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Differential Subcellular Localization (differential + subcellular_localization)
Selected AbstractsCentral nervous system neurons acquire mast cell products via transgranulationEUROPEAN JOURNAL OF NEUROSCIENCE, Issue 9 2005M. Wilhelm Abstract Resting and actively degranulating mast cells are found on the brain side of the blood,brain barrier. In the periphery, exocytosis of mast cell granules results in the release of soluble mediators and insoluble granule remnants. These mast cell constituents are found in a variety of nearby cell types, acquired by fusion of granule and cellular membranes or by cellular capture of mast cell granule remnants. These phenomena have not been studied in the brain. In the current work, light and electron microscopic studies of the medial habenula of the dove brain revealed that mast cell-derived material can enter neurons in three ways: by direct fusion of the granule and plasma membranes (mast cell and neuron); by capture of insoluble granule remnants and, potentially, via receptor-mediated endocytosis of gonadotropin-releasing hormone, a soluble mediator derived from the mast cell. These processes result in differential subcellular localization of mast cell material in neurons, including free in the neuronal cytoplasm, membrane-bound in granule-like compartments or in association with small vesicles and the trans-Golgi network. Capture of granule remnants is the most frequently observed form of neuronal acquisition of mast cell products and correlates quantitatively with mast cells undergoing piecemeal degranulation. The present study indicates that mast cell-derived products can enter neurons, a process termed transgranulation, indicating a novel form of brain,immune system communication. [source] Characterization of the Drosophila myeloid leukemia factorGENES TO CELLS, Issue 12 2006Séverine Martin-Lannerée In human, the myeloid leukemia factor 1 (hMLF1) has been shown to be involved in acute leukemia, and mlf related genes are present in many animals. Despite their extensive representation and their good conservation, very little is understood about their function. In Drosophila, dMLF physically interacts with both the transcription regulatory factor DREF and an antagonist of the Hedgehog pathway, Suppressor of Fused, whose over-expression in the fly suppresses the toxicity induced by polyglutamine. No connection between these data has, however, been established. Here, we show that dmlf is widely and dynamically expressed during fly development. We isolated and analyzed the first dmlf mutants: embryos lacking maternal dmlf product have a low viability with no specific defect, and dmlf - , adults display weak phenotypes. We monitored dMLF subcellular localization in the fly and cultured cells. We were able to show that, although generally nuclear, dMLF can also be cytoplasmic, depending on the developmental context. Furthermore, two differently spliced variants of dMLF display differential subcellular localization, allowing the identification of regions of dMLF potentially important for its localization. Finally, we demonstrate that dMLF can act developmentally and postdevelopmentally to suppress neurodegeneration and premature aging in a cerebellar ataxia model. [source] Classic and soma-restricted proteolipids are targeted to different subcellular compartments in oligodendrocytesJOURNAL OF NEUROSCIENCE RESEARCH, Issue 6 2001Ernesto R. Bongarzone Abstract The myelin proteolipid (PLP) gene is very active in oligodendrocytes (OLs) and generates at least four proteins: the classic PLP and DM20 proteolipids, which are associated with compact myelin and the srPLP and srDM20, which are associated with the cell soma. These proteins are extremely hydrophobic and appear to follow the biosynthetic route used by secretory proteins. In this study, we have analyzed the subcellular distribution of the newly described sr-proteolipids and compared it to that of the classic proteolipids. Immunocytochemical analysis indicates that the sr-proteolipids and classic proteolipids are found in association with the endoplasmic reticulum (ER) and Golgi apparatus of mature OLs in vitro. Whereas the classic proteolipids become associated with the myelin-like sheets elaborated by OLs, the sr-proteolipids are not targeted to the myelin leaflets. The sr-proteolipids were associated with endosomes and with recycling vesicles as determined by double immunocytochemistry with markers such as syntaxin 6 and clathrin. In vivo, immunohistochemical analysis showed a distribution of the sr-proteolipids that was similar to that obtained in vitro, with a total absence of incorporation of sr-proteolipids into compact myelin. This differential subcellular localization is further evidence for a biological role for these products of the PLP/DM20 gene, which is different from that of the classic proteolipids. J. Neurosci. Res. 65:477,484, 2001. © 2001 Wiley-Liss, Inc. [source] Differential cellular compartmentalization of the nuclear receptor SpSHR2 splicing variants in early sea urchin embryosMOLECULAR REPRODUCTION & DEVELOPMENT, Issue 2 2001Aikaterini Kontrogianni-Konstantopoulos Abstract SpSHR2 is a member of the nuclear receptor superfamily, expressed in embryos, larvae, and adult tissues of sea urchin. During embryonic development, two receptor isoforms are produced via alternative splicing. One exhibits the typical structure of nuclear receptors (SpSHR2-full length), whereas the other is missing the entire LBD (SpSHR2-splice variant). DNA-constructs encoding these isoforms and two additional in vitro generated deletion mutants were engineered in an expression vector carrying the myc-tag. Expression of the tagged isoforms in S. purpuratus embryos showed that the exogenous SpSHR2 full-length protein displays a similar subcellular localization as the endogenous receptor. In early cleavage stages (4-cells), the full-length isoform is predominantly localized in the nucleus, whereas two cell divisions later (16-cells) protein accumulations are detected in both the nucleus and cytoplasm. To the contrary, the SpSHR2-splice variant is confined in the embryonic nuclei both at 4- and 16-cell stage embryos. Analysis of the intracellular distribution of two receptor mutants, one having a deletion within the DBD (,P) and the other a truncation of the C-terminal F-domain (,F), revealed that ,P is localized similarly to full-length receptor, whereas ,F is maintained in the nucleus, similar to the SpSHR2 splice variant. Investigation of the DNA binding and dimerization properties of the two SpSHR2 isoforms demonstrated that they recognize and bind to a DR1-element as monomers, whereas ,P does not bind DNA and ,F binds to DR1 poorly. These results suggest that the receptor's putative LBD is responsible for the differential subcellular localization of the two natural SpSHR2-isoforms in early development. Mol. Reprod. Dev. 60: 147,157, 2001. © 2001 Wiley-Liss, Inc. [source] | |||||||||||||||||||