vascular endothelial cells, but not human peripheral blood mononuclear cells, markedly enhanced OPG release in culture. In contrast, high glucose concentrations did not modulate OPG release when used alone or in association with tumor necrosis factor-alpha. Moreover, the ability of soluble RANKL to activate the extracellular signal-regulated kinase/mitogen-activated protein kinase and endothelial nitric-oxide synthase pathways in endothelial cells was neutralized by preincubation with recombinant OPG. Altogether, these findings suggest that increased OPG production represents an early event in the natural history of diabetes mellitus, possibly contributing to disease-associated endothelial cell dysfunction.
Published: 2006

108. Age-dependent changes in the expression of superoxide dismutases and catalase are associated with ultrastructural modifications in human granulosa cells

Author: M.C. Carbone, Roberto Marci, Donatella Caserta, Pierpaolo Aimola, Annalisa Giardinelli, Anna Maria Ragnelli, Assunta Pandolfi, Carla Tatone, Stefano Falone, and Fernanda Amicarelli
Subjects: Aging, endocrine system, Embryology, medicine.medical_specialty, Granulosa cell, SOD1, reproductive ageing, SOD2, medicine.disease_cause, Superoxide dismutase, Superoxide Dismutase-1, Ovarian Follicle, antioxidant enzymes, Internal medicine, Genetics, medicine, Humans, RNA, Messenger, Molecular Biology, Cells, Cultured, chemistry.chemical_classification, Reactive oxygen species, gene expression, granulosa cells, mitochondria, biology, Superoxide Dismutase, Obstetrics and Gynecology, Cell Biology, Catalase, Lipids, Body Fluids, Oxidative Stress, Endocrinology, Reproductive Medicine, chemistry, Ageing, Enzyme Induction, biology.protein, Female, Reactive Oxygen Species, Infertility, Female, Oxidative stress, Developmental Biology
Abstract: Limited knowledge exists about changes in follicle quality associated with age. The aim of this work was to investigate whether ageing may cause oxidative stress-mediated alterations in human granulosa cells (GCs) from periovulatory follicles. GCs employed in this study were obtained from follicular aspirates of 20 younger women (range 27-32 years) and 20 older women (range 38-41 years) undergoing an IVF treatment. Results obtained from comparative RT-PCR analysis revealed that the mean relative levels of mRNAs coding for superoxide dismutases, Cu, ZnSOD (SOD1), MnSOD (SOD2) and catalase were significantly decreased in women > or =38 years (P < 0.05, Student's t-test). These changes were associated with a reduced expression of SOD1, SOD2 and catalase at the protein level. When examined at an ultrastructural level, most of the GCs from this group showed defective mitochondria and fewer lipid droplets than those observed in the younger group. These results indicate that GCs from older patients suffer from age-dependent oxidative stress injury and are taken as an evidence for reduced defence against reactive oxygen species (ROS) in GCs during reproductive ageing.
Published: 2006

109. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) regulates endothelial nitric oxide synthase (eNOS) activity and its localization within the human vein endothelial cells (HUVEC) in culture

Author: Agostino Consoli, Silvia Sancilio, Roberta Di Pietro, Annalisa Giardinelli, Simone Guarnieri, Sara Di Silvestre, Maria A. Mariggiò, Giorgio Zauli, and Assunta Pandolfi
Subjects: Endothelium, Golgi Apparatus, TRAIL, Apoptosis, Biology, Nitric Oxide, Biochemistry, Nitric oxide, Cell Line, eNOS intracellular localization, endothelial cells, TNF-Related Apoptosis-Inducing Ligand, chemistry.chemical_compound, symbols.namesake, Microtubule, Enos, medicine, Animals, Humans, Enzyme Inhibitors, Molecular Biology, Cytoskeleton, Membrane Glycoproteins, Tumor Necrosis Factor-alpha, Nocodazole, Cell Biology, Golgi apparatus, biology.organism_classification, Cell biology, medicine.anatomical_structure, NG-Nitroarginine Methyl Ester, chemistry, Gene Expression Regulation, Cell culture, symbols, Tumor necrosis factor alpha, Endothelium, Vascular, Nitric Oxide Synthase, Apoptosis Regulatory Proteins
Abstract: We have recently demonstrated that tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) increases endothelial nitric oxide synthase (eNOS) phosphorylation, NOS activity, and nitric oxide (NO) synthesis in cultured human umbilical vein endothelial cells (HUVEC), without inducing apoptotic cell death. Although an important factor that regulates eNOS activity is its localization within the cells, little is known about the role of TRAIL in the regulation of eNOS trafficking among cellular compartments and the cytoskeleton involvement in this machinery. Then, we did both quantitative and semi-quantitative evaluations with biochemical assays and immune fluorescence microscopy in the presence of specific inhibitors of NOS activity as well as of cytoskeletal microtubule structures. In our cellular model, TRAIL treatment not only increased NO levels but also caused a time-dependent NO migration of fluorescent spots from the plasma membrane to the inner part of the cells. In unstimulated cells, most of the eNOS was localized at the cell membranes. However, within 10 min following addition of TRAIL, nearly all the cells showed an increased cytoplasm localization of eNOS which appeared co-localized with the Golgi apparatus at a higher extent than in unstimulated cells. These effects were associated to an increased formation of trans-cytoplasm stress fibers with no significant changes of the microtubule network. Conversely, microtubule disruption and Golgi scattering induced with Nocodazole treatment inhibited TRAIL-increased NOS activity, indicating that, on cultured HUVEC, TRAIL ability to affect NO production by regulating eNOS sub-cellular distribution is mediated by cytoskeleton and Golgi complex modifications.
Published: 2005

110. G972R IRS-1 variant impairs insulin regulation of endothelial nitric oxide synthase in cultured human endothelial cells

Author: Renato Lauro, Agostino Consoli, Assunta Pandolfi, Marina Cardellini, Mario R. Romano, Davide Lauro, Massimo Federici, Giorgio Sesti, Elena A. De Filippis, Rossella Menghini, and Giuliana Pellegrini
Subjects: Enzymologic, Settore MED/09 - Medicina Interna, Arginine, medicine.medical_treatment, Messenger, chemistry.chemical_compound, Phosphatidylinositol 3-Kinases, Enos, Citrulline, Insulin, Phosphorylation, Cells, Cultured, Cultured, Settore M-EDF/01 - Metodi e Didattiche delle Attivita' Motorie, Polymorphism, Genetic, Humans, Proto-Oncogene Proteins c-akt, Protein-Serine-Threonine Kinases, Insulin Receptor Substrate Proteins, Endothelium, Vascular, RNA, Messenger, Proto-Oncogene Proteins, Gene Expression Regulation, Enzymologic, Nitric Oxide Synthase, Nitric Oxide Synthase Type III, Phosphoproteins, Mitogen-Activated Protein Kinases, Signal Transduction, Nitric oxide synthase, Endothelial stem cell, medicine.anatomical_structure, Cardiology and Cardiovascular Medicine, medicine.medical_specialty, Endothelium, Cells, Biology, Protein Serine-Threonine Kinases, Nitric oxide, Genetic, Vascular, Physiology (medical), Internal medicine, medicine, Polymorphism, biology.organism_classification, Endocrinology, Gene Expression Regulation, chemistry, biology.protein, RNA
Abstract: Background— Impaired insulin-mediated vasodilation might contribute to vascular damage in insulin-resistant states. Little is known about insulin regulation of nitric oxide (NO) synthesis in insulin-resistant cells. The aim of this work was to investigate insulin regulation of NO synthesis in human umbilical vein endothelial cells (HUVECs) carrying the IRS-1 gene G972R variant, known to be associated with impaired insulin activation of the PI3-kinase (PI3-K) pathway in transfected cells. Methods and Results— HUVECs were screened for the presence of the G972R-IRS-1 (HUVEC-G972R) variant by restriction fragment length polymorphisms. After 24-hour exposure to 10 −7 mol/L insulin, endothelial NO synthase (eNOS) mRNA (reverse transcription–polymerase chain reaction), eNOS protein levels (Western blotting), and NOS activity (conversion of [ 3 H]arginine into [ 3 H]citrulline) were increased in wild-type HUVECs (HUVEC-WT), whereas they did not change from baseline in HUVEC-G972R. Compared with HUVEC-WT, in HUVEC-G972R after 2 and 10 minutes of insulin stimulation, IRS-1–associated PI3-K activity was reduced by 47% and 32%, respectively; Akt phosphorylation was decreased by 40% at both time points; and eNOS-Ser1177 phosphorylation was reduced by 38% and 51%, respectively. In HUVEC-WT, eNOS-Thr495 phosphorylation decreased after insulin stimulation. In contrast, in HUVEC-G972R, eNOS-Thr495 phosphorylation increased after insulin stimulation and was 40% greater than in HUVEC-WT. Conclusions— Our data demonstrate that genetic impairment of the (IRS)-1/PI3-K/PDK-1/Akt insulin signaling cascade determines impaired insulin-stimulated NO release and suggest that the G972R-IRS-1 polymorphism, through a direct impairment of Akt/eNOS activation in endothelial cells, may contribute to the genetic predisposition to develop endothelial dysfunction and cardiovascular disease.
Published: 2004

