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Biomedical subjects

A Ferri

Publications and source records attributed to A Ferri.

At least 55 records · Page 3Linked to original sources
PubMed1994

Two distinct mechanisms of inhibition of platelets aggregation by acetylsalicylic acid.

The von Willebrand Factor-Ristocetin adduct activates Platelets aggregation and secretion. Acetylsalicylic acid inhibits Platelets activation by two distinct mechanisms indicating that the adduct activates Platelets by triggering at least two distinct intraplatelet metabolic pathways. The first starts from the activation of Phospholipase A-2 that produces Arachidonic acid, which, in turn, undergoes the metabolic pathway leading to Thromboxane A-2; this pathway can be blocked by the intraplatelet Acetylsalicylic acid by irreversible inactivation of Cyclooxygenase but it is insensitive to the extra-platelet Acetylsalicylic acid. The second pathway is triggered by intact von Willebrand Factor, but not by the Acetylsalicylic acid-treated one; it is insensitive to intraplatelet Acetylsalicylic acid and therefore unrelated to the Arachidonic acid metabolism.

Arachidonic Acid↗
PubMed1994

The function of NADPH bound to Catalase.

NADPH bound to each Catalase subunit was replaced by NADP+ or by the dehydrogenases inhibitor 3-amino-pyridine-adenine dinucleotide phosphate (AADP). The comparison of the three enzyme forms with respect to the capability to dismutate H2O2, or to oxidize ethanol by a peroxidation process using peroxoacetic acid, showed that the enzyme activity is approximately unchanged whatever the nucleotide bound. On the contrary, the dismutation of peroxoacetic acid drops to zero when NADPH is replaced either by the oxidized NADP+ or by the inhibitor AADP. The spectral changes induced by peroxoacetic acid at the heme Soret region indicate that the three enzyme types are quickly oxidized to Compound I [FeV(O)] and successively reduced by two monoelectron intramolecular reactions leading to Compound II [FeIV(OH)] and finally to the resting state (FeIII). Therefore NADPH bound to Catalase is not essential to catalyze peroxidation processes or H2O2 dismutation, but it is essential to prevent the enzyme denaturation and to catalyze dismutation of peroxides other than H2O2.

Adenine Nucleotides↗
PubMed1994

[In vivo dosimetry and radiographic confirmation in radiotherapy of Hodgkin's lymphoma].

In September 1991 a protocol for quality control of large shaped irradiation fields was started in our department. In vivo dosimetry with semiconductor detectors was used to measure the absorbed dose and patient positioning was checked with portal films weekly. First, we set a computed dosimetric system yielding dosimetric values in real time and allowing their easy storage. Then, we calibrated the diodes and determined the correction factors for each of them outside standard conditions. Entrance dose, exit dose and midline dose were measured in 62 patients undergoing supradiaphragmatic radiation therapy for Hodgkin's lymphoma. The exist dose was measured weekly to assess treatment repeatability. High agreement was observed between measured and calculated doses; repeatability was also high, since only 6% of exit dose measurements exceeded 5% of the first determination. In 33 patients portal films were obtained in the first treatment session, and thereafter weekly, to assess mispositioning relative to simulation (reproducibility) and from one session to another (repeatability). A small systematic error was detected in both longitudinal (x = -3 mm; SD = 3.7 mm) and transverse (x = -2 mm; SD = 3.4 mm) directions. Statistically significant errors (> 6 mm) were observed in 14% of patients. Reproducibility was excellent. The protocol reported on in this paper not only helps avoid systematic dosimetric and/or positioning errors in the patients, but also helps identify the main causes of uncertainty and thus remove them.

Hodgkin Disease↗
PubMed1992

[Effect of ASA on the interaction of von Willebrand factor with the platelet membrane].

