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152. Nitrogen metabolism during liver regeneration

Author

Lorenzi, M., primary, De Martino, A., additional, Carlucci, F., additional, Tabucchi, A., additional, Porcelli, B., additional, Pizzichini, M., additional, Marinell, E., additional, and Pagani, R., additional

Published
1993
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170. In vitro biocompatibility assessment of poly(#x03B5;-caprolactone) films using L929 mouse fibroblasts

Author

Serrano, M.C., Pagani, R., Vallet-Regí, M., Peña, J., Rámila, A., Izquierdo, I., and Portolés, M.T.

Subjects
*BIOMEDICAL materials, *FIBROBLASTS, *VASCULAR grafts, *ADHESION
Abstract

Biodegradable and biocompatible materials are the basis for tissue engineering. As an initial step for developing vascular grafts, the in vitro biocompatibility of poly(#x03B5;-caprolactone) (PCL), recently suggested for several clinical applications, was evaluated in this study using L929 mouse fibroblasts. Different cellular aspects were analyzed in order to know the cell viability during cell culture on PCL films: adhesion, proliferation, morphology, LDH release and mitochondrial function. Since topography and other surface characteristics of materials play an essential part in cell adhesion, PCL membranes with either smooth or rough surface were prepared, characterized and used to carry out cell cultures. During short culture times, PCL produced a significant stimulation of mitochondrial activity evaluated by reduction of the MTT reagent. The results provide evidences of good adhesion, growth, viability, morphology and mitochondrial activity of cells on PCL films. Therefore, it can be concluded that PCL is a suitable and biocompatible material as a scaffold for vascular graft development. [Copyright &y& Elsevier]

Published
2004
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171. Differential expression of α1 and β subunits of voltage dependent Ca2+ channel at the neuromuscular junction of normal and p/q Ca2+ channel knockout mouse

Author

Pagani, R., Song, M., McEnery, M., Qin, N., Tsien, R.W., Toro, L., Stefani, E., and Uchitel, O.D.

Subjects
*CALCIUM channels, *NEUROPLASTICITY, *EFFERENT pathways, *IMMUNOCYTOCHEMISTRY
Abstract

Voltage-dependent calcium channels (VDCC) have a key role in neuronal function transforming the voltage signals into intracellular calcium signals. They are composed of the pore-forming α1 and the regulatory α2δ, γ and β subunits. Molecular and functional studies have revealed which α1 subunit gene product is the molecular constituent of each class of native calcium channel (L, N, P/Q, R and T type). Electrophysiological and immunocytochemical studies have suggested that at adult mouse motor nerve terminal (MNT) only P/Q type channels, formed by α1A subunit, mediate evoked transmitter release. The generation of α1A-null mutant mice offers an opportunity to study the expression and localization of calcium channels at a synapse with complete loss of P/Q calcium channel. We have investigated the expression and localization of VDCCs α1 and β subunits at the wild type (WT) and knockout (KO) mouse neuromuscular junction (NMJ) using fluorescence immunocytochemistry. The α1A subunit was observed only at WT NMJ and was absent at denervated muscles and at KO NMJ. The subunits α1B, α1D and α1E were also present at WT NMJ and they were over- expressed at KO NMJ suggesting a compensatory expression due to the lack of the α1A. On the other hand, the β1b, β2a and β4 were present at the same levels in both genotypes. The presence of other types of VDCC at WT NMJ indicate that they may play other roles in the signaling process which have not been elucidated and also shows that other types of VDCC are able to substitute the α1A subunit, P/Q channel under certain pathological conditions. [Copyright &y& Elsevier]

Published
2004
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173. Threonine Aldolase and Allothreonine Aldolase in Rat Liver.

Author

Riario-Sforza, G., Pagani, R., and Marinello, E.

Subjects
*AMINO acids, *HYDROLYSIS, *PROTEINS, *ACETALDEHYDE, *ENZYMES, *LIVER, *RATS
Abstract

The aldol breakdown of L-threonine and L-allothreonine in rate liver is catalyzed by systems localized in the soluble fraction of the homogenate. 2. Evidence in presented that two different enzymes, indicated as ‘threonine aldolase’ and lsquo;allothreonine aldolase’, are involved in the breakdown of the two amino acids. [ABSTRACT FROM AUTHOR]

Published
1969
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174. The binding ofEscherichia coliendotoxin to isolated rat hepatocytes