111. 40(th) EASD Annual Meeting of the European Association for the Study of Diabetes : Munich, Germany, 5-9 September 2004

Author: S. Artigas, A V Dreval, Mark I. McCarthy, C Watson, Peter H. Bennett, M Quint, Y Ikeda, E Alpert, F Schiele, H Sekihara, Erik Gylfe, P Lowe, J Kuhlmann, Alain Golay, V Longo, Shahidul Alam Khan Akm., L G Mantovani, M Zawodniak-Szalapska, G Winkler, T Harrity, L Virág, U Johne, Kuo S-W., Linda C Tapsell, J Rodriguez, Michel Komajda, K Kankova, Carole A. Cull, M Sporna, E Estilles, U Ribel, M C Spruce, E Buzzigoli, T Prazak, J K McLaughlin, M K Lingohr, M Lim, F Calara, A Siebenhofer, G Meregalli, Roberto Anichini, A D Baron, R Kurashvili, P C Butler, G I Fantus, T. E. De Gooyer, Park Y-M., R. Walther, S Heinrich, Agnieszka Zawiejska, S Mukherjee, Nikolaos Papanas, G Wong, Ian D. Caterson, David M. Maahs, Shuichi Kaneko, Alexandra E. Butler, Francisco Javier Ampudia-Blasco, O N Kong, Attali J-R., C A Hedman, K Oshinyemi, Nicolle Müller, I C Cranston, N Okumus, M V Vlaiculescu, Balasubramanian Ravikumar, W W Cheatham, K Mukasa, K B Biswas, Annunziata Lapolla, Phil McEwan, G Mader, Gilles Chassot, Dragi Anevski, Werner A. Scherbaum, M Donath, C Hesselmann, R A Gandhi, David E. Moller, Ezio Bonifacio, C Garcia, V Ifandi, P Hornnes, Nieuwenhoven Fav., C Puech, S Pérez-Del-Pulgar, Kim S-R., G Hines, C Rubio Terrés, Michael Gaster, N. Hosszufalusi, A Scholze, Andrew A. Young, Stavros Liatis, F Hariri, S Tan, Paul Valensi, Allan E. Karlsen, J Kim, E. Moberg, J Kaiser, L Berman, G Nelson, A Altkrüger, P Kothare, D B Cook, S Doran, G. van Dijk, Shahnaz Shahinfar, Kim C-S., P Stahl, M Manousaki, S Sigrist, S K Lim, M. P. Stern, A Guberti, C Rezzani, J McKenney, Karl Thomaseth, Sofia Carlsson, M Julia, R Brillante, I Rubesova, T Darkow, E Matsumoto, Wendy M. Macfarlane, M Di Martino, G Bardini, Rossella Menghini, D Duhot, E Farcasiu, Annalisa Natalicchio, I Lindner, J Buvat, Christian L. Brand, Harry Dorchy, Iwona Pietrzak, Z T Luo, P Home, M Ekelund, Jesper Gromada, Kristine Færch, F Piarulli, H Kim, R Mentel, Zsuzsanna K. Zsengellér, Dullaart Rpf., Anton Luger, Thomas A. Pearson, V Manicardi, P Rösen, Feng Y-M., R Morganti, Lars Hansen, Demuth H-U., Haruo Kasai, A Shostak, Rudi Steffensen, G Taylor, Markolf Hanefeld, C Santini, E Hamaguchi, Roberto Miccoli, F Storms, M Cooper, Y Lee, Allison E. Aiello, P Smith, T Suehiro, K Treece, M Waluś, Timothy A Welborn, Simone Baltrusch, E Kontela, S Chai, J Crean, H Yokoyama, Johan G. Eriksson, Rafael Hernández Hernández, J Rodríguez-Saldaña, M P Tornero, G Formoso, D. Lovell, E Bingham, A Mylonakis, M Manteghetti, D Fedele, Antonio Martín-Duce, Ralph A. DeFronzo, D Salcedo, Kurt Højlund, Antonio Petrone, Sheu Whh., C Gutierrez, Flavia Pricci, S Kurita, Z G Abbas, M M Benedetti, Philippe A. Halban, Daniel J. Cox, O Ljungkvist, Justine Davies, J Palsgaard, Lars Sjöström, E Bosi, L Janin-Manificat, W. F. Kelly, M. Fernandez, E Colak, O V Mulyarchik, B Kronshage, F Lang, M Erfurth, Takashi Kadowaki, N Jendrike, U Walter, J Wishart, Y. Neye, D Kim, N Furuhashi, M Barsotti, D Florow, L Ke, L Borgquist, N C Jackson, Ffolliott M. Fisher, V Baskar, K Yoshioka, Bryan A. Wolf, G Chabrier, R Skoumal, Livio Luzi, H Kose, I Pharisien, B. Klein, H Winiarska, M C Johnson, L Griffiths, Nonna Kravchun, C Combe, Baptist Gallwitz, J Zdychova, L Skorda, Jorma Ilonen, W Gao, I N Steen, A Terrinoni, P D Ambery, W Kern, C M Kusminski, Cho M-H., Paolo Pozzilli, Louise G. Grunnet, E Schönle, David R Matthews, Robert W. Taylor, Y Cohen, Kim H-S., M P Eccles, N B Tutuncu, D McDowell, Richard M. Bergenstal, K Takamatsu, T Steiner, Jaan Palgi, Valdemar Grill, N Niculescu, G Federici, S Lehto, P. M. McKeigue, M Barone, Michael E. Trautmann, S Smirnov, J Mannion, M Eto, C Rousseau, M Conti, C S Ernest, Antonio Ceriello, D H Schweitzer, Jung E-D., Andreas Festa, Avijit Lahiri, A Shepelkevich, A Murro, A Kollmann, Jonathan R.S. Arch, R Landgraf, Son H-Y., I Engelsberger, E Agardh, S Rodríguez-Mulero, P J Kraml, K Lee, D. F. Du Toit, E Kim, G Fadini, Williams Ajk., Philip Home, M B Antcieferov, C Perlemoine, D Perrea, Song X-L., D Ruggieri, Krister Bokvist, Heidi Sørensen, Bilbao, G Yoshino, J P Taylor, Shen H-M., S M Furier, R Urquhart, J Wohlgelernter, Jianping Weng, T. Baba, Q Hong, C Silva, Castaigne J-P., M Felaco, X X Zhang, M Jaroň, Milla Rosengård-Bärlund, J G Papp, Toshio Miyata, Lervang H-H., Park M-K., I Kinalska, A Long, Oomen Phn., N Kogawa, Ippolita Patrizia Patera, S. Karadeniz, Dinesh Selvarajah, D S Chung, A Wensaas, Richard Imrich, M Recasens, J Ruxer, O Buchea, E Wilpart, S P Stepanenko, Le Ttd., H Ohgawara, Mariaconsuelo Valentini, A Mondok, M Peltonen, Marianne O. 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Jensen, G, Fisher, A, Petrovsky, N, Srikusalanukul, W, Budge, M, Trifunovic zamaklar, D, Zivkovic, M, Jelic, V, Vukomanovic, G, Ristic, A, Seferovic, P, Costa, J, Duarte, S, Manley, S, Sailesh, S, Venkataraman, A, Haider, Y, Groza, I, Oprean, M, Ardelean, A, Morosanu, A, Darkow, T, Vanderplas, A, Mamas, M, Mcelduff, P, Burns, J, Edwards, R, Fitchet, A, Young, R, Gibson, J, Lichiardopol, R, Niculescu, N, Totora, A, Pencea, C, Tomescu, I, Cinteza, M, Manicardi, V, Coscelli, C, Navazio, A, Catellani, E, Michelini, M, Dall'Asta, D, Guberti, A, Piazza, A, Gasparini, E, Pantaleoni, M, Guiducci, U, Manari, A, Sejil, S, Janand delenne, B, Avierinos, J, Habib, G, Labastie, N, Vague, P, Lassmann vague, V, Luźniak, P, Tatoń, J, Wojciechowska Luźniak, A, Zairis, M, Lyras, A, Patsourakos, N, Tsirimbis, V, Foussas, S, Lupón, J, Urrutia, A, Herreros, J, González, B, Coll, R, Altimir, S, Prats, M, Valle, V, Abreu padí, C, Rábago, G, Ivanova, L, Brasacchio, D, Harno, E, Keenan, A, Li, H, Lu, Z, Ke, L, Liu, H, Jeong, I, Chae, M, Choi, M, Yoo, H, Kim, C, Yun, M, Na, M, Kang, Y, Kong, O, Son, S, Kim, I, Tanaka, N, Hosoi, M, Matsuyama, Y, Fukumoto, M, Yamakita, T, Yoshioka, K, Ishii, T, Sato, T, Fujii, S, Aoki, T, Shibata, T, Mizutani, N, Suzuki, J, Fowelin, J, Samuelsson, P, Brandrup wogsen, G, Okumura, K, Tokmakova, A, Staroverova, D, Antcieferov, M, Shutichina, I, Kuntchevich, G, Vriesendorp, T, Morélis, Q, Legemate, D, Schaper, F, Mainas, E, Gkioulmpasanis, I, Panagiotou, I, Vassilikos, G, Skorda, L, Sidira, M, Christoforidou, M, Alaveras, A, Artikis, V, Evdemon, E, Lechleitner, M, Koch, T, Ebenbichler, C, Sturm, W, Moretti, L, Moruzzo, D, Boldrini, E, Pandolfo, C, Kameyama, M, Iwasa, R, Cho, M, Nam, J, Huh, K, Kaplar, M, Paragh, G, Erdei, A, Csongradi, E, Garai, I, Varga, J, Galuska, L, Udvardy, M, Higa, M, Kaneko, Y, Hiroi, N, Koziarska, D, Nowacki, P, Majkowska, L, Luzniak, P, Wojciechowska luźniak, A, Tushuizen, M, Nieuwland, R, Snoeck, D, Sturk, A, Diamant, M, Aguiar, L, Bahia, 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D, Torjesen, P, Kilhovd, B, Berg, T, Sandvik, L, Hanssen, K, Mentink, C, Donchenko, G, Stepanenko, S, Maingrette, F, Deng, H, Lindenmair, A, Freudenthaler, A, Baumgartner parzer, S, Nizheradze, K, Khoruzhenko, A, Tronko, N, Sheu, W, Ou, H, Shen, H, Lin, T, Wu, H, Yang, C, Mogylnytska, L, Schmoelzer, I, Davies, J, Band, M, Struthers, A, Prázný, M, Škrha, J, Kasalová, Z, Neelotpol, S, Jahan, P, Kauschke, S, Harrop, C, Schäfer, A, Widder, J, Eigenthaler, M, Walter, U, Uchimura, I, Ikebukuro, M, Kaibara, M, Hirata, M, Helal, R, Pervin, F, Yang, X, Jansson, P, Nagaev, I, Jack, M, Carvalho, E, Sunnerhagen, K, Cam, M, Cushman, S, Smith, U, Creely, S, Farmer, J, Gustafson, B, Kusminski, C, Krusinova, E, Wohl, P, Klementova, M, Lanska, V, Mcdougall, C, Kelly, I, Abbas, Z, Lutale, J, Archibald, L, Karunajeewa, H, Stingemore, N, Stuccio, G, Mcgechie, D, Muller, L, Hak, E, Goudzwaard, W, Montorsi, F, Homering, M, Sprenger, K, Goldstein, I, Asnaghi, V, Ferrari, G, Rastaldi, M, Gabellini, D, Dell'Antonio, G, Maestroni, A, Ruggieri, D, Luzi, L, Piemonti, L, Zerbini, G, Anafaroglu, I, Tutuncu, N, Sultana, M, Siddiqua, N, Iwasaki, T, Nakajima, A, Yoneda, M, Mukasa, K, Tanaka, S, and Sekihara, H
Subjects: 0303 health sciences, medicine.medical_specialty, business.industry, EASD, Endocrinology, Diabetes and Metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Diabetes mellitus, Family medicine, Internal Medicine, Medicine, business, 030217 neurology & neurosurgery, 030304 developmental biology
Published: 2004

