972 resultados para G. I. Gurdjieff


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Il Lavoro é incentrato sull' influenza dell'insegnamento di G. I Gurdjieff sul teatro del novecento in particolare sul lavoro di Peter Brook, Declan Donnellan e Robert Lepage

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Signatur des Originals: S 36/G03281

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The Austrian glacier inventory 1969 was compiled from airborne photogrammetry dating from September and October 1969. It includes not only area and surface elevation, but also a number of other parameters as aspect, maximum and minimum elevation, position, ablation and accumulation area. The dataset published here are the orginal results. In course of the compilation of the second Austrian glacier inventory, the photogrammetric data partly has been reanalysed. While in this data set snow areas connected to the glaciers and snow patches in the upper parts of the glacier have not been added to the glacier area, the second glacier inventory included the snow patches.

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Chemotaxis is mediated by activation of seven-transmembrane domain, G protein-coupled receptors, but the signal transduction pathways leading to chemotaxis are poorly understood. To identify G proteins that signal the directed migration of cells, we stably transfected a lymphocyte cell line (300-19) with G protein-coupled receptors that couple exclusively to ±q (the m3 muscarinic receptor), ±i (the κ-opioid receptor), and ±s (the β-adrenergic receptor), as well as the human thrombin receptor (PAR-1) and the C-C chemokine receptor 2B. Cells expressing receptors that coupled to ±i, but not to ±q or ±s, migrated in response to a concentration gradient of the appropriate agonist. Overexpression of ± transducin, which binds to and inactivates free ²Î³ dimers, completely blocked chemotaxis although having little or no effect on intracellular calcium mobilization or other measures of cell signaling. The identification of ²Î³ dimers as a crucial intermediate in the chemotaxis signaling pathway provides further evidence that chemotaxis of mammalian cells has important similarities to polarized responses in yeast. We conclude that chemotaxis is dependent on activation of ±i and the release of ²Î³ dimers, and that ±i-coupled receptors not traditionally associated with chemotaxis can mediate directed migration when they are expressed in hematopoietic cells.

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RGS-GAIP (±-interacting protein) is a member of the RGS (regulator of G protein signaling) family of proteins that functions to down-regulate ±i/±q-linked signaling. GAIP is a GAP or guanosine triphosphatase-activating protein that was initially discovered by virtue of its ability to bind to the heterotrimeric G protein ±i3, which is found on both the plasma membrane (PM) and Golgi membranes. Previously, we demonstrated that, in contrast to most other GAPs, GAIP is membrane anchored and palmitoylated. In this work we used cell fractionation and immunocytochemistry to determine with what particular membranes GAIP is associated. In pituitary cells we found that GAIP fractionated with intracellular membranes, not the PM; by immunogold labeling GAIP was found on clathrin-coated buds or vesicles (CCVs) in the Golgi region. In rat liver GAIP was concentrated in vesicular carrier fractions; it was not found in either Golgi- or PM-enriched fractions. By immunogold labeling it was detected on clathrin-coated pits or CCVs located near the sinusoidal PM. These results suggest that GAIP may be associated with both TGN-derived and PM-derived CCVs. GAIP represents the first GAP found on CCVs or any other intracellular membranes. The presence of GAIP on CCVs suggests a model whereby a GAP is separated in space from its target G protein with the two coming into contact at the time of vesicle fusion.

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GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of G-protein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein ±i3 and was recently shown to be a GTPase-activating protein (GAP). In AtT-20 cells stably expressing GAIP, we found that GAIP is membrane-anchored and faces the cytoplasm, because it was not released by sodium carbonate treatment but was digested by proteinase K. When Cos cells were transiently transfected with GAIP and metabolically labeled with [35S]methionine, two pools of GAIP—a soluble and a membrane-anchored pool—were found. Since the N terminus of GAIP contains a cysteine string motif and cysteine string proteins are heavily palmitoylated, we investigated the possibility that membrane-anchored GAIP might be palmitoylated. We found that after labeling with [3H]palmitic acid, the membrane-anchored pool but not the soluble pool was palmitoylated. In the yeast two-hybrid system, GAIP was found to interact specifically with members of the ±i subfamily, ±i1, ±i2, ±i3, ±z, and ±o, but not with members of other ± subfamilies, ±s, ±q, and ±12/13. The C terminus of ±i3 is important for binding because a 10-aa C-terminal truncation and a point mutant of ±i3 showed significantly diminished interaction. GAIP interacted preferentially with the activated (GTP) form of ±i3, which is in keeping with its GAP activity. We conclude that GAIP is a membrane-anchored GAP with a cysteine string motif. This motif, present in cysteine string proteins found on synaptic vesicles, pancreatic zymogen granules, and chromaffin granules, suggests GAIP’s possible involvement in membrane trafficking.

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Vol 4. ends with article "Antonio Diziani"; no more published.