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Biomedical subjects

G Solaini

Publications and source records attributed to G Solaini.

At least 37 records · Page 2Linked to original sources
PubMed1991

Polyamines reduce heart injury caused by doxorubicin.

Isolated rat heart was perfused with 18 microM doxorubicin in the recirculating buffer. This treatment resulted in progressive contractile impairment. Aortic flow and minute work (i.e the product of cardiac output and peak systolic pressure) were reduced up to 20 and 29% of basal values, respectively. These parameters were partially restored in hearts perfused with 400 microM spermine, a naturally occurring polyamine, and 18 microM doxorubicin in the recirculating buffer. The results suggest the need for an investigation of the possible antagonistic role of polyamines against anthracycline cardiotoxicity.

Animals↗
PubMed1990

Dietary lipid effects on microsome fatty acid composition of liver and brain, on liver glucose-6-phosphatase, and on brain 5'-nucleotidase activity in the rat.

The effects of incorporation of dietary oils with different n6/n3 ratio and polyunsaturated fatty acids content into rat liver and brain microsomes has been studied. The investigation of membrane fatty acid composition of liver microsomes and that of brain microsomes gave different results. In particular, liver microsomes of rats fed fish oil showed a relatively higher content of 20:5n3 and 22:6n3, and a lower content of 20:4n6. Under these conditions, a reduced glucose-6-phosphatase activity was measured. Brain microsomal fatty acid composition was only slightly affected by dietary lipid intake. The 5'-nucleotidase activity of those particles was similar, although statistically different values were found in fish-oil-fed rats and in olive-oil-fed rats. The effects of membrane fatty acid composition on membrane-bound enzyme activity are discussed.

Journal Article↗
PubMed1990

Does 2-hydroxy-5-nitrobenzyl bromide react with the epsilon-subunit of the mitochondrial F1-ATPase?

The incubation of bovine mitochondrial F1-ATPase with 2-hydroxy-5-nitrobenzyl bromide (HNB), a selective reagent toward tryptophan residues in proteins, produced a concentration dependent inactivation of the enzyme and the covalent binding of 0.88 mol reagent/mol F1. Although HNB is highly specific for tryptophan it has also some reactivity toward cysteine, then a pre-treatment of F1 with several sulphydryl reagents has been performed to make the site of reaction clearer. This pre-treatment had neither effects in the binding stoichiometry nor in the extent of catalytic inhibition, suggesting that readly accessible thiol groups are not involved in the reaction with HNB. Since the only tryptophan bearing polypeptide of the bovine mitochondrial F1-ATPase complex is its smallest subunit, subunit-epsilon, this is the most probable candidate for HNB reaction. Therefore it may be inferred that the intactness and/or the correct conformation of this subunit could be important factor(s) for the multisite ATP hydrolytic activity of the enzyme.

2-Hydroxy-5-nitrobenzyl Bromide↗
PubMed1989

Temperature-induced states of isolated F1-ATPase affect catalysis, enzyme conformation and high-affinity nucleotide binding sites.

Isolated, nucleotide-depleted bovine-heart F1-ATPase exhibits a break in Arrhenius plot with a 2.7-fold increase in activation energy of ATP hydrolysis below 18-19 degrees C. Analysis of intrinsic tyrosine fluorescence and of the circular dichroism of F1-ATPase showed an abrupt and reversible conformational change occurring at the break temperature, characteristic of a structural tightening at low temperature. Analysis of catalytic nucleotide binding sites using fluorescent ADP analog, 3'-O-(1-naphthoyl)adenosine diphosphate did not show any significant change in affinity of nucleotide binding around the transition temperature but the bound fluorophore exerted a more restricted motion and slower rotation at temperature below the break, indicating a change in the mobility of groups in the close neighbourhood. It is concluded that, as a result of temperature, two kinetically distinct states of F1-ATPase are induced, due to a change in enzyme conformation, which influences directly the properties of catalytic nucleotide binding sites.

Adenosine Diphosphate↗
PubMed1989

Spermine antagonizes the binding of adriamycin to the inner membrane of heart mitochondria.

The biologically active polyamine, spermine, has been found to function as a cationic antagonist of adriamycin binding to ox heart submitochondrial particles. This effect is specifically shown by spermine since other cations tested in the same conditions, can antagonize the binding only to a very low extent. Analysis of the adriamycin binding data in the presence of spermine indicate that the polyamine can greatly reduce the total number of binding sites for the anthracycline in submitochondrial particles and it can increase the apparent dissociation constant, whilst it leaves unchanged the degree of cooperativity of the binding. These results provide evidence on previously unexplored effects of spermine, suggesting that this polyamine might be examined as a possible in vivo antagonist of the adriamycin binding to mitochondria.

