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S J Pearson

Publications and source records attributed to S J Pearson.

22 records · Page 2Linked to original sources
PubMed1988

Brain quinolinic acid in Huntington's disease.

Concentrations of the endogenous neurotoxic tryptophan metabolite, quinolinic acid (QA), were measured in postmortem brain tissue obtained from patients with Huntington's disease (HD) and matched controls, using a gas chromatography/mass spectrometry method. There was no significant difference in either the putamen or the frontal cortex between the HD and control groups. These results do not support the hypothesis that increased QA is responsible for neuronal degeneration in HD.

Brain↗
PubMed1987

Decreased glutamic acid and increased 5-hydroxytryptamine in Huntington's disease brain.

gamma-Aminobutyric acid (GABA), glutamate and serotonin (5-HT), along with its major metabolite, 5-hydroxyindoleacetic acid (5-HIAA), have been measured in 4 brain regions taken post-mortem from patients with Huntington's disease and from control subjects. GABA was found to be significantly reduced, not only in the basal ganglia, but also in the cortex and hippocampus. Glutamate was also reduced in all regions except the pallidum, and thus was unrelated to the GABA deficit which was greatest in this area. 5-HT and 5-HIAA were significantly increased in all areas except the hippocampus.

Brain Chemistry↗
PubMed1983

Activation of human alpha 1-antitrypsin gene in rat hepatoma x human fetal liver cell hybrids depends on presence of human chromosome 14.

In order to study the involvement of human chromosomes in the expression of liver-specific functions, we have produced somatic cell hybrids between a rat hepatoma (7777) cell line and human diploid skin fibroblasts (series XIX) or human fetal liver cells (series XXII). Production of human serum proteins was detected by immunoelectrophoretic analyses of concentrated serum-free hybrid culture supernatants. Human alpha 1-antitrypsin (AAT) was secreted by a subset of hybrids but not by the parental cells. The activated human AAT phenotype segregated concordantly with human chromosome 14 in 18 primarily HAT-selected and five azaguanine back-selected series XXII hybrids. All other chromosomes were excluded as playing a role in AAT expression. Therefore, the AAT gene (PI) is assigned to chromosome 14. This quasi-constitutive expression of a liver-specific function was not observed for the other serum proteins studied, nor was it seen in the skin fibroblast-derived hybrids (series XIX) although AAT was produced by some of them.

Animals↗