112. Insulin enhances vascular cell adhesion molecule-1 expression in human cultured endothelial cells through a pro-atherogenic pathway mediated by p38 mitogen-activated protein-kinase

Author: R. De Caterina, Agostino Consoli, Assunta Pandolfi, Rosalinda Madonna, and Marika Massaro
Subjects: medicine.medical_specialty, Umbilical Veins, Endothelium, Arteriosclerosis, MAP Kinase Signaling System, Pyridines, Endothelial cells, Cells, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Biology, p38 Mitogen-Activated Protein Kinases, Wortmannin, chemistry.chemical_compound, Insulin resistance, Vascular, Internal medicine, Internal Medicine, medicine, Humans, Insulin, Enzyme Inhibitors, Cells, Cultured, Phosphoinositide-3 Kinase Inhibitors, Cultured, Cell adhesion molecule, Imidazoles, Atherosclerosis, medicine.disease, Intercellular Adhesion Molecule-1, Cell biology, Endothelial stem cell, Androstadienes, medicine.anatomical_structure, Endocrinology, chemistry, Gene Expression Regulation, Mitogen-activated protein kinase, biology.protein, Endothelium, Vascular, Signal transduction, Adhesion molecules, Signal Transduction
Abstract: Although hyperinsulinaemia in Type 2 diabetes in states of insulin resistance is a risk factor for atherosclerotic vascular disease, underlying mechanisms are poorly understood. We tested the hypothesis that insulin increases monocyte-endothelial interactions, which are implicated in atherosclerosis.We treated human umbilical vein endothelial cells with insulin (10(-10) to 10(-7) mol/l) for 0 to 24 h. To dissect potentially implicated signal transduction pathways, we treated endothelial cells with known pharmacological inhibitors of two distinct insulin signalling pathways: the phosphatidylinositol-3'-kinase (PI3'-kinase) inhibitor wortmannin (3 x 10(-8) to 10(-6) mol/l), involved in insulin-induced endothelial nitric oxide synthase stimulation, and the p38 mitogen-activated protein (p38MAP) kinase inhibitor SB-203580 (10(-7) to 2 x 10(-6) mol/l). We measured adhesion molecule expression by cell surface enzyme immunoassays and U937 monocytoid cell adhesion in rotational adhesion assays.At pathophysiological concentrations (10(-9) to 10(-7) mol/l), insulin concentration-dependently induced vascular cell adhesion molecule (VCAM)-1 (average increase: 1.8-fold) peaking at 16 h. By contrast, the expression of intercellular adhesion molecule-1 and E-selectin were unchanged. The effect on VCAM-1 was paralleled by increased U937 cell adhesion. In the absence of cytotoxicity, wortmannin significantly potentiated the effect of insulin alone on VCAM-1 surface expression and monocytoid cell adhesion, whereas SB-203580 (10(-6) mol/l) completely abolished such effects.These observations indicate that insulin promotes VCAM-1 expression in endothelial cells through a p38MAP-kinase pathway, amplified by the PI3'-kinase blockage. This could contribute to explaining the increased atherosclerosis occurring in subjects with hyperinsulinaemia, or in states of insulin resistance, which feature a defective PI3'-kinase pathway.
Published: 2003

113. TRAIL promotes the survival and proliferation of primary human vascular endothelial cells by activating the Akt and ERK pathways