Animals↗
PubMed1988

Effect of 2-hydroxy-5-nitrobenzyl bromide on proton translocation by the mitochondrial H+-ATPase.

2-Hydroxy-5-nitrobenzyl bromide, a highly reactive reagent towards tryptophan residues in proteins, is shown to activate the passive proton flux through the inner mitochondrial membrane of bovine heart submitochondrial particles (ETPH). When added at low concentrations, the reagent increased both the ATPase activity of the particles and the passive proton transport rate through the membrane. The presence of oligomycin reduced the extent of the 2-Hydroxy-5-nitrobenzyl bromide action on the proton conductivity suggesting that it acted primarily on the H+-ATPase complex. Similar effects were observed on F1-depleted particles, whilst no effect was observed on the isolated F1-ATPase activity. The results suggest that polypeptides bearing tryptophan residues may be involved in the gating function of proton channels of the mitochondrial membrane and this is particularly evident for the F0F1-ATPase complex.

2-Hydroxy-5-nitrobenzyl Bromide↗
PubMed1987

Protective effect of endogenous coenzyme Q on both lipid peroxidation and respiratory chain inactivation induced by an adriamycin-iron complex.

Mitochondria from beef heart have been partially depleted of coenzyme Q by pentane extraction. It has been found that lipid peroxidation induced by an adriamycin-iron complex proceeds at a higher rate in this preparation than in coenzyme Q reincorporated mitochondria. Moreover in coenzyme Q depleted mitochondria both NADH and succinate oxidase activities result more affected. These observations indicate that endogenous coenzyme Q can effectively protect mitochondria from membrane lipid oxidative damage induced by adriamycin-iron and can reduce the inactivation of NADH and succinate oxidases.

Animals↗
PubMed1987

Resolution of the circular dichroism spectra of the mitochondrial cytochrome bc1 complex.

The circular dichroic spectrum of the mitochondrial cytochrome bc1 complex isolated from bovine heart has been resolved into the contributions from the prosthetic groups: cytochrome c1, the 'Rieske' iron-sulphur centre and the two b cytochromes. It is apparent that firstly, the circular dichroism (CD) properties of cytochrome c1 within the bc1 complex differ from those found in the isolated cytochrome c1 and secondly, both the oxidized and reduced b cytochromes exhibit an intense spectrum of bilobic shape, with the wavelengths of the cross-over points closely corresponding to those of the maxima in the optical absorbance spectra. These latter CD features are discussed in relation to the proposed structure of cytochrome b.

Animals↗
PubMed1987

The circular-dichroic properties of the 'Rieske' iron-sulphur protein in the mitochondrial ubiquinol: cytochrome c reductase.

We have studied the c.d. spectra of the 'Rieske' iron-sulphur protein isolated from the ubiquinol: cytochrome c reductase (bc1 complex) of bovine heart mitochondria. Both the oxidized and the reduced form of the 'Rieske' protein display a series of well-resolved c.d. features resembling those reported for the 'Rieske'-type iron-sulphur protein purified from the bacterium Thermus thermophilus [Fee, Findling, Yoshida, Hille, Tarr, Hearshen, Dunham, Day, Kent & Münck (1984) J. Biol, Chem. 259, 124-133]. In particular, the difference spectra, reduced minus oxidized, of both proteins have a distinctive negative band at 497 nm. The c.d. features characteristic of the isolated 'Rieske' protein were found in the dichroic spectra of the whole bc1 complex in the region between 450 and 520 nm. The reduction of the enzyme by ascorbate or ubiquinol is accompanied by the formation of a negative band at about 500 nm that corresponds, in all its c.d. properties, to the specific dichroic absorption of the reduced 'Rieske' iron-sulphur protein.

Animals↗
PubMed1986

The kinetic and structural changes of the mitochondrial F1-ATPase with temperature.

Mitochondrial F1-ATPase shows a break in the Arrhenius plot with an increase of the activation energy below 17 degrees C, this may imply that the F1-ATPase undergoes a conformational change at this temperature. Further, a structural change of the F1-ATPase is indicated by analysis of the intrinsic fluorescence at 307 nm between 33 and 11 degrees C and also by evaluation of the circular dichroism spectra of the enzyme at temperatures below and above the temperature corresponding to the discontinuity of the Arrhenius plot. It is therefore suggested that F1-ATPase exists in two temperature dependent conformational states to which different catalytic properties may be assigned.

