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S Justice

Publications and source records attributed to S Justice.

4 recordsLinked to original sources
PubMed1994

Export and trimerization pathways of maltoporin overlap in the inner membrane of Escherichia coli.

The production of functional porins involves multiple steps including: export of precursor polypeptides from the cytoplasm, assembly of monomers into trimers, and stabilization of trimers by association with lipopolysaccharide. In this report, a late export/assembly intermediate of the maltoporin (LamB) is found in the inner membrane of Escherichia coli using cell fractionation studies. This processed intermediate is transiently associated with a unique Triton X-100-insoluble subfraction of the inner membrane. The kinetics of appearance and solubility characteristics of this intermediate correspond to those of the metastable trimer form of LamB, suggesting that the export and assembly pathways overlap in the inner membrane prior to final localization in the bulk outer membrane.

Bacterial Outer Membrane Proteins↗
PubMed1991

Interleukin-6 secreting human pituitary adenomas in vitro.

Interleukin-6 was found to be secreted from seven out of ten human pituitary tumours cultured in vitro. These tumours included prolactin-secreting, growth hormone-secreting and clinically non-functioning adenomas. The amount of Interleukin-6 secreted was variable from 58 to 10,000 units per ml. in medium removed after a four-day incubation under basal conditions. Four tumours secreted IL-6 in excess of 500U/ml, three of which were clinically non-functioning, but each secreted follicle stimulating hormone in vitro. This is the first report of a cytokine growth factor being released basally by human pituitary tumours.

Adenoma↗
PubMed1990

The secretory characteristics of epidermal growth factor in human saliva.

A series of unstimulated and stimulated saliva samples from healthy volunteers was tested for EGF by radioimmunoassay. Salivary EGF, like other salivary constituents, was secreted in a diurnal pattern. On stimulation the rate of EGF secretion doubled but the concentration fell by 70% because of dilution by salivary fluid. EGF secretion was positively related to saliva flow (p = 0.00001) but the coefficient of correlation was low (r = 0.47). Over a period of 30 min continual salivary stimulation, EGF was released in a bimodal pattern with peaks occurring at 3 and 12 min. Subsequently, EGF secretion remained stable at a rate of release that was approx. 80% of the initial peak value (7.4 ng/min). Chromatography indicated that both high and low molecular-weight forms of EGF were present in unstimulated and stimulated saliva and that the low-weight form predominated. However, the proportion of high molecular-weight EGF increased from 18 to 38% of the total on short-term (3 min) stimulation.

Adolescent↗