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Biomedical subjects

A Finazzi Agro

Publications and source records attributed to A Finazzi Agro.

8 recordsLinked to original sources
PubMed1999

Lipid peroxidation and polyamine metabolism in K562 cells subjected to altered gravity.

The mechanisms underlying cell sensitivity to the gravistimulus are still largely unknown. Recently, the oxidation of membrane lipids and the alteration of polyamine content have been shown to be involved in several cellular processes, from cell growth and differentiation, to aging and resistance to (a)biotic stress. Such an involvement was mediated by the modification of the activity and expression of lipoxygenase (LOX; E.C. 1.13.11.12) and diamine oxidase (DAO; E.C. 1.4.3.6), the enzymes which control membrane properties (LOX) and the catabolism of polyamines (DAO), respectively. In this study, the possible effects of altered gravity on membrane lipid peroxidation and polyamine metabolism were investigated, by subjecting human erythroleukemia K562 cell cultures to simulated hypogravity (by clinorotation) or hypergravity (by centrifugation).

Amine Oxidase (Copper-Containing)↗
PubMed1998

Altered gravity modulates 5-lipoxygenase in human erythroleukemia K562 cells.

Mammalian lipoxygenases catalyse the first committed step in the so-called "arachidonate cascade", leading to the production of potent bioactive molecules, such as leukotrienes, lipoxins and hepoxilins. Leukotrienes interact with G protein-couple receptors involved in neuronal plasticity and T lymphocyte activation, lipoxins activate leukocytes, hepoxilines control the insulin release and stimulate the phospholipase C. Lipoxygenase (linoleate:oxygen oxidoreductase; E.C. 1.13.11.34; 5-LOX) are responsible for lymphocyte maturation and programmed death (apoptosis) of neuronal cells. Therefore, 5-LOX might be Space relevant, because among the most striking effects of Space enviroment are indeed those on T lymphocyte activation, neuronal cell growth and suspectedly apoptosis. In this study, the possible effects of the force of gravity on the activity and expression of 5-LOX have been investigated by subjecting human erythroleukemia K562 cells to simulated hypogravity or hypergravity.

Arachidonate 5-Lipoxygenase↗
PubMed1997

Ozone stress modulates amine oxidase and lipoxygenase expression in lentil (Lens culinaris) seedlings.

The effect of ozone stress on polyamine metabolism and membrane lipid peroxidation in lentil seedlings through the amine oxidase and lipoxygenase activity and expression has been investigated. Ozone is shown to control the expression of these enzymes at the transcriptional level, down-regulating the amine oxidase gene and up-regulating the lipoxygenase gene. The decrease of amine oxidase activity correlated with the increase of putrescine concentration in the ozone-treated plantlets, whereas the increase of lipoxygenase activity was paralleled by enhanced membrane lipid peroxidation. Finally, polyamines are shown to inhibit lipoxygenase activity in lentils.

Amine Oxidase (Copper-Containing)↗
PubMed1977

The fine structure of luminescence spectra of azurin.

The spectra of azurin absorption, fluorescence, phosphorescence and fluorescence excitation have been measured in aqueous solutions at ordinary and liquid nitrogen temperatures. The fluorescence spectra of azurin even at ordinary temperatures have a well resolved fine vibrational structure. The frequency analysis reveals practically the same wave number distances between the main structure peaks in fluorescence spectra at room and low temperatures and in phosphorescence spectra. The comparison of the protein absorption and excitation spectra shows that all the energy absorbed by tyrosine residues is transferred onto indole chromophore. These data suggest an unusual tryptophan environment in this protein, which is characterized by the absence of any hydrogen bonding or other polar interaction of tryptophan with its environment. The problem of the possibility of contributions of two electronic transitions (1La in equilibrium A and 1Lb in equilibrium A) in absorption and emission spectra of azurin tryptophan arising from their mirror symmetry is discussed.

Azurin↗
PubMed1975

Selenium binding to beef-kidney rhodanese.

The reaction of beef kidney rhodanese with selenosulfate was studied. The selenium-treated enzyme shows an absorption spectrum with a maximum at 375 nm attributable to a sulfoselenide group. This absorption is bleached by addition of cyanide. After cyanide treatment stoichiometric amount of selenocyanate can be found. The intrinsic fluorescence of rhodanese is quenched by addition of stoichiometric selenosulfate. This effect can be reversed by cyanide or sulfite but not by selenite or glutathione. By comparison with model complexes the selenium-rhodanese intermediate was identified as a cysteinyl-selenium derivative.

Animals↗
PubMed1975

The effect of azide on the spectral and catalytic properties of ascorbate oxidase.

(1) 45% of the total copper of green zucchini ascorbate oxidase is EPR-detectable. At least two species of copper are present, one with a small A parallel (Type 1) and one with a large A parallel (Type 2). Computer simulated spectra indicated 50% contribution by each type of copper. (2) Azide inhibited ascorbate oxidase activity by an uncompetitive mechanism. EPR and optical spectra performed on titration of ascorbate oxidase with azide indicated the formation of a copper-azide complex. The Type 2 copper appears to be the binding site of azide. The involvement of the EPR non-detectable copper as an anion binding site with high affinity toward azide can not be excluded.

Ascorbate Oxidase↗