Author

Ángel Manuel Gento Municio, María Teresa Portolés, and Pagani R

Subjects
Lipopolysaccharides, Male, Cell Survival, Chemistry, Biophysics, Cell Biology, Glucagon, medicine.disease_cause, Biochemistry, Rats, Microbiology, Endotoxins, Liver, Structural Biology, Escherichia coli, Lactates, Genetics, medicine, Animals, Lactic Acid, Molecular Biology
Published
1981

175. Effect ofEscherichia coli lipopolysaccharide on the microviscosity of liver plasma membranes and hepatocyte suspensions and monolayers

Author

Pagani R, Ángel Manuel Gento Municio, María Teresa Portolés, and Inés Díaz-Laviada

Subjects
Lipopolysaccharides, Lipopolysaccharide, Membrane Fluidity, Clinical Biochemistry, Fluorescence Polarization, In Vitro Techniques, medicine.disease_cause, Biochemistry, Microviscosity, chemistry.chemical_compound, Escherichia coli, medicine, Animals, Viscosity, Cell Membrane, Temperature, Rats, Inbred Strains, Biological activity, Cell Biology, General Medicine, Rats, medicine.anatomical_structure, Membrane, Liver, chemistry, Cell culture, Hepatocyte, Biophysics, lipids (amino acids, peptides, and proteins), Fluorescence anisotropy
Abstract

The fluorescence probe 1,6‐diphenylhexa‐1,3,5‐triene (DPH) was used for monitoring structural perturbations induced by lipopolysaccharide (LPS) of Escherichia coli (0111 : B4) in plasma membranes of rat liver. Changes in microviscosity were observed in plasma membrane preparations from control rats after treatment with LPS and in plasma membrane preparations from liver perfused with LPS. In both systems fluorescence polarization was measured from which microviscosity was calculated. This parameter increases with LPS treatment. From temperature dependence studies was inferred that LPS interaction with plasma membrane preparations induces an increase of both the polarization term (r0/r–1)−1 and flow activation energy (ΔE). Addition of LPS to hepatocyte suspensions also induces an increase on microviscosity and a delay in the fall of microviscosity induced by a temperature rise in hepatocyte monolayers grown on microcover slides. These data suggest that LPS interaction can be attributed to its binding to membrane hydrophobic regions in a non‐specific manner. Copyright © 1987 John Wiley & Sons Ltd.

Published
1987

177. Threonine Aldolase and Allothreonine Aldolase in Rat Liver

Author

Pagani R, G. Riario‐Sforza, and Enrico Marinello

Subjects
Threonine, Fructose-bisphosphate aldolase, Centrifugation, Mitochondria, Liver, Biochemistry, Threonine aldolase, Chlorides, Microsomes, Animals, Chemical Precipitation, Amino Acids, Edetic Acid, Aldehyde-Lyases, Cell Nucleus, chemistry.chemical_classification, biology, Aldolase B, Aldolase A, Temperature, Mercury, Hydrogen-Ion Concentration, Molecular biology, Rats, Amino acid, Kinetics, Enzyme, Liver, Solubility, chemistry, Serine hydroxymethyltransferase, biology.protein, Lysosomes
Abstract

1 The aldol breakdown of l-threonine and l-allothreonine in rat liver is catalyzed by systems localized in the soluble fraction of the homogenate. 2 Evidence in presented that two different enzymes, indicated as “threonine aldolase” and “allothreonine aldolase”, are involved in the breakdown of the two amino acids

Published
1969

180. The microviscosity of liver plasma membranes of rats fed with oleoylanilide

Author

Pagani, R, Portoles, M T, Gavilanes, F G, Garcia-Barreno, P, and Municio, A M

Abstract

Oleoylanilide was administered orally to groups of rats according to different patterns. Oleoylanilide was perfused at different concentrations through rat liver. Oleoylanilide was added to isolated hepatocytes. Oleoylanilide was added to plasma-membrane preparations. Membrane preparations were obtained after experiments performed in vivo and perfusion experiments and, by using 1,6-diphenylhexa-1,3,5-triene as fluorescence probe, the fluorescence polarization parameter was measured, from which the microviscosity (eta) was calculated. In all cases the microviscosity decreased markedly. Addition of oleoylanilide to hepatocyte preparations and to isolated membranes produced the same effect, increasing the fluidity of the membranes. These data suggest that oleoylanilide partitions into the membrane, disordering some lipid interactions.