Ristocetin induces a conformational change on von Willebrand Factor (vWF) similar to that due to the interaction with the subendothelium, by which the former can interact with the Glycoprotein-1 B (GPIB) of the platelet membrane and trigger aggregation and granule content secretion. Platelet Rich Plasma (PRP) treated with Acetyl Salicylic Acid (ASA) loses completely the aggregability induced by addition of Ristocetin whereas ASA-treated and successively Washed Platelets (AWP) supplemented with normal plasma (PPP) give an aggregation and a secretory response to Ristocetin similar to that given by PRP; similarly normal Washed Platelets (WP) supplemented with ASA-treated plasma (APPP) give identical aggregation, and secretion by Ristocetin addition. Ours results indicate that the Ristocetin-vWF complex can trigger two distinct intraplatelet metabolic pathways. A first well known way starts from the activation of Phospholipase A-2 (PL-A2), by which arachidonic acid is produced, that, in turn, undergoes the metabolic pathway leading to Thromboxane A-2; this pathway can be blocked by the intraplatelet ASA by irreversible inactivation of Cyclooxygenase, but it is insensitive to the extra-platelet ASA. A second, independent metabolic pathway, can be triggered by intact vWF, but not by the ASA treated one. It is insensitive to intraplatelet ASA and therefore unrelated to the arachidonic acid metabolism. This pathway could start from the activation of Phospholipase C (PL-C).

Aspirin↗
PubMed1990

Action of catalase on peroxyacetic acid. Kinetic studies.

The activity of catalase on peroxoacetic acid was studied by a kinetic point of view. The "inactivation-reactivation" sequence consists in two first order (intramolecular) one-electron redox reactions. In the catalytic cycle, the reaction producing Compound I is, as espected, a second order process rate determined by the enzyme-peroxide adduct formation step, whereas, surprisingly, the reaction restoring the enzyme resting state is a first order process in which the limiting step is the 0-0 linkage breaking inside the Compound I-peroxide adduct.

Animals↗
PubMed1989

Evidence for a factor promoting the conversion of VWF from low and intermediate to high molecular mass polymers on the platelet membrane.

On the membrane surface of resting platelets exists a factor capable of promoting the conversion of plasma von Willebrand factor from low and intermediate molecular mass to high molecular mass polymers. The process is accompanied by a parallel increase in the von Willebrand factor activity. This could be a regulatory system for the molecular mass distribution of von Willebrand factor during its lifetime in plasma. Glycoprotein Ib of the platelet membrane appears not to be involved in the process.

Blood Platelets↗
PubMed1988

Photoexcitation of the methionine-iron bond in iron(III) cytochrome c: bimolecular reaction with NADH.

When iron(III) cytochrome c aqueous solutions containing NADH are irradiated with polychromatic light (wavelength greater than 280 nm), iron(II) cytochrome c and NAD+ in the stoichiometric ratio 2/1 are observed to be the principal reaction products, independently of the presence of oxygen; in addition, a minor process due to direct photodegradation of the nucleotide is observed. The selection of monochromatic 290 nm irradiation light (at which NADH has an absorbance minimum) and an adequate reactant concentration allowed parallel reactions to be minimized and new information to be obtained on the mechanism of the photoredox process. The experimental results are consistent with a reaction mechanism whereby NADH donates one electron to a "reactive intermediate" of the hemoprotein formed from the light-induced methionine-to-iron charge transfer excited state. In this process an NAD. radical is formed which, in deaerated solution, immediately reduces another molecule of the hemoprotein, and is itself oxidized to NAD+. In aerated solution, the NAD. radical rapidly reacts with oxygen to give NAD+ and superoxide O2- anion radical which, in turn, reduces the second iron(III) cytochrome c molecule.

Cytochrome c Group↗
PubMed1985

[Reduction of cytochrome c by NADH induced by light].

We have studied the behaviour of Fe(III) cytochrome c upon irradiation in the 290-360 nm wavelength range either in the presence or in the absence of NADH; in both cases the photoexcitation caused the reduction of the heme iron. When the irradiation was performed in the absence of NADH, the iron reduction was coupled to a non reversible modification in the protein structure; the photoreduction quantum yield was decreasing with the increase of the irradiation wavelength. Irradiation in the presence of NADH gave heme iron reduction coupled to NADH oxidation and the protein resulted finally unmodified; the quantum yield depended on the irradiation wavelength in a way similar to the observed in the absence of NADH, but it was tenfold higher. We propose that in both cases the active species is an electronic excited state of the heme iron.

Animals↗
PubMed1984

Characterization of the ATP-G-actin aggregates formed at low potassium chloride concentration.

