Search PubMed⌕ Search

Biomedical subjects

G Rotilio

Publications and source records attributed to G Rotilio.

303 records · Page 17Linked to original sources
PubMedDate not supplied

Liposome-mediated increase of the superoxide dismutase content in human erythrocytes: characterization by electron spin resonance.

Room temperature electron spin resonance (ESR) spectroscopy, together with enzyme activity measurements, have been used to study the liposome-mediated enrichment of human red blood cells with superoxide dismutase. The ESR technique was found to be useful not only for qualitative and quantitative determinations, but also for demonstration of enzyme activity inside intact cells. The molecular properties of superoxide dismutase in relation to pharmacological and biotechnological applications are reviewed.

Drug Carriers↗
PubMedDate not supplied

Copper-dependent oxidative stress and neurodegeneration.

Copper is an essential trace element, but its redox reactivity leads to risks of damage to cell and tissues. These are well exemplified by several forms of neurodegenerative diseases, either arising as inherited disorders of copper metabolism, such as Menkes' and Wilson's disease, or as conformational diseases such as Alzheimer's disease and prion diseases. This review will cover some aspects of the involvement of copper-mediated oxidative stress in degenerative processes in the central nervous system, with special focus on the familial form of amyotrophic lateral sclerosis (FALS). Furthermore, a possible role of copper reactivity in inducing critical steps in the apoptotic pathways leading to neurodegeneration is envisaged.

Alzheimer Disease↗
PubMedDate not supplied

Involvement of reactive oxygen species in bacterial killing within epithelial cells.

Several non-phagocytic cells can actively generate the superoxide anion by NAD(P)H oxidases resembling the enzymatic complex typical of phagocytes. Overexpression of periplasmic Cu,ZnSOD rescues invasive E. coli strains from killing within epithelial cells, suggesting that superoxide generation by such cells can oxidatively damage invading bacteria. Pre-treatment of HeLa cells with diphenyl iodonium or 4'-hydroxy-3'-methoxyacetophenone, two inhibitors of NAD(P)H oxidase, significantly enhances intracellular survival of wild type invasive E. coli cells. On the contrary, these inhibitors have no effect on the intracellular survival of an invasive E. coli strain engineered to overexpress Cu,ZnSOD. These results support the hypothesis that superoxide generation by a NAD(P)H oxidase-like complex can limit bacterial survival within epithelial cells and suggest that the role of periplasmic Cu,ZnSOD in bacterial infections is not simply that of conferring protection against the phagocytic oxidative burst.

Enzyme Inhibitors↗
PubMedDate not supplied

The primary structure of human erythrocyte copper/zinc superoxide dismutase: cleavage with Staphylococcus aureus protease, determination of the N-terminal blocking group and location of the disulfide bond.

Results obtained after digestion of copper/zinc superoxide dismutase from human erythrocytes with S. aureus protease are described. In particular, peptides soluble in alkaline conditions proved essential for completing the determination of the primary structure of the enzyme; other peptides were important for establishing the amidation state of dicarboxylic amino acid residues and for confirming controversial sequences. The human enzyme is acetylated at the NH2 terminus and contains an intrasubunit disulfide bond connecting half-cystine residues 57 and 146.

Amino Acid Sequence↗