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Biomedical subjects

D J Roy

Publications and source records attributed to D J Roy.

At least 91 records · Page 5Linked to original sources
PubMed1989

Ethical issues in the treatment of cancer patients.

Nineteen speakers at the International Conference on Supportive Care--More than Medicine, which was cosponsored by WHO and held in Château Montebello, Quebec, Canada, 18-21 July 1988, presented short introductory lectures and led the Ethics Working Group's discussions on the following ethical issues relating to cancer research and the treatment of cancer patients: telling the truth; allowing to die and practice of euthanasia; clinical research; and limited resources leading to hard choices. This article presents the discussions and recommendations of this Working Group.

Congresses as Topic↗
PubMed1988

Is dying a matter of ethics?

The decisions that must be made at the time of an anticipated death, ideally by the patient but often by family or caregivers, call forth our highest values and deepest beliefs. Dying with dignity means different things to different people but must take into account the patient's autonomy, pain status, and dominion.

Attitude to Death↗
PubMed1987

Cloning and characterization of the gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae.

The LPD1 gene of S. cerevisiae, which encodes lipoamide dehydrogenase (EC 1.8.1.4), has been cloned and characterized. The LPD1 gene is present as a single copy in the yeast genome and is transcribed to give a polyadenylated mRNA species of approximately 2.0 kb. The synthesis of lipoamide dehydrogenase in yeast is subject to carbon catabolite repression since both the level of the LPD1 transcript and the accumulation of the lipoamide dehydrogenase subunit polypeptide were greatly reduced in wild-type cells grown on glucose compared to those grown on a variety of non-fermentable carbon sources. Strains defective in LPD1 but transformed with the LPD1 gene on a high copy number vector exhibited elevated levels of the LPD1 transcript as well as increased lipoamide dehydrogenase activity when grown on glycerol. Immunoblotting experiments confirmed that such transformants over-expressed lipoamide dehydrogenase protein. Transcription from the LPD1 sequence on plasmid pGP1 still appeared to be subject to some catabolite repression despite the presence of multiple copies of the plasmid in the cell.

Autoradiography↗
PubMed1986

A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiae.

In Saccharomyces cerevisiae a nuclear recessive mutation, lpd1, which simultaneously abolishes the activities of lipoamide dehydrogenase, 2-oxoglutarate dehydrogenase and pyruvate dehydrogenase has been identified. Strains carrying this mutation can grow on glucose or poorly on ethanol, but are unable to grow on media with glycerol or acetate as carbon source. The mutation does not prevent the formation of other tricarboxylic acid cycle enzymes such as fumarase, NAD+-linked isocitrate dehydrogenase or succinate-cytochrome c oxidoreductase, but these are produced at about 50%-70% of the wild-type levels. The mutation probably affects the structural gene for lipoamide dehydrogenase since the amount of this enzyme in the cell is subject to a gene dosage effect; heterozygous lpd1 diploids produce half the amount of a homozygous wild-type strain. Moreover, a yeast sequence complementing this mutation when present in the cell on a multicopy plasmid leads to marked overproduction of lipoamide dehydrogenase. Homozygous lpd1 diploids were unable to sporulate indicating that some lipoamide dehydrogenase activity is essential for sporulation to occur on acetate.

Dihydrolipoamide Dehydrogenase↗