Adenosine Triphosphate↗
PubMed1986

Effects of cholesterol on the kinetics of mitochondrial ATPase.

Enrichment of the inner mitochondrial membrane with cholesterol induces an increase in ATPase activity with a decrease in the Km for ATP. Cholesterol also abolishes the discontinuity normally found in the Arrhenius plot of ATPase activity. Since no change is detected in the rate of proton translocation through the ATPase membrane sector, it is concluded that cholesterol incorporation induces changes in the hydrolytic step of ATPase via a conformational change transmitted from the membrane sector to the catalytic sector F1.

Adenosine Triphosphatases↗
PubMed1985

Cardiotoxic effects of adriamycin and mitochondrial oxidation in rat cardiac tissue.

Rats were subjected to chronic treatment with adriamycin (ADR). Significant alterations of ECG tracings were induced, starting from the third week of treatment. These alterations were related to mitochondrial damage of the heart tissue. A decrease of respiration rate in phosphorylating conditions was observed in isolated organelles over a period of three weeks. Meanwhile, adriamycinol (ADRol) concentration in heart extracts increased during chronic treatment.

Animals↗
PubMed1985

Studies on the effects of anthracyclines on mitochondrial respiration in vitro.

Aclacinomycin, 4'-epi-doxorubicin and 4'-epi-tetrahydropyranyl-adriamycin, three novel anthraquinone derivatives under investigation for their antitumour activity, showed an inhibitory effect on the in vitro respiration of mitochondria from rat hearts. The inhibition proved to be concentration-dependent in the range 0.05 to 1.40 mM and both the NADH-oxidase and the succinate oxidase systems were affected to different extents. Among the compounds tested, 4'-epi-tetrahydropyranyl-adriamycin appeared to be the least powerful effector, requiring a significantly higher concentration for 50% inhibition of oxidation than doxorubicin and the other analogues examined.

Aclarubicin↗
PubMed1985

Inhibitory effects of several anthracyclines on mitochondrial respiration and coenzyme Q10 protection.

A set of three novel anthracyclines, active as antitumour agents, has been examined for their possible effects on rat heart mitochondrial respiration. The in vitro inhibiting effects of the compounds have been compared with that of the older doxorubicin. Aclacinomycin was generally more inhibitory than doxorubicin, 4'-epi-doxorubicin and 4'-epi-tetrahydropyranyl-adriamycin, with both succinate and NAD+-linked substrates. Attempts to prevent anthracycline from inhibiting the succinate oxidase activity by means of adding exogenous coenzyme Q10 gave encouraging results, the inhibiting effect being in fact reduced.

Aclarubicin↗
PubMed1984

Spermine binding to submitochondrial particles and activation of adenosine triphosphatase.

Studies on the effects of polyamines on oligomycin-sensitive ATPase activity of ox heart submitochondrial particles showed that, of the polyamines tested, only spermine affected the enzyme activity. Spermine within the physiological concentration range increased the Vmax. of the enzyme, but the Km for ATP was virtually unaffected. Binding studies of [14C]spermine to submitochondrial particles, under the same conditions as used for the ATPase assay, showed that the spermine binds to submitochondrial particles in a co-operative way; Hill plots of the data gave a Hill coefficient of 2 and a Kd of 8 microM. When submitochondrial particles were treated with trypsin, ATPase was not stimulated by spermine and the amount of spermine bound concomitantly was drastically decreased. The ATPase activity of isolated F1-ATPase was not affected by spermine. Removal of the natural protein ATPase inhibitor did not suppress either the stimulation of the ATPase activity by spermine or the spermine binding to the particles. The results obtained suggested that the polyamine binds and acts at the level of the liaison between the coupling factor F1 and the membrane sector F0 of the ATPase complex.

Adenosine Triphosphatases↗
PubMed1984

Myofibrillar ATPase activity of lateral muscle from the catfish and mullet.

The histochemical and biochemical myofibrillar ATPase activities of red and white muscle of the catfish and mullet have been investigated. The histochemical reactions confirmed the typical pattern of red and white muscle and the absence of growing fibers in the white muscle of the mullet. Biochemical assay were used to determine the ATPase activity of red and white muscle myofibrils. Ratios of white muscle activity/red muscle activity were found to 2.2 in the mullet and 2.3 in the catfish. The myofibrillar ATPase activity of mullet was less thermostable than that of catfish but is still in the range for fish leaving in warm waters.

Adenosine Triphosphatases↗