Author: Davide Zella, Arianna Gonelli, Paola Secchiero, Daniela Milani, Assunta Pandolfi, Giorgio Zauli, and Edvige Carnevale
Subjects: MAPK/ERK pathway, Pathology, medicine.medical_specialty, Endothelium, endothelium, Cell Survival, MAP Kinase Signaling System, signalntransduction, inflammation, Inflammation, Apoptosis, Biology, Protein Serine-Threonine Kinases, Receptors, Tumor Necrosis Factor, TNF-Related Apoptosis-Inducing Ligand, Physiology (medical), Proto-Oncogene Proteins, medicine, Humans, Protein kinase B, Cells, Cultured, Mitogen-Activated Protein Kinase 1, Membrane Glycoproteins, Mitogen-Activated Protein Kinase 3, Cell growth, Tumor Necrosis Factor-alpha, NF-kappa B, Endothelial stem cell, Enzyme Activation, medicine.anatomical_structure, Cell culture, Cancer research, Endothelium, Vascular, Signal transduction, medicine.symptom, Mitogen-Activated Protein Kinases, Cardiology and Cardiovascular Medicine, Apoptosis Regulatory Proteins, Cell Adhesion Molecules, Proto-Oncogene Proteins c-akt, Cell Division, Signal Transduction
Abstract: Background— TRAIL protein is expressed in the medial smooth cell layer of aorta and pulmonary artery, whereas endothelial cells express all TRAIL receptors (TRAIL-Rs). Methods and Results— The role of TRAIL/TRAIL-Rs in vascular biology was investigated in primary human umbilical vein endothelial cells (HUVECs) and aortic endothelial cells, which showed comparable surface expression of death (TRAIL-R1 and -R2) and decoy (TRAIL-R3 and -R4) TRAIL-Rs. TRAIL activated the protein kinase Akt in HUVECs, as assessed by Western blot for phospho-Akt. Moreover, experiments performed with a pharmacological inhibitor of the phosphatidylinositol 3-kinase/Akt pathway (LY294002) or a dominant-negative Akt (K179M) demonstrated that TRAIL significantly protected HUVECs from apoptosis induced by trophic withdrawal via Akt and that inhibition of Akt sensitized HUVECs to TRAIL-induced caspase-dependent apoptosis. TRAIL also stimulated the ERK1/2 but not the p38 or the JNK pathways and induced a significant increase in endothelial cell proliferation in an ERK-dependent manner. Conversely, TRAIL did not activate NF-κB or affect the surface expression of the inflammatory markers E-selectin, intercellular adhesion molecule-1, and vascular cell adhesion molecule-1. Conclusions— The ability of TRAIL to promote the survival/proliferation of endothelial cells without inducing NF-κB activation and inflammatory markers suggests that the TRAIL/TRAIL-R system plays an important role in endothelial cell physiology.
Published: 2003

114. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) sequentially upregulates nitric oxide and prostanoid production in primary human endothelial cells

Author: R. Rana, Simone Guarnieri, Giovanni Ciabattoni, Assunta Pandolfi, Paola Secchiero, Arianna Gonelli, Marco Vitale, Roberta Di Pietro, and Giorgio Zauli
Subjects: Time Factors, Physiology, Angiogenesis, medicine.medical_treatment, TNF-Related Apoptosis-Inducing Ligand, Cell Movement, Serine, Enzyme Inhibitors, Phosphorylation, Cells, Cultured, Phosphoinositide-3 Kinase Inhibitors, Sulfonamides, Membrane Glycoproteins, biology, Nitric Oxide Synthase Type III, Cell migration, Up-Regulation, Cell biology, Endothelial stem cell, Nitric oxide synthase, NG-Nitroarginine Methyl Ester, medicine.anatomical_structure, Cytokine, Tumor necrosis factor alpha, tumor necrosis factor–related apoptosis-inducing ligand, nitric oxide, prostanoids, Cardiology and Cardiovascular Medicine, medicine.medical_specialty, Endothelium, Morpholines, Internal medicine, medicine, Humans, Cyclooxygenase Inhibitors, Nitrobenzenes, Tumor Necrosis Factor-alpha, Actins, Enzyme Activation, Endocrinology, Chromones, Prostaglandins, biology.protein, Pyrazoles, Calcium, Endothelium, Vascular, Nitric Oxide Synthase, Apoptosis Regulatory Proteins
Abstract: Endothelial cells express tumor necrosis factor–related apoptosis-inducing ligand (TRAIL) receptors, but the function of TRAIL in endothelial cells is not completely understood. We explored the role of TRAIL in regulation of key intracellular signal pathways in endothelial cells. The addition of TRAIL to primary human endothelial cells increased phosphorylation of endothelial nitric oxide synthase (eNOS), NOS activity, and NO synthesis. Moreover, TRAIL induced cell migration and cytoskeleton reorganization in an NO-dependent manner. TRAIL did not activate the NF-κB or COX-2 pathways in endothelial cells. Instead, TRAIL increased prostanoid production (PGE 2 =PGI 2 >TXA 2 ), which was preferentially inhibited by the COX-1 inhibitor SC-560. Because NO and prostanoids play a crucial role in the state of blood vessel vasodilatation and angiogenesis, our data suggest that TRAIL might play an important role in endothelial cell function.
Published: 2003

115. State-of-the-Art on Basic and Applied Stem Cell Therapy; Stem Cell Research Italy–International Society for Cellular Therapy Europe, Joint Meeting, Montesilvano (PE)–Italy, June 10–12, 2011

Author: Assunta Pandolfi, Umberto Galderisi, and Dario Siniscalco
Subjects: Oncology, medicine.medical_specialty, Cell growth, Cellular differentiation, medicine.medical_treatment, Cell, Cell Biology, Hematology, Stem-cell therapy, Biology, medicine.disease, Regenerative medicine, Cell therapy, medicine.anatomical_structure, Internal medicine, medicine, Stem cell, Spinal cord injury, Developmental Biology
Abstract: Over 160 stem cell-based therapeutic products are undergoing development for the treatment of several diseases, ranging from cardiac and artery diseases to immune and neurodegenerative pathologies, including diabetes, spinal cord injury. Therefore, stem cell therapy plays a key role for developing new cell-based drugs for the future molecular and regenerative medicine. The second meeting organized by Stem Cell Research Italy (SCR Italy) and by the International Society for Cellular Therapy-Europe (ISCT) in Montesilvano/Citta S. Angelo (Pescara)-Italy, on June 10th-12th, 2011, focused on the state-of-the-art of stem cell therapy and associated novel findings on stem cell research ( www.stemcellitaly.org ).
Published: 2012
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116. Plasminogen activator inhibitor type 1 is increased in the arterial wall of type II diabetic subjects

Author: M.M. Alberta, Ester Vitacolonna, D. Cetrullo, A. Calafiore, Assunta Pandolfi, Giuliana Pellegrini, R. Polishuck, Agostino Consoli, and Fabio Capani
Subjects: Male, medicine.medical_specialty, Arteriosclerosis, medicine.medical_treatment, Fibrin, Pathogenesis, chemistry.chemical_compound, Internal medicine, Diabetes mellitus, Fibrinolysis, Plasminogen Activator Inhibitor 1, medicine, Humans, Thrombus, Aged, biology, Vascular disease, business.industry, Arteries, Middle Aged, medicine.disease, medicine.anatomical_structure, Endocrinology, chemistry, Diabetes Mellitus, Type 2, Plasminogen activator inhibitor-1, biology.protein, Female, Cardiology and Cardiovascular Medicine, business, Diabetic Angiopathies, Artery
Abstract: Plasma plasminogen activator inhibitor type 1 (PAI-1) increases in diabetes, and this might contribute to decreased fibrinolysis and accelerated atherosclerosis. Increased PAI-1 levels in the vessel wall could decrease local fibrinolysis and elevate thrombus formation and the unfavorable evolution of atherosclerotic plaques. High glucose increases PAI-1 synthesis in arterial wall cells in culture, and aortic wall PAI-1 levels have been found to be elevated in diabetic animals. However, arterial wall PAI-1 levels have not been investigated in diabetic subjects. Therefore, the aim of this study was to determine the effect of diabetes on PAI-1 levels in the arterial wall. Blood samples and small tissue specimens from the mammary artery were obtained from 11 diabetic and 10 nondiabetic subjects who underwent coronary artery bypass graft surgery. PAI-1 antigen localization in the arterial wall was obtained by immunohisto- chemistry and was read by laser scanning confocal microscopy; plasma fibrinolytic activity was measured by lysis of fibrin plates; and PAI-1 activity was assessed by a chromogenic method. PAI-1-related immunofluorescence was increased in the arterial wall of diabetic patients, whereas plasma fibrinolysis was reduced. These data provide evidence that diabetes is associated with increased PAI-1 in the arterial wall. This might be an important factor for increased cardiovascular risk and unfavorable plaque evolution in diabetes. (Arterioscler Thromb Vasc Biol. 2001;21:1378- 1382.)
Published: 2001

