Laser `direct writing' of silicon pn junctions

Rectifying pn junctions have been deposited by a focused argon laser beam from silane and dopant gases on to oxidised silicon wafers. The characteristics depend on the deposition conditions and on the dopant gas content but are not those of ideal junctions, probably due to a nonabrupt interface from the present growth parameter values     

The Drosophila gene Medea demonstrates the requirement for different classes of Smads in dpp signaling

Signals from transforming growth factor-beta (TGF-beta) ligands are transmitted within the cell by members of the Smad family, which can be grouped into three classes based on sequence similarities. Our previous identification of both class I and II Smads functioning in a single pathway in C. elegans, raised the issue of whether the requirement for Smads derived from different classes is a general feature of TGF-beta signaling. We report here the identification of a new Drosophila class II Smad, Medea, a close homolog of the human tumor-suppressor gene DPC4. Embryos from germline clones of both Medea and Mad (a class I Smad) are ventralized, as are embryos null for the TGF-beta-like ligand decapentaplegic (dpp). Loss of Medea also blocks dpp signaling during later development, suggesting that Medea, like Mad, is universally required for dpp signaling. Furthermore, we show that the necessity for these two closely related, non-redundant Smads, is due to their different signaling properties - upon activation of the Dpp pathway, Mad is required to actively translocate Medea into the nucleus. These results provide a paradigm for, and distinguish between, the requirement for class I and II Smads in Dpp/BMP signaling.     

Effect of tuftsin on human Kupffer cell

BACKGROUND/AIMS: Kupffer cells are the most important category of reticuloendothelial cells which are critical for host defense in the liver. We investigated the effects of tuftsin (Thr-Lys-Pro-Arg) on human Kupffer cells. METHODOLOGY: Human Kupffer cells were obtained from the livers of patients with colon cancer. Phagocytosis assay was done by microscopic counting of the number of Kupffer cells that engulfed fluorescent particle(s), and the number of the particles engulfed per Kupffer cell when Kupffer cells were incubated with and without tuftsin. Effect of tuftsin on the release of tumor necrosis factor from Kupffer cells was also studied. RESULTS: Phagocytosis was enhanced significantly by tuftsin. The greatest effect on percentage of phagocytic cells was observed at 1.0 microg/ml of tuftsin. The mean number of particles engulfed per Kupffer cell was also increased with tuftsin 1.0 microg/ml. Tumor necrosis factor release was also significantly increased; the greatest effect was observed at 1.0 microg/ml of tuftsin. CONCLUSIONS: Tuftsin enhances phagocytic activity and tumor necrosis factor release of human Kupffer cells, which are advantageous for host defense against invading microorganisms and tumor cells.     

An essential role for a small synaptic vesicle-associated phosphatidylinositol 4-kinase in neurotransmitter release

Glutamate release from nerve terminals is the consequence of Ca2+-triggered fusion of small synaptic vesicles with the presynaptic plasma membrane. ATP dependence of neurotransmitter release has been suggested to be founded, in part, on phosphorylation steps preceding membrane fusion. Here we present evidence for an essential role of phosphatidylinositol phosphorylation in stimulated release of neurotransmitter glutamate from isolated nerve terminals (synaptosomes). Specifically, we show that a phosphatidylinositol 4-kinase (PtdIns 4-kinase) activity resides on nerve terminal-derived small synaptic vesicles (SSVs) and that inhibition of the PtdIns 4-kinase activity in intact synaptosomes leads to attenuation of the evoked release of glutamate. The attenuation of transmitter release is reversible and correlates with respective changes in intrasynaptosomal PtdIns 4-kinase activity. Because only the Ca2+-dependent release of glutamate is affected, regulation appears to be at the level of exocytosis. Taken together, our data imply a mandatory role for PtdIns 4-kinase and phosphoinositide products in the regulated exocytosis of SSV in mammalian nerve terminals.