The ATP-G-actin aggregates formed by incubation of ATP-G-actin in 7.5 mM-KCl were characterized by electron-microscopical observation, by high-pressure liquid chromatography and by the study of the 1,N6-etheno-ATP-ATP exchange reaction between the free and the actin-bound nucleotide. In 30 mM-KCl the initial rate of the reduced-viscosity increase is found to be directly related to the amount of the aggregates formed in the course of the preincubation in 7.5 mM-KCl.

Actins↗
PubMed1983

The polymerization of actin. A study of the nucleation reaction.

We compared the properties of the nuclei that accumulate in 7.5 mM-KCl in ATP-G-actin solutions and of the oligomers that are formed by sonication of either G-actin or F-actin. We found that the ability of the above species to prime the polymerization of actin decays with different rates. The nuclei are stable in 7.5 mM-KCl (they decay with a rate constant of 1.5 X 10(-3) s -1 at pH 7.8 at 22 degrees C in the absence of KCl). The oligomers formed by sonication of either G-actin or F-actin, once the sonication is stopped, revert to simpler structures or evolve into F-actin, depending on the KCl concentration in which they are kept. In 10.5 mM-KCl at pH 7.8 at 22 degrees C their priming ability decays with a rate constant of 6 X 10(-3) s -1. We propose that the nuclei that form spontaneously in 7.5 mM-KCl are not directly susceptible to elongation. They must first be converted into activated nuclei, which exist in very low concentration at the steady state. The activated nuclei are directly susceptible to elongation, they have a short life and they decay rapidly into the ground state unless the elongation reaction occurs. Sonication displaces the steady-state concentration in favour of the activated state.

Actins↗
PubMed1982

Mechano-chemical energy transduction in biological systems. The effect of mechanical stimulation on the polymerization of actin: a kinetic study.

Mechanical stimulation (forced circulation in narrow tubing) accelerates as much as 10-fold the rate of polymerization of actin. The increase in the rate is proportional to the intensity of the stimulation for flow rates between 0 and 3 cm/s. This supports the hypothesis that a statistical factor (the orientation of the flowing particles) is influenced by the flow. Comparison of the kinetics of the polymerization of resting and of mechanically stimulated actin solutions shows that both the nucleation and the elongation steps are accelerated. It is thus concluded that flow orients not only the oligomeric structures but also the actin monomers. The elongation reaction, also in the flow-stimulated samples, occurs always by the addition of ATP--G-actin (or ATP-containing oligomers) and not by the fusion of ADP-containing oligomeric structures.

Actins↗
PubMed1981

Different polymeric forms of actin detected by the fluorescent probe terbium ion.

The interaction of actin with Tb3+ was studied by following the fluorescence emitted at 545 nm when the protein was excited at 285 nm in the presence of Tb3+. It was shown that, at low ionic strength, each actin monomer binds, at saturation, six Tb3+ with an association constant of 0.8 microM-1. In the presence of 0.1 M KCl the association constant decreases to 0.15 and 0.24 microM-1 at subcritical and overcritical actin concentrations, respectively; the number of the binding sites remains six. When polymeric actin is formed by the addition of 2 mM MgCl2, the association constant drops to 0.008 micro M-1 and the number of the binding sites to four. The lower number of the Tb3+ binding sites (four) in the actin polymerized by MgCl2 as compared to the number of binding sites (six) of the actin polymerized by KCl is taken as evidence of a looser structure of this latter polymer. We have also shown that Tb3+ does not replace 45Ca2+ at the single, "high-affinity" site of G-actin. Removal of this Ca2+, in the presence of Tb3+, destroys the typical G- and F-actin structures.

Actins↗
PubMedDate not supplied

Changes in lymphocyte subsets in depressed HIV-infected patients without antiretroviral therapy.

The authors studied the effects of major depression on lymphocyte subsets by comparing depressed and matched control subjects in a population of HIV-seropositive outpatients not treated with antiretroviral therapy. Twelve patients with major depression, as determined by the Structured Clinical Interview for DSM-III-R, were assessed in comparison with 15 matched nondepressed control subjects. Flow cytometric analysis of peripheral blood lymphocyte subsets together with immunological parameters were performed. In HIV-infected patients, major depression was significantly (P=0.001) associated with a reduction in natural killer cell absolute count and percentage. This report suggests that depression may alter the natural killer cell population that provides a cytotoxic defense against HIV infection.

Adolescent↗