117. Acute hyperglycemia and acute hyperinsulinemia decrease plasma fibrinolytic activity and increase plasminogen activator inhibitor type 1 in the rat

Author: M.M. Alberta, Assunta Pandolfi, Andrea Giaccari, E.A. De Filippis, L Morviducci, A. Buongiorno, Giuliana Pellegrini, C Cilli, Agostino Consoli, and Fabio Capani
Subjects: Male, medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Type 2 diabetes, Fibrin, Rats, Sprague-Dawley, chemistry.chemical_compound, Endocrinology, In vivo, Hyperinsulinism, Internal medicine, insulin resistance, Plasminogen Activator Inhibitor 1, Blood plasma, Fibrinolysis, Internal Medicine, Hyperinsulinemia, Animals, Insulin, Medicine, biology, business.industry, Settore MED/13 - ENDOCRINOLOGIA, General Medicine, Glucose clamp technique, medicine.disease, Rats, Glucose, Diabetes Mellitus, Type 2, chemistry, inflammation, Hyperglycemia, Tissue Plasminogen Activator, Plasminogen activator inhibitor-1, Glucose Clamp Technique, biology.protein, business
Abstract: Decreased plasma fibrinolysis may contribute to accelerated atherothrombosis in diabetes. To observe whether hyperglycemia and hyperinsulinemia, common findings in type 2 diabetes, acutely affect plasma fibrinolysis in vivo, we evaluated plasma fibrinolysis (lysis of fibrin plates, free PAI-1 activity and t-PA activity) in the rat after a hyperglycemic euinsulinemic clamp (n=8), an euglycemic hyperinsulinemic clamp (n=7) or a saline infusion (n=15). Plasma fibrinolytic activity was sharply reduced after both the hyperglycemic and hyperinsulinemic clamps as compared to the respective controls (mean lysis areas on the fibrin plate, 139+/-21 vs. 323+/-30 mm2, p
Published: 2001

118. C-reactive protein: A potential new molecular link between inflammation, thrombosis and vascular cell proliferation?

Author: Assunta Pandolfi
Subjects: Physiology, Cell growth, Monocyte, C-reactive protein, Inflammation, Biology, Blood proteins, medicine.anatomical_structure, Physiology (medical), Immunology, medicine, biology.protein, medicine.symptom, Cardiology and Cardiovascular Medicine, Cell adhesion, Plasminogen activator, Intracellular
Abstract: See article by Cirillo et al. [9] (pages 47–55) in this issue. C-reactive protein (CRP), a pentraxin synthesized in the liver, is a highly conserved pentameric plasma protein that participates in the systemic response to inflammation. In humans, plasma levels of CRP may rise rapidly and markedly (>1000-fold) after an acute inflammatory stimulus and presumably contribute to host defence [1]. On the other hand, although CRP may exert pleiotropic effects, both “pro-inflammatory” [2] and “anti-inflammatory” (reviewed in Ref. [1]), a large number of studies have demonstrated an association between slightly elevated CRP plasma levels (3–10 μg/ml) and increased risk of developing cardiovascular disease in apparently healthy individuals [2]. This suggests that CRP might be not only a simple downstream marker of inflammation but may have a direct role in atherothrombosis. Accumulating evidence suggests that CRP may directly elicit a variety of pro-atherogenic effects in vascular tissue. In particular, it has been reported that CRP stimulates production of interleukin-8 (IL-8), monocyte chemoattractant protein-1 (MCP-1), plasminogen activator inhibitor-1 (PAI-1), intercellular cell adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1) and E-selectin …
Published: 2005
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119. Glucose and insulin independently reduce the fibrinolytic potential of human vascular smooth muscle cells in culture

Author: Assunta Pandolfi, M.B. Donati, Ester Vitacolonna, Agostino Consoli, Fabio Capani, and Licia Iacoviello
Subjects: medicine.medical_specialty, Vascular smooth muscle, Time Factors, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Enzyme-Linked Immunosorbent Assay, Muscle, Smooth, Vascular, Umbilical Arteries, chemistry.chemical_compound, Plasminogen Activators, Diabetes mellitus, Internal medicine, Fibrinolysis, Plasminogen Activator Inhibitor 1, Internal Medicine, medicine, Hyperinsulinemia, Myocyte, Humans, Hypoglycemic Agents, Insulin, Cells, Cultured, business.industry, Osmolar Concentration, Antibodies, Monoclonal, medicine.disease, Blotting, Northern, Endocrinology, Glucose, L-Glucose, chemistry, Tissue Plasminogen Activator, Electrophoresis, Polyacrylamide Gel, Female, business, Plasminogen activator
Abstract: Hyperglycaemia and hyperinsulinaemia have both been related to accelerated atherosclerosis in non-insulin-dependent diabetes mellitus (NIDDM). Plasma fibrinolytic potential is reduced in NIDDM and it is known that glucose and insulin can modulate plasminogen activator inhibitor (PAI-1) and tissue-plasminogen activator (t-PA) secretion and can therefore regulate local fibrinolysis. Vascular smooth muscle cells (vSMC) play an important role in the development of atherosclerotic lesions; however, the role of insulin and glucose in regulating PAI-1 and t-PA production in vSMC is presently not known. Therefore, we cultured arterial vSMC explanted from human umbilical cords and exposed them to increasing concentrations of glucose (5, 12, 20, 27, 35 mmol/l) or insulin (0.1, 0.5, 1, 10 nmol/l) in a serum free medium. After 24 h, PAI-1 and t-PA antigens and activity were evaluated in the culture medium; in cells exposed to 20 mmol/l glucose and to 0.5 nmol/l insulin PAI-1 gene expression was also evaluated. An increase in PAI-1 antigen was observed at each glucose concentration (by 138, 169, 251 and 357 % as compared to 5 mmol/l glucose) which was paralleled by an increase in PAI-1 activity. t-PA concentration was also increased by glucose but its activity was sharply reduced. An increase in PAI-1 antigen was detected at each insulin level (by 121, 128, 156 and 300 % as compared to no insulin). PAI-1 activity was slightly increased at the lowest insulin concentrations but markedly increased by 10 nmol/l insulin. t-PA antigen was also increased by insulin; however, its activity was markedly reduced at each concentration. As compared to control cells, PAI-1 mRNA was increased by 2.5 and 2.0 fold by 20 mmol/l glucose and 0.5 nmol/l insulin, respectively. We conclude that in human vSMC both glucose and insulin can affect the fibrinolytic balance so as to reduce fibrinolytic potential. This might contribute to decreased local fibrinolysis and thereby might accelerate the atherothrombotic process in NIDDM subjects. [Diabetologia (1996) 39: 1425–1431]
Published: 1996

120. Effects of long-term treatment with pioglitazone on cognition and glucose metabolism of PS1-KI, 3xTg-AD, and wild-type mice