Published
1984
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195. Involvement of cytochrome b5 in the cytotoxic response to Escherichia coli lipopolysaccharide

Author

Ángel Manuel Gento Municio, María Teresa Portolés, Pagani R, Ainaga Mj, and Inés Díaz-Laviada

Subjects
Lipopolysaccharides, Male, Lipopolysaccharide, Clinical Biochemistry, medicine.disease_cause, Microbiology, chemistry.chemical_compound, Mice, Biosynthesis, Cytochrome P-450 Enzyme System, Detoxification, Cytochrome b5, medicine, Escherichia coli, Cytotoxic T cell, Animals, Molecular Biology, Cells, Cultured, biology, L-Lactate Dehydrogenase, Cell Membrane, Cytochrome P450, Rats, Inbred Strains, Cell Biology, General Medicine, Cytochrome b Group, Shock, Septic, Rats, Endotoxins, Cytochromes b5, Biochemistry, chemistry, biology.protein, Microsome, Microsomes, Liver
Abstract

Cytotoxic lesions, induced by Gram-negative lipopolysaccharides (LPS), occur mainly in liver where the microsomal compartment of hepatocytes is involved in the detoxification mechanisms as well as in the biosynthesis of different active metabolites. The alterations induced by LPS from E. coli 0111:B4 on cytochrome b5 and its correlation with cytochrome P450, have been studied using an in vivo reversible endotoxic shock model and 24 h non-replicative hepatocyte monolayers. Results show that cytochrome b5 is directly affected by LPS that induces also a membrane damage with an active release of lactate dehydrogenase (LDH). The increase of cytochrome b5 levels may enhance the efficiency of the electron transport, thus facilitating the cytochrome P450-associate oxidations and reactions involved in the repair mechanisms of membranes.

Published
1989

197. Blood chemistry of rats pretreated with <TOGGLE>Mucuna Pruriens</TOGGLE> seed aqueous extract MP101UJ after <TOGGLE>Echis carinatus</TOGGLE> venom challenge

Author

Aguiyi, J. C., Guerranti, R., Pagani, R., and Marinello, E.

Abstract

The effect of a lethal Echis carinatus venom on serum enzyme levels and blood plasma coagulation parameters in rats pretreated with Mucuna pruriens seed aqueous extract MP101UJ (21 mg/kg body wt) 24 h and 3 wk before i.p venom injection (0.50 mg/kg rat) and rats injected with venom alone (0.50 mg/kg body wt) was investigated. The enzyme levels and coagulation parameter levels were measured 4 h after venom administration. The results showed that the increased enzymes lactate dehydrogenase (LDH), glutamic pyruvic transaminase (SGPT), creatinine kinase (CK) and changed coagulation parameters D-Dimer and Quick levels due to the venom effect were inhibited by M. pruriens seed aqueous extract MP101UJ in pretreated rats. Rats pretreated with a single dose (21 mg/kg and multiple doses 21 mg/kg rat) of extract MP101UJ maintained the normal enzyme levels and showed an anticoagulant effect as evidenced by the high PTT level which was also observed in venom treated animals. D-Dimer and Quick values were normal. However, the extract MP101UJ appeared to significantly inhibit the lethal venom induced myotoxic, cytotoxic and coagulation activities in experimental animals. Copyright © 2001 John Wiley & Sons, Ltd.

Published
2001
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198. Blood chemistry of rats pretreated with Mucuna Pruriensseed aqueous extract MP101UJ after Echis carinatusvenom challenge

Author

Aguiyi, J. C., Guerranti, R., Pagani, R., and Marinello, E.

Abstract

The effect of a lethal Echis carinatusvenom on serum enzyme levels and blood plasma coagulation parameters in rats pretreated with Mucuna pruriensseed aqueous extract MP101UJ (21 mg/kg body wt) 24 h and 3 wk before i.p venom injection (0.50 mg/kg rat) and rats injected with venom alone (0.50 mg/kg body wt) was investigated. The enzyme levels and coagulation parameter levels were measured 4 h after venom administration. The results showed that the increased enzymes lactate dehydrogenase (LDH), glutamic pyruvic transaminase (SGPT), creatinine kinase (CK) and changed coagulation parameters D‐Dimer and Quick levels due to the venom effect were inhibited by M. pruriensseed aqueous extract MP101UJ in pretreated rats. Rats pretreated with a single dose (21 mg/kg and multiple doses 21 mg/kg rat) of extract MP101UJ maintained the normal enzyme levels and showed an anticoagulant effect as evidenced by the high PTT level which was also observed in venom treated animals. D‐Dimer and Quick values were normal. However, the extract MP101UJ appeared to significantly inhibit the lethal venom induced myotoxic, cytotoxic and coagulation activities in experimental animals. Copyright © 2001 John Wiley & Sons, Ltd.

Published
2001
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