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Biomedical subjects

B W Moore

Publications and source records attributed to B W Moore.

At least 55 records · Page 3Linked to original sources
PubMed1974

Effect of nerve growth factor on the expression of colchicine-binding activity and 14-3-2 protein in an established line of human neuroblastoma.

Purified nerve growth factor induced the outgrowth of neurites from cultured human neuroblastoma cells (NJB line) and a concomitant increase in colchicine-binding activity in extracts from these cultures. The parallel stimulation of neurite outgrowth from the cells and colchicine-binding activity of the extracts is interpreted to represent de novo synthesis of microtubular subunit protein in response to the challenge by nerve growth factor. The regulation of the expression of 14-3-2 protein, a protein characteristic of differentiated neuronal cells, was not affected in NJB cells by the addition of nerve growth factor to the culture medium. 14-3-2 protein is present in NJB cells at a concentration equal to that present in human brain from subculture to the stationary phase of growth of the tumor cells. It was concluded that these two gene products, characteristic of differentiated neural cells, are not coordinately regulated in NJB human neuroblastoma cells.

Cell Division↗
PubMed1973

Laboratory diagnosis of trachoma: a collaborative study.

A collaborative study on the laboratory diagnosis of trachoma was carried out in three laboratories. A standardized complement fixation (CF) test with chlamydial (bedsonial) group antigen was found to be highly reproducible. The results obtained by different laboratories using the method and reagents suggested by the WHO International Reference Centre for Trachoma and other Chlamydial Infections agreed in more than 95% of the tests. Similar agreement was observed between the results obtained with these reagents and those routinely used in one of these laboratories. In confirmation of previous studies, the CF test was found to give positive results in only a limited proportion of trachoma cases. However, in an area where the disease is hyperendemic the rates showed good correlation with the intensity of clinical signs. A comparison was also made between Giemsa staining and a fluorescent antibody (FA) technique for the cytological examination of conjunctival scrapings. The results obtained with the former method correlated well with clinical activity but the positivity rate was lower than that obtained by the FA technique. The FA results, however, were not an accurate indicator of clinical intensity. These results suggest that the Giemsa method may detect only the most heavily infected individuals.

Child↗
PubMed1972

Synthesis of a brain-specific protein (S100 protein) in a homologous cell-free system programmed with cerebral polysomal messenger RNA.

Polyribosomes, carrying nascent polypeptide chains, were prepared from whole brain, cortex, and hindbrain-medullary white matter of young adult rats. In a homologous cell-free system, a brain-specific protein (S100 protein) was identified in the mixture of polypeptides released from the polyribosomes during incubation for 1 hr at 37 degrees . De novo synthesis of the S100 protein was achieved in a reconstituted cerebral cell-free system containing polysome-derived mRNA and 40S + 60S subunits. The radioactively labeled S100 protein synthesized in vitro was identified by precipitation with antibody to S100 after addition of purified S100 as a carrier, and migration of the solubilized precipitate on acrylamide gels in the presence of sodium dodecyl sulfate. In vitro synthesis of the S100 protein did not occur in analogous cell-free systems derived from hepatic tissue or in a heterologous system containing liver polyribosomes and cerebral enzymes.

Amino Acids↗
PubMed1970

Turnover of the brain specific protein, S-100.

Rats were killed after intraventricular administration of [(3)H]leucine, and the turnover rates of total soluble proteins and of the brain specific S-100 protein were determined. The half-life of S-100 was estimated to be 16 days. The S-100 protein, thus, has a turnover not unlike that of the average water-soluble protein of brain.

Animals↗