Biomedical subjects

C Nicotra

Publications and source records attributed to C Nicotra.

At least 19 recordsLinked to original sources

PubMed1995

Polyamines and ripening of photoreceptor outer segments in chicken embryos.

Polyamines and their related monoacetyl derivatives were studied in rod outer segment (ROS) and cone outer segment (COS) of photoreceptor cells from chick embryo retina during eye development (7th-18th days). Putrescine was found to be necessary, in the second phase of retinogenesis, to sustain both ROS and COS differentiation and, after acetylation, gamma-aminobutyric acid synthesis. On the other hand, spermidine and even more spermine intervene in the third phase of development when photoreceptors mature. Moreover, the presence of N1-acetylspermidine already at the 7th day indicates that in the outer segment of photoreceptor cells too, as in the whole retina, putrescine synthesis comes about by two pathways. One pathway involves ornithine decarboxylase; the other, spermidine/spermine N1-acetyltransferase and FAD-dependent polyamine oxidase activities that convert spermidine to putrescine via N1-acetylspermidine. These different biosynthetic pathways are probably also decisive in permitting gamma-aminobutyric acid synthesis, which is very important in the ripening process of neural retina.

Acetyltransferases↗

PubMed1989

Analysis of a soluble lipid-protein complex carrying endogenous 11-cis retinaldehyde from bovine retinal pigment epithelium.

A soluble lipid-protein complex in bovine retinal pigment epithelium is shown to carry endogenous 11-cis retinaldehyde, in the extent of 15% of the total 11-cis retinaldehyde found in this tissue. The complex, analyzed with respect to its chemical composition, exhibits a lipid composition close resembling the lipid composition of the rod outer segment membrane; the SDS-PAGE evidences the presence of a number of protein bands, two of which of 34 and 27 kDa appear glycoproteins. Finally, the lipid-protein complex exhibits a discrete level of a Cathepsin D-like protease activity. From the above, the possibility is discussed that the soluble lipid-protein complex could represent some phagolysosomal inclusion occurring in the pigment epithelial cells upon rod outer segment phagocytosis.

Animals↗

PubMed1989

Cardiac peroxisomal enzymes and starvation.

In mice subjected to 3-day periods of food deprivation an increase in plasma free fatty acids occurred together with a rise in the cardiac content of fatty acyl CoA-oxidase (+ 15.2%) and catalase (+ 136.2%) activities. Stimulation of hydrogen peroxide production by the heart was found after 30 hours of fasting and this phenomenon was almost completely eliminated by 6 hours of refeeding. These data suggest that high myocardial loads of free fatty acids involve the peroxisomal enzymes in the beta-oxidation process. The resulting increase in hydrogen peroxide production could be partly responsible for the myocardial injury caused by starvation.

Acyl-CoA Oxidase↗

PubMed1987

Binding of 11-cis retinaldehyde to the partially purified cellular retinaldehyde binding protein from bovine retinal pigment epithelium.

11-cis retinaldehyde binding analysis was performed on a bovine retinal pigment epithelium preparation of cellular retinaldehyde binding protein (CRALBP), whose purity degree was estimated as 75%. Equilibrium binding studies were carried out measuring the replacement of tritium-labeled with unlabeled 11-cis retinaldehyde at 25 degrees C. Analysis of the experimental data both by a direct curve-fitting procedure utilizing a non linear least square regression analysis and by a conventional Scatchard plot revealed a single non-interacting binding site with an apparent equilibrium constant of 0.9 X 10(-7) M. A binding stoichiometry of approximately 1 mol of 11-cis retinaldehyde/mol of binding protein can be calculated from the experimental data. Competition studies carried out in the presence of unlabeled 'trans' and 'cis' isomers of vitamin A derivatives confirm the high degree of specificity of the 11-cis retinaldehyde binding.

Animals↗

PubMed1987

Effects of doxorubicin on mouse heart catalase.

The behaviour of heart and liver catalase was studied 4 days after the administration of different doxorubicin doses to CD 1 mice. The antiblastic increased the specific activity of the heart enzyme with a clear dose-response relationship (+27% after 5 mg/kg i.p.; +61% after 7 mg/kg; + 108% after 10 mg/kg; + 147% after 15 mg/kg). This did not occur in the liver where, on the contrary, a significant reduction of catalase (-31%) was noticed after the highest dose. Analyses by gel filtration excluded the possibility that doxorubicin induces major changes in the molecular properties of heart catalase. In vivo experiments with aminotriazole, which blocks catalase irreversibly, indicated that doxorubicin stimulates the synthesis of cardiac catalase. These findings are discussed with reference to the possible mechanisms of anthracycline cardiotoxicity. The catalase elevation could represent a reaction by the heart to free radicals generated by doxorubicin.

Amitrole↗

PubMed1982

Retinol dehydrogenase from bovine retinal rod outer segments. Kinetic mechanism of the solubilized enzyme.

Retinol dehydrogenase solubilized by Lubrol 12A9 from bovine retinal rod outer segments forms mixed micelles of Stokes radius 8.5 nm. The kinetic properties of the solubilized retinol dehydrogenase were examined and retinaldehyde reduction and retinol oxidation were seen to proceed at pH 8.3 by a sequential Ordered Bi Bi mechanism. This conclusion was supported by bisubstrate initial velocity studies, dead-end and product inhibition. The kinetic mechanism of retinol dehydrogenase is not altered by the effect of Lubrol until a concentration of 2 mM is reached, at which the detergent lowers the values of the Michaelis and dissociation constants. The catalytic rate of the retinol dehydrogenase is significantly lowered by detergent in the range of pH 3 to 9.

Alcohol Oxidoreductases↗

PubMed1980

Isolation procedure for bovine retinal rod outer segments.

An isolation procedure to obtain rod outer segments from cattle retinas is reported. Centrifugation of homogenates in discontinuous and continuous sucrose density gradients yields purified photoreceptor cell outer segments. Assay of the final preparation for rhodopsin content gives a ratio of 2.4 for DO280nm/DO498nm.

Animals↗

PubMed1976

Retinol and retinyl esters in pigment epithelium of rats with inherited retinal degeneration.

A comparative study of the retinol and retinyl ester concentrations was performed in the retinal pigment epithelium of the normal and affected rats. Our findings indicate that in dystrophic rat retinol content increases, whereas the amount of retinyl esters is always lower than normal. An hypothesis can be made on the deficiency of enzymic activities which regulate retinol retinol and retinyl esters levels in the pigment epithelium.

Age Factors↗

PubMed1976