Author: Michele Curcio, Manuela Bomba, Elena Silvestri, Assunta Pandolfi, Caterina Pipino, Lorella M.T. Canzoniero, Domenico Ciavardelli, F. Masciopinto, Stefano L. Sensi, N. Di Pietro, A. Di Castelnuovo, Carlo Corona, and Israel Sekler
Subjects: Male, Genetically modified mouse, Cancer Research, medicine.medical_specialty, Time Factors, LDH, glucose metabolism, Immunology, Morris water navigation task, Mice, Transgenic, Carbohydrate metabolism, Mitochondrion, Mice, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Cognition, Alzheimer Disease, Diabetes mellitus, Internal medicine, Lactate dehydrogenase, Medicine and Health Sciences, Presenilin-1, medicine, Animals, Humans, insulin signaling, Pioglitazone, biology, business.industry, neurodegeneration, Life Sciences, Cell Biology, medicine.disease, pioglitazone, mitochondrial complex activity, LDH activated-receptor-gamma, nonsteroidal antiinflammatory drugs, sporadic alzheimers-disease, ppar-gamma, object recognition, diabetes-mellitus, transgenic mice, mouse model, native electrophoresis, insulin-receptors, Disease Models, Animal, Insulin receptor, Glucose, Endocrinology, chemistry, biology.protein, Female, Thiazolidinediones, Original Article, business, medicine.drug
Abstract: In this study, we investigated the effects of long-term (9-month) treatment with pioglitazone (PIO; 20 mg/kg/d) in two animal models of Alzheimer's disease (AD)-related neural dysfunction and pathology: the PS1-KI(M146V) (human presenilin-1 (M146V) knock-in mouse) and 3xTg-AD (triple transgenic mouse carrying AD-linked mutations) mice. We also investigated the effects on wild-type (WT) mice. Mice were monitored for body mass changes, fasting glycemia, glucose tolerance, and studied for changes in brain mitochondrial enzyme activity (complexes I and IV) as well as energy metabolism (lactate dehydrogenase (LDH)). Cognitive effects were investigated with the Morris water maze (MWM) test and the object recognition task (ORT). Behavioral analysis revealed that PIO treatment promoted positive cognitive effects in PS1-KI female mice. These effects were associated with normalization of peripheral gluco-regulatory abnormalities that were found in untreated PS1-KI females. PIO-treated PS1-KI females also showed no statistically significant alterations in brain mitochondrial enzyme activity but significantly increased reverse LDH activity.PIO treatment produced no effects on cognition, glucose metabolism, or mitochondrial functioning in 3xTg-AD mice. Finally, PIO treatment promoted enhanced short-term memory performance in WT male mice, a group that did not show deregulation of glucose metabolism but that showed decreased activity of complex I in hippocampal and cortical mitochondria. Overall, these results indicate metabolically driven cognitive-enhancing effects of PIO that are differentially gender-related among specific genotypes.
Published: 2012
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121. Differences in the glutathione system of cultured aortic smooth muscle cells from young and aged rats

Author: Ettore Porreca, Nicola Martelli, Concetta Di Febbo, Andrea Mezzetti, Andria D'Orazio, Assunta Pandolfi, Franco Cuccurullo, and Andreina Poggi
Subjects: medicine.medical_specialty, Aging, Glutamate-Cysteine Ligase, Glutathione reductase, Aorta, Thoracic, Biology, Muscle, Smooth, Vascular, chemistry.chemical_compound, medicine.artery, Internal medicine, Methionine Sulfoximine, medicine, Thoracic aorta, Animals, Sulfhydryl Compounds, Incubation, Buthionine Sulfoximine, Cells, Cultured, chemistry.chemical_classification, Aorta, Glutathione Peroxidase, Dose-Response Relationship, Drug, Cell growth, Glutathione, Rats, Endocrinology, Glutathione Reductase, chemistry, Cell culture, cardiovascular system, Thiol, Cardiology and Cardiovascular Medicine, Cell Division
Abstract: We studied the relation between the glutathione (GSH) system and cell proliferation in a model of smooth muscle cells (SMC) derived from the thoracic aorta of 4–6-week-old (young) and 15-month-old (aged) rats. SMC from aged rats showed greater levels of total non-protein thiol compounds (T-SH), increased glutathione transferase (GST) and increased glutathione reductase (GSSG-Red) activities compared with cells from young rats. These changes were associated with an increased proliferation rate of SMC from aged rats. To evaluate the role of GSH on cell proliferation better, a specific inhibitor of gamma-glutamyl-cystein synthetase, dl-buthionine- SR -sulphoximine (BSO) was used. BSO showed a dose-dependent inhibition of cell growth, with an IC 50 of 10 −4 M, after 48–72 h of incubation. Removal of BSO restored cell growth, further suggesting a link between GSH levels and vascular cell proliferation. The inhibitory effect of BSO was about two times greater on SMC from young than on SMC from aged rats. BSO showed 56% inhibition on the proliferation of SMC from young rats and 32% inhibition on SMC from aged rats (10 −4 M, 72 h of incubation). A parallel reduction of GSH levels of 38% and 19% for SMC from young and aged rats, respectively, was observed, suggesting that age-related factors may influence the involvement of GSH system in cell proliferation.
Published: 1993

122. We-P11:35 Metformin improves oxidative stress and decreases platelet activation in newly diagnosed type 2 diabetic subjects

Author: Assunta Pandolfi, E.A. De Filippis, Noemi Michetti, Giovanni Ciabattoni, P. Di Fulvio, Giovanni Davì, Fabio Capani, Gloria Formoso, and Agostino Consoli
Subjects: medicine.medical_specialty, business.industry, General Medicine, Newly diagnosed, medicine.disease_cause, Metformin, Endocrinology, Internal medicine, Internal Medicine, medicine, Platelet activation, Cardiology and Cardiovascular Medicine, business, Oxidative stress, medicine.drug
Published: 2006
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123. Mo-W2:5 Increased vascular wall endothelial nitric oxide synthase (ENOS) levels in umbilical cords from gestational diabetic women

Author: Agostino Consoli, S. Di Silvestre, Assunta Pandolfi, P. Di Fulvio, R. La Sorda, Annalisa Giardinelli, M Piantelli, P. Di Tomo, Gloria Formoso, and N. Di Pietro
Subjects: Vascular wall, medicine.medical_specialty, Endothelial nitric oxide synthase, biology, business.industry, General Medicine, biology.organism_classification, Endocrinology, Enos, Internal medicine, Internal Medicine, Gestation, Medicine, Cardiology and Cardiovascular Medicine, business
Published: 2006
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124. We-P11:156 Visceral but not subcutaneous fat reduction is responsible for metabolic improvements (MI) after weight loss (WL)

Author: Agostino Consoli, E. Ciccarone, Merilda Taraborrelli, Assunta Pandolfi, Gloria Formoso, S. Martinotti, M.T. Guagnano, and Armando Tartaro
Subjects: medicine.medical_specialty, business.industry, medicine.medical_treatment, General Medicine, Subcutaneous fat, Endocrinology, Weight loss, Internal medicine, Internal Medicine, medicine, medicine.symptom, Cardiology and Cardiovascular Medicine, business, Reduction (orthopedic surgery)
Published: 2006
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125. 1106-182 Insulin enhances vascular cell adhesion molecule-1 expression in human cultured endothelial cells: A link to the pathogenesis of accelerated atherosclerosis in diabetes

Author: Agostino Consoli, Rosalinda Madonna, Marika Massaro, Raffaele De Caterina, and Assunta Pandolfi
Subjects: Cell adhesion molecule, business.industry, Insulin, medicine.medical_treatment, Soluble cell adhesion molecules, Intercellular adhesion molecule, Cell biology, Vascular endothelial growth factor B, Vascular endothelial growth factor A, Vascular endothelial growth factor C, Immunology, cardiovascular system, medicine, Neural cell adhesion molecule, Cardiology and Cardiovascular Medicine, business, circulatory and respiratory physiology
Published: 2004
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126. Tumor necrosis factor‐related apoptosis‐inducing ligand (TRAIL) regulates endothelial nitric oxide synthase (eNOS) activity and its localization within the human vein endothelial cells (HUVEC) in cultureRoberta Di Pietro and Maria A. Mariggiò contributed equally to this study.

Author: Roberta Di Pietro, Maria A. Mariggiò, Simone Guarnieri, Silvia Sancilio, Annalisa Giardinelli, Sara Di Silvestre, Agostino Consoli, Giorgio Zauli, and Assunta Pandolfi
Published: 2006
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127. Phenotype modulation in cultures of vascular smooth muscle cells from diabetic rats: Association with increased nitric oxide synthase expression and superoxide anion generation.

