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Biomedical subjects

F Nicol

Publications and source records attributed to F Nicol.

62 records · Page 4Linked to original sources
PubMed1987

The effects of selenium and copper deficiencies on glutathione S-transferase and glutathione peroxidase in rat liver.

Selenium (Se) deficiency in rats produced significant increases in the activity of hepatic glutathione S-transferase (GST) with 1-chloro-2,4-dinitrobenzene as substrate and in various GST isoenzymes when determined by radioimmunoassay. These changes is GST activity and concentration were associated with Se deficiency that was severe enough to provoke decreases of over 98% in hepatic Se-containing glutathione peroxidase activity (Se-GSHpx). However, decreases in hepatic Se-GSHpx of 60% induced by copper (Cu) deficiency had no effect on GST activity or concentration. Increased GST activity in Se deficiency has previously been postulated to be a compensatory response to loss of Se-GSHpx, since some GSTs have a non-Se-glutathione peroxidase (non-Se-GSHpx) activity. However, the GST isoenzymes determined in this study, GST Yb1Yb1, GST YcYc and GST YaYa, are known to have up to 30-fold differences in non-Se-GSHpx activity, but they were all significantly increased to a similar extent in the Se-deficient rats.

Animals↗
PubMed1985

Studies on the effects of copper deficiency on rat liver mitochondria. I. Changes in mitochondrial composition.

As part of an investigation of the lesions of copper (Cu) deficiency a study was undertaken of the copper, iron, cytochrome and fatty acid composition of liver mitochondria from Cu deficient and Cu-adequate control rats. Cu concentrations were significantly decreased in whole liver, liver mitochondria and in blood plasma. Total iron was significantly increased in whole liver but remained at the normal level in mitochondria. Cytochrome c oxidase (EC 1.9.3.1) and its component cytochromes a and a3 were significantly reduced in liver mitochondria from Cu-deficient rats, whereas there was no effect on the concentration of cytochromes b, c1 and c. Evidence from comparisons between cytochrome c oxidase activity and the amount of enzyme present, as assessed from the mitochondrial cytochrome a and a3 content, suggests that in addition to an absolute loss of enzyme, Cu-deficiency adversely affects the efficiency of the residual enzyme. Severe Cu deficiency had no effect on 'ageing' or 'swelling' properties of liver mitochondria, indicating no marked effects on fatty acid composition. Fatty acid analyses demonstrated a slight but significant increase in docosapentenoic acid (22:5) of Cu-deficient mitochondria, but since this represents a minor component there was no change observed in the 'unsaturation index'. It was concluded that, in contrast to previous reports, Cu deficiency of the severity reported did not have a deleterious effect on the integrity and permeability of the inner mitochondrial membrane as exemplified by any qualitative modification of fatty acid constitution per se.

Animals↗
PubMed1984

Repeat prescribing in the elderly. A case for audit?

An audit of repeat drug prescriptions in 531 elderly patients in an urban practice was undertaken. Two thirds of the patients (64%) were receiving repeat prescriptions at time of review and had been doing so for up to 20 years (mean 5.3 years). Individual practitioners' rates of starting repeat prescriptions and monitoring them were reviewed. The data revealed that drug prescription in this highly susceptible group was not being adequately monitored and stimulated the introduction of repeat prescription cards.

Aged↗
PubMedDate not supplied

The role of selenium in thyroid hormone metabolism and effects of selenium deficiency on thyroid hormone and iodine metabolism.

Selenium deficiency impairs thyroid hormone metabolism by inhibiting the synthesis and activity of the iodothyronine deiodinases, which convert thyroxine (T4) to the more metabolically active 3,3'-5 triiodothyronine (T3). Hepatic type I iodothyronine deiodinase, identified in partially purified cell fractions using affinity labeling with [125I]N-bromoacetyl reverse triiodothyronine, is also labeled with 75Se by in vivo treatment of rats with 75Se-Na2SeO3. Thus, the type I iodothyronine 5'-deiodinase is a selenoenzyme. In rats, concurrent selenium and iodine deficiency produces greater increases in thyroid weight and plasma thyrotrophin than iodine deficiency alone. These results indicate that a concurrent selenium deficiency could be a major determinant of the severity of iodine deficiency.

Animals↗
PubMedDate not supplied

Iodine deficiency in cattle: compensatory changes in thyroidal selenoenzymes.

The trace elements selenium and iodine are both essential for normal thyroid hormone metabolism. To investigate the relationships between these functions, heifers were maintained on iodine-deficient or iodine-sufficient diets from mid pregnancy to term. In these heifers and their offspring the interrelationship between iodine and selenium was apparent with the preferential 10- to 12-fold induction of the selenoenzyme, thyroidal type I, selenium-containing iodothyronine deiodinase activity by iodine deficiency. This was accompanied by two- to four-fold increases in cytosolic glutathione peroxidase activity, probably reflecting increased oxidative activity and metabolism in the thyroid gland in response to iodine deficiency. The above selenoenzyme activities were not affected in liver, kidney, pituitary and brain by iodine deficiency. The results are consistent with a critical role for selenium in both the normal function of cattle thyroid and key enzymes to compensate for the effects of iodine deficiency.

Animals↗
PubMedDate not supplied

Surface aggregation and membrane penetration by peptides: relation to pore formation and fusion.

The peptide GALA undergoes a conformational change to an amphipathic alpha-helix when the pH is reduced, inducing leakage of contents from vesicles. Leakage from neutral or negatively-charged vesicles at pH 5.0 was similar and could be adequately explained by a mathematical model which assumed that GALA becomes incorporated into the vesicle bilayer and irreversibly aggregates to form a pore consisting of M = 10 +/- 2 peptides. Increasing cholesterol content in the membranes resulted in reduced leakage, and increased reversibility of surface aggregation of the peptide. Employing fluorescently labelled peptides confirmed that the degree of reversibility of surface aggregation of GALA was significantly larger in cholesterol containing liposomes. Orientation of the peptide GALA in bilayers was determined by a bodipy-avidin/biotin binding assay. The peptide was labelled by biotin at the N- or C-terminus and bodipy-avidin molecules were added externally or were preencapsulated in the vesicles. The peptides are arranged in the pore perpendicularly to the membrane, such that 3/4 of the N-termini are on the internal side of the membrane. The pores are stable and persist for at least 10 min. When the peptides form an aggregate of size smaller than M, the orientation of the peptide is mostly parallel to the surface and the biotinylated peptide does not translocate. When a critical size of the aggregate is attained, a rearrangement of the peptide occurs, which amounts to rapid penetration and formation of a pore structure. Induction of fusion by peptides may be antagonistic to pore formation, the outcome being dependent on vesicle aggregation.

Liposomes↗