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Biomedical subjects

F Omodeo-Sale

Publications and source records attributed to F Omodeo-Sale.

7 recordsLinked to original sources
PubMed1997

Lipid peroxidation and antioxidant systems in rat brain: effect of chronic alcohol consumption.

The effect of chronic ethanol exposure, in a liquid diet, on lipid peroxidation and some antioxidant systems of rat brain was investigated. Chronic ethanol administration induced a greater susceptibility to iron/ascorbate-induced lipid peroxidation, estimated as thiobarbituric reactive substances (TBARS) production, in the microsomal fraction, but a lower lipid peroxidation in the total homogenate. Glutathione (GSH) levels as well as GSH peroxidase and GSH reductase were unaffected, while the activity of Cu-Zn superoxide dismutase was decreased and that of catalase increased. Lipid peroxidation experiments performed in the presence of some hydroxyl radical scavengers suggested that a greater OH. generation may be responsible of the greater TBARS production in the microsomal fraction of ethanol treated rats; differently, in total homogenate of control and ethanol rats a relationship was found between the redox state of iron and TBARS production, suggesting that the lower lipid peroxidation in treated rats may depend on a different modulation of the iron redox state.

Alcoholism↗
PubMed1993

Age related changes in functions and physicochemical properties of rat jejunal brush border membrane after chronic ethanol administration.

1. We investigated the chronic effects of a 4 week treatment with ethanol on functions and physicochemical properties of BBM of young and adult rats (2 and 7 months old respectively). 2. In the ethanol treated groups the cholesterol/phospholipid and the protein/lipid ratios as well as the D-glucose uptake and lactase specific activity and Vmax were increased. In spite of a minor alcohol consumption the adult group was the more affected. 3. Membranes from the ethanol fed rats were less fluid and more tolerant to the in vitro addition of ethanol.

Aging↗
PubMed1987

Interactions of insulin with sulfatide-containing vesicles of phosphatidylcholine at different pHs.

Positively charged insulin is described to induce aggregation of phosphatidylcholine vesicles containing 10 mol% sulfatide at acidic pH. Techniques including light-scattering, Sepharose chromatography, centrifugation, trapped volume determination, circular dichroism and fluorescence polarization, demonstrate that large amounts of negatively charged insulin remain firmly associated to the vesicles upon raising the pH to 7. This is surprising, since only trace amounts of insulin associate to the sulfatide-containing vesicles upon direct incubation at pH 7. The possible molecular explanation of the phenomenon and the relevance of these findings to the actions of insulin in vivo are discussed.

Circular Dichroism↗
PubMed1980

A lysosomal storage disorder in mice characterized by a dual deficiency of sphingomyelinase and glucocerebrosidase.

Lipid and lysosomal enzyme levels in the tissues of a strain of mice afflicted with an autosomal rescessive neuroviscereal storage disorder were examined. Sphingomyelinase and glucocerebrosidase activities were consistently diminished in a wide variety of tissues obtained from the affected mice. The activities of these enzymes were clearly attenuated in new-born mice, which at this age, were otherwise indistinguishable from littermates and age-matched controls. The deficiency of sphingomyelinase was more pronounced than glucocerebrosidase. There was progressive accumulation of sphingomyelin, glucocerebroside, lactosylceramide and unesterified cholesterol in the tissues of these mice in the postnatal period. Gangliosides GM2 and GM3 accumulated in the brain of the animals, and GM3 and asialo-GM2 were stored in the liver. Furthermore, there was a large increase in the quantity of hepatic bis(monoacylglycero)phosphate. The accumulation of lipids was parallelled by a progressive elevation in the activity of several lysosomal hydrolases in various tissues. Heterozygous mice were biochemically indistinguishable from normal controls. The phenotypic manifestations in these metabolically mutated animals are compared with those in Niemann-Pick disease and Gaucher's disease in humans.

Animals↗
PubMed1980

A lysosomal storage disorder in mice characterized by the accumulation of several sphingolipids.

A strain of BALB/c mice with an autosomal recessive neurologic disorder has been reported previously [1, 2]. The tissues of affected animals have been further examined and the activities of varius lysosomal hydrolases and levels of sphingolipids were compared to those in control mice. There was a substantial diminution of sphingomyelinase and glucocerebrosidase activities in liver, spleen, lung, thymus, and kidney of affected mice. There was a corresponding accumulation of sphingomyelin and glucocerebroside in these tissues. The activity of several other lysosomal hydrolases was elevated. Heterozygotes did not show any of the enzymatic alterations. The brain of affected animals showed substantial accumulation of the gangliosides GM3 and GM2.

Animals↗
PubMed1978

Effect of thyroid phospholipids on the interaction of thyrotropin with thyroid membranes.

Various lipids extracted from bovine thyroid glands were tested for their ability to affect the binding of 125I-labeled thyrotropin to bovine thyroid membranes. The most potent inhibitors were the acidic phospholipids in the order cardiolipin greater than phosphatidylglycerol greater than phosphatidylinositol greater than phosphatidylserine. Other phospholipids, neutral lipids, and neutral glycolipids were ineffective. As reported previously [mullin, B. R., Pacuszka, T., Lee, G., Kohn, L. D., Brady, R. O. & Fishman, P. H. (1978) Science 199, 77--79], thyroid gangliosides also inhibited thyrotropin binding but not as effectively as phospholipids. In addition, the mode of action of these two classes of acidic lipids was different. When thyroid membranes were preincubated with the phospholipids and then separated by centrifugation, their ability to bind thyrotropin was still diminished. In contrast, gangliosides appear to interact with the hormone and not with the membranes. The effect of phospholipids on thyroid membranes was further examined by incubating the membranes with phospholipase A. The treated membranes now bound more labeled hormone. These results suggest that certain acidic phospholipids, which are present in only small amounts in thyroid membranes, influence the state of the thyrotropin receptor and its ability to bind thyrotropin.

Animals↗