Author: Assunta Pandolfi, Alfredo Grilli, Carlo Cilli, Antonia Patruno, Andrea Giaccari, Sara Di Silvestre, Maria Anna De Lutiis, Giuliana Pellegrini, Fabio Capani, Agostino Consoli, and Mario Felaco
Subjects: *CELLS, *MUSCLES, *DIABETIC acidosis, *GENETICS
Abstract: Proliferative modification of vascular smooth muscle cell (vSMC) and impaired bioavailability of nitric oxide (NO) have both been proposed among the mechanisms linking diabetes and atherosclerosis. However, diabetes induced modifications in phenotype and nitric oxide synthase(s) (NOS) expression and activity in vSMC have not been fully characterized. In this study, cell morphology, proliferative response to serum, alpha-SMactin levels, eNOS expression and activity, cGMP intracellular content, and superoxide anion release were measured in cultures of vSMC obtained from aorta medial layer of ten diabetic (90% pancreatectomy, DR) and ten control (sham surgery, CR) rats. Vascular SMC from DR showed a less evident hill and valley culture morphology, increased growth response to serum, greater saturation density, and lower levels of α-SMactin. In the same cells, as compared to CR cells, eNOS mRNA levels and NOS activity were increased, while intracellular cGMP level was lower and superoxide anion production was significantly greater. These data indicate that chronic hyperglycemia might induce, in the vascular wall, an increased number of vSMC proliferative clones which persist in culture and are associated with increased eNOS expression and activity. However, upregulation of eNOS and increased NO synthesis occur in the presence of a marked concomitant increase of O2- production. Since NO bioavailabilty, as reflected by cGMP levels, was not increased in DR cells, it is tempting to hypothesize that the proliferative phenotype observed in DR cells is associated with a redox imbalance responsible quenching and/or trapping of NO, with the consequent loss of its biological activity. J. Cell. Physiol. 196: 378385, 2003. © 2003 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]
Published: 2003
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128. Growth of aortic smooth muscle cells from young and adult rats

Author: Andria D'Orazio, Assunta Pandolfi, Andreina Poggi, and Cinzia Gasbarro
Subjects: medicine.medical_specialty, Endocrinology, Smooth muscle, Internal medicine, medicine, Cell Biology, Biology
Published: 1990
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129. Increased Plasma Levels of Platelet-Derived Growth Factor Activity in Patients with Progressive Systemic Sclerosis

Author: Maria Benedetta Donati, Maria Florita, Paolo D. Pigatto, Glanfranco Altomare, Andreina Poggi, and Assunta Pandolfi
Subjects: Systemic disease, medicine.medical_specialty, Platelet-derived growth factor, medicine.medical_treatment, General Biochemistry, Genetics and Molecular Biology, Scleroderma, Cell Line, Pathogenesis, chemistry.chemical_compound, Internal medicine, medicine, Humans, Platelet, Platelet activation, Whole blood, Immunoassay, Platelet-Derived Growth Factor, Scleroderma, Systemic, business.industry, Growth factor, DNA, medicine.disease, Endocrinology, chemistry, Immunology, Biological Assay, business
Abstract: We measured mitogenic activity of whole blood serum and platelet-poor plasma-derived serum of a group of 10 patients with progressive systemic sclerosis and of 8 controls. Mitogenic activity of plasma-derived serum was greater in patients than in controls, in the absence of other signs of platelet activation. This increased activity was inhibited by specific antibodies, anti-platelet derived growth factor, suggesting that circulating levels of platelet-derived growth factor may be present in progressive systemic sclerosis patients. Platelet-derived growth factor, released either by platelets or by monocytes, might play a role in the pathogenesis of scleroderma.
Published: 1989
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130. Transcriptome analysis of human primary endothelial cells (HUVEC) from umbilical cords of gestational diabetic mothers reveals candidate sites for an epigenetic modulation of specific gene expression

Author: Agostino Consoli, A. De Marco, M.C. Palumbo, Fabio Virgili, Sonia Manca, Assunta Pandolfi, Roberto Ambra, Lucia Natarelli, and Guido Leoni
Subjects: Adult, Biology, Bioinformatics, Umbilical vein, Epigenesis, Genetic, Umbilical Cord, Transcriptome, HUVEC, Pregnancy, Gene expression, Human Umbilical Vein Endothelial Cells, Genetics, Humans, Gene Regulatory Networks, Epigenetics, Promoter Regions, Genetic, Gene, Cells, Cultured, Gestational diabetes, DNA Primers, Oligonucleotide Array Sequence Analysis, Fetus, Base Sequence, Gene Expression Profiling, Epigenetic, Molecular Sequence Annotation, DNA Methylation, Cell biology, Diabetes, Gestational, Case-Control Studies, Hyperglycemia, DNA methylation, Female, Reprogramming
Abstract: Within the complex pathological picture associated to diabetes, high glucose (HG) has ". per se" effects on cells and tissues that involve epigenetic reprogramming of gene expression. In fetal tissues, epigenetic changes occur genome-wide and are believed to induce specific long term effects. Human umbilical vein endothelial cells (HUVEC) obtained at delivery from gestational diabetic women were used to study the transcriptomic effects of chronic hyperglycemia in fetal vascular cells using Affymetrix microarrays. In spite of the small number of samples analyzed (n=6), genes related to insulin sensing and extracellular matrix reorganization were found significantly affected by HG. Quantitative PCR analysis of gene promoters identified a significant differential DNA methylation in TGFB2. Use of Ea.hy926 endothelial cells confirms data on HUVEC. Our study corroborates recent evidences suggesting that epigenetic reprogramming of gene expression occurs with persistent HG and provides a background for future investigations addressing genomic consequences of chronic HG. © 2014 Elsevier Inc.
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131. Adherence of uremic erythrocytes to vascular endothelium decreases endothelial nitric oxide synthase expression

Author: Maria Anna De Lutiis, Natalia Di Pietro, Mario Felaco, Mario Bonomini, Luigi Amoroso, Agostino Consoli, Annalisa Giardinelli, Federico Gizzi, Assunta Pandolfi, and Vittorio Sirolli
Subjects: Male, medicine.medical_specialty, Erythrocytes, Endothelium, Nitric Oxide Synthase Type III, Gene Expression, In Vitro Techniques, urologic and male genital diseases, Nitric oxide, chemistry.chemical_compound, uremia, Enos, Internal medicine, medicine, Cell Adhesion, Humans, RNA, Messenger, Endothelial dysfunction, Cells, Cultured, Aged, endothelial nitric oxide synthase, biology, business.industry, Middle Aged, medicine.disease, biology.organism_classification, Nitric oxide synthase, Endothelial stem cell, medicine.anatomical_structure, Endocrinology, chemistry, Nephrology, Cardiovascular Diseases, Case-Control Studies, biology.protein, Kidney Failure, Chronic, Female, Endothelium, Vascular, erythrocyte, Nitric Oxide Synthase, business, Blood vessel
Abstract: Adherence of uremic erythrocytes to vascular endothelium decreases endothelial nitric oxide synthase expression. Background High prevalence of atherosclerotic cardiovascular events accounts for much of the mortality among patients suffering from end-stage renal disease (ESRD). Endothelial dysfunction as a pathogenic mechanism might contribute to increasing the cardiovascular risk of ESRD. Reduced endothelium-dependent vasodilation has consistently been observed in chronic renal failure patients. Since nitric oxide (NO) is the principal endothelium-derived vasodilator, a reduction in the NO bioavailability may be envisaged in ESRD patients. Methods To clarify whether exposure to erythrocytes from ESRD patients might modulate NO release by the endothelium, we evaluated endothelial NO synthase (eNOS) protein levels (Western blot), eNOS mRNA quantity (real-time PCR), and NOS activity (conversion of L-[3H] arginine in L-[3H] citruline) in endothelial cultures stimulated by erythrocytes from healthy subjects and ESRD patients. Results A time-dependent decrease in eNOS protein levels was evident in cultures treated with erythrocytes from ESRD patients. This observation was consistent with the decreased eNOS mRNA quantities induced by erythrocytes from such patients. Moreover, compared to controls, NOS activity exhibited a significant reduction after incubation with erythrocytes from ESRD patients. The observed eNOS reduction induced by erytrocytes from ESRD patients was totally abolished by annexin V, able to mask red blood cell (RBC) surface-exposed phosphatidylserine. Conclusion These findings suggest that adhesion of erythrocytes from ESRD patients to vascular endothelium may cause a decrease in the levels of eNOS mRNA and protein, and inhibition of NOS activity. This might contribute to endothelial dysfunction, and may play a role in the pathogenesis of cardiovascular disease in ESRD patients.
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132. Combined effect of glucose and insulin in stimulating plasminogen activator inhibitor-1 secretion and gene expression in human vascular smooth muscle cells in culture

Author: Assunta PANDOLFI, Di Febbo, C., Baccante, G., Alberta, M. M., Capani, F., Vitacolonna, E., Porreca, E., and Consoli, A.

133. Diabetes mellitus induces decreased plasma fibrinolytic activity and increased tissue synthesis of plasminogen activator inhibitor-1 (PAI-1) in the rat

Author: R. Polishuck, Agostino Consoli, Assunta Pandolfi, Andrea Giaccari, Giuliana Pellegrini, A. Buongiorno, M.M. Alberta, Ester Vitacolonna, L. Morviducci, and Fabio Capani
Subjects: medicine.medical_specialty, biology, business.industry, medicine.medical_treatment, Adipose tissue, Type 2 diabetes, medicine.disease, Fibrin, Staining, chemistry.chemical_compound, Endocrinology, chemistry, Diabetes mellitus, Internal medicine, Plasminogen activator inhibitor-1, Fibrinolysis, medicine, biology.protein, business, Plasminogen activator
Abstract: In diabetes, plasma fibrinolytic activity is decreased while plasma plasminogen activator inhibitor-1 (PAI-1) is increased. Both liver and adipose tissue can synthesize and release PAI-1, but PAI-1 synthesis in these tissues has not been investigated in diabetes. Furthermore, little is known about PAI-1 localization in arterial wall cells of diabetic animals. The aim of this study was to determine the effect of chronic hyperglycemia on plasma fibrinolysis and plasma PAI-1 levels and on liver, adipose tissue and arterial wall PAI-1 content in the rat. We compared plasma fibrinolytic activity (lysis of fibrin plates) and plasma PAI-1 activity (chromogenic assay) in 10 Sprague Dowley 90% pancreatectomized rats (a model of diabetes characterized by normal fasting insulin and the absence of obesity, therefore closely resembling lean type 2 diabetes) and in 15 sham-operated rats. Furthermore, we measured PAI-1-related fluorescence, by immunofluorescent staining and Laser Scanning Confocal Microscopy, in liver, adipose tissue and aortic wall in diabetic and control animals. In the diabetic animals plasma fibrinolytic activity was reduced (lysis areas = 163 ± 23 vs 308 ± 21 mm2, P These data provide evidence that in diabetes mellitus hyperglycemia is associated with increased PAI-1 content in the liver, adipose tissue and in the arterial wall. This suggests that in diabetes the liver and adipose tissue can be important sources for increased plasma PAI-1 and local fibrinolysis can be affected by increased PAI-1 levels in the arterial wall.

134. Osteogenic differentiation of amniotic fluid mesenchymal stromal cells and their bone regeneration potential.

Author: Pipino C and Pandolfi A
Abstract: In orthopedics, tissue engineering approach using stem cells is a valid line of treatment for patients with bone defects. In this context, mesenchymal stromal cells of various origins have been extensively studied and continue to be a matter of debate. Although mesenchymal stromal cells from bone marrow are already clinically applied, recent evidence suggests that one may use mesenchymal stromal cells from extra-embryonic tissues, such as amniotic fluid, as an innovative and advantageous resource for bone regeneration. The use of cells from amniotic fluid does not raise ethical problems and provides a sufficient number of cells without invasive procedures. Furthermore, they do not develop into teratomas when transplanted, a consequence observed with pluripotent stem cells. In addition, their multipotent differentiation ability, low immunogenicity, and anti-inflammatory properties make them ideal candidates for bone regenerative medicine. We here present an overview of the features of amniotic fluid mesenchymal stromal cells and their potential in the osteogenic differentiation process. We have examined the papers actually available on this regard, with particular interest in the strategies applied to improve in vitro osteogenesis. Importantly, a detailed understanding of the behavior of amniotic fluid mesenchymal stromal cells and their osteogenic ability is desirable considering a feasible application in bone regenerative medicine.
Published: 2015
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134 results on '"Assunta Pandolfi"'

101. Insulin resistance affects gene expression in endothelium

102. Decreased in vivo oxidative stress and decreased platelet activation following metformin treatment in newly diagnosed type 2 diabetic subjects

103. Chronic hyperglicemia and nitric oxide bioavailability play a pivotal role in pro-atherogenic vascular modifications

104. Possible role for nitric oxide dysregulation in critical illness myopathy

105. The prominent role of p38 mitogen-activated protein kinase in insulin-mediated enhancement of VCAM-1 expression in endothelial cells

106. Osteogenic differentiation of amniotic fluid mesenchymal stromal cells and their bone regeneration potential

107. An increased osteoprotegerin serum release characterizes the early onset of diabetes mellitus and may contribute to endothelial cell dysfunction

108. Age-dependent changes in the expression of superoxide dismutases and catalase are associated with ultrastructural modifications in human granulosa cells

109. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) regulates endothelial nitric oxide synthase (eNOS) activity and its localization within the human vein endothelial cells (HUVEC) in culture

110. G972R IRS-1 variant impairs insulin regulation of endothelial nitric oxide synthase in cultured human endothelial cells

111. 40(th) EASD Annual Meeting of the European Association for the Study of Diabetes : Munich, Germany, 5-9 September 2004

112. Insulin enhances vascular cell adhesion molecule-1 expression in human cultured endothelial cells through a pro-atherogenic pathway mediated by p38 mitogen-activated protein-kinase

113. TRAIL promotes the survival and proliferation of primary human vascular endothelial cells by activating the Akt and ERK pathways

114. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) sequentially upregulates nitric oxide and prostanoid production in primary human endothelial cells

115. State-of-the-Art on Basic and Applied Stem Cell Therapy; Stem Cell Research Italy–International Society for Cellular Therapy Europe, Joint Meeting, Montesilvano (PE)–Italy, June 10–12, 2011

116. Plasminogen activator inhibitor type 1 is increased in the arterial wall of type II diabetic subjects

117. Acute hyperglycemia and acute hyperinsulinemia decrease plasma fibrinolytic activity and increase plasminogen activator inhibitor type 1 in the rat

118. C-reactive protein: A potential new molecular link between inflammation, thrombosis and vascular cell proliferation?

119. Glucose and insulin independently reduce the fibrinolytic potential of human vascular smooth muscle cells in culture

120. Effects of long-term treatment with pioglitazone on cognition and glucose metabolism of PS1-KI, 3xTg-AD, and wild-type mice

121. Differences in the glutathione system of cultured aortic smooth muscle cells from young and aged rats

122. We-P11:35 Metformin improves oxidative stress and decreases platelet activation in newly diagnosed type 2 diabetic subjects

123. Mo-W2:5 Increased vascular wall endothelial nitric oxide synthase (ENOS) levels in umbilical cords from gestational diabetic women

124. We-P11:156 Visceral but not subcutaneous fat reduction is responsible for metabolic improvements (MI) after weight loss (WL)

125. 1106-182 Insulin enhances vascular cell adhesion molecule-1 expression in human cultured endothelial cells: A link to the pathogenesis of accelerated atherosclerosis in diabetes

126. Tumor necrosis factor‐related apoptosis‐inducing ligand (TRAIL) regulates endothelial nitric oxide synthase (eNOS) activity and its localization within the human vein endothelial cells (HUVEC) in cultureRoberta Di Pietro and Maria A. Mariggiò contributed equally to this study.

127. Phenotype modulation in cultures of vascular smooth muscle cells from diabetic rats: Association with increased nitric oxide synthase expression and superoxide anion generation.

128. Growth of aortic smooth muscle cells from young and adult rats

129. Increased Plasma Levels of Platelet-Derived Growth Factor Activity in Patients with Progressive Systemic Sclerosis

130. Transcriptome analysis of human primary endothelial cells (HUVEC) from umbilical cords of gestational diabetic mothers reveals candidate sites for an epigenetic modulation of specific gene expression

131. Adherence of uremic erythrocytes to vascular endothelium decreases endothelial nitric oxide synthase expression

132. Combined effect of glucose and insulin in stimulating plasminogen activator inhibitor-1 secretion and gene expression in human vascular smooth muscle cells in culture

133. Diabetes mellitus induces decreased plasma fibrinolytic activity and increased tissue synthesis of plasminogen activator inhibitor-1 (PAI-1) in the rat

134. Osteogenic differentiation of amniotic fluid mesenchymal stromal cells and their bone regeneration potential.

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