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  • 1
    Electronic Resource
    Electronic Resource
    Control of apoptosis and mitotic spindle checkpoint by survivin (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 396 (1998), S. 580-584 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Progression of the cell cycle and control of apoptosis (programmed cell death) are thought to be intimately linked processes, acting to preserve homeostasis and developmental morphogenesis. Although proteins that regulate apoptosis have been implicated in restraining cell-cycle entry and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/25141
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  • 2
    Electronic Resource
    Electronic Resource
    The intracellular organization of actin and tubulin in cultured C-1300 mouse neuroblastoma cells (clone NB41A3) (1978)
    Springer
    Journal of neurocytology 7 (1978), S. 571-582 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cells of clone NB41A3 of the C-1300 mouse neuroblastoma were grown to a critical density at which many of the cells flatten, assume a variety of shapes and sizes and some sprout processes resembling neurites. We have studied the distribution of actin and tubulin in these cells using fluorescence microscopy and antibodies against actin or tubulin under these conditions. Actin-containing structures are variably arranged and predominantly associated with motile areas of the cell periphery including the growth cone. Microtubules appear to run radially from the perinuclear area towards the cell periphery. When neurites are present, microtubules converge into them and run to the growth cone but rarely contact its edge.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01260890
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  • 3
    Electronic Resource
    Electronic Resource
    Radioautographic evidence for protein transport along the optic pathway of early chick embryos (1972)
    Springer
    Journal of neurocytology 1 (1972), S. 101-108 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The optic system of chick embryos was used to study axonal transport during early embryogenesis. Axonal transport of proteins from the retina to the contralateral tectum could be detected by radioautography following intraocular injection of3H-leucine in 7 day old embryos. The rate of transport was approximately 5mm/day, and no evidence was obtained for a more rapid axonal transport at this stage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01098649
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of nerve growth factor in chick embryo sympathetic neuronsin vitro (1981)
    Springer
    Journal of neurocytology 10 (1981), S. 45-55 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The distribution of nerve growth factor (NGF) in chick embryo sympathetic neurons has been followed by two distinct procedures, that is, indirect immunofluorescence microscopy employing purified NGF antibodies and autoradiography after exposure of cells to [125I]NGF. This study shows that NGF bound to sympathetic neurons is not uniformly distributed but appears in spots over the surface of perikarya and along processes. If the same cells, after incubation with NGF and fixation, are treated with methanol-acetone to allow permeation of immunoglobulins across the plasma membrane, NGF antibody immunoreactive material is also found within the cytoplasm and notably in the paranuclear area only in sympathetic neurons. Analogous findings are obtained when sympathetic neurons are incubated in the presence of [125I]NGF, fixed, sectioned and processed for autoradiography. Also with this technique NGF appears to be localized in the cytoplasmic compartment and is found around the nucleus. These studies are discussed in connection with the results of similar experiments performed on a clonal line of NGF target cells known as PC12.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01181744
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  • 5
    Electronic Resource
    Electronic Resource
    Radioautographic analysis of 3H-fucose labelled glycoproteins transported along the optic pathway of chick embryos (1974)
    Springer
    Cell & tissue research 153 (1974), S. 465-476 
    Details
    ISSN: 1432-0878
    Keywords: Axonal transport ; Labelled glycoproteins ; Optic pathway ; Chick embryo ; Radioautography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The axonal transport of 3H-fucose labelled glycoproteins along the developing optic pathway was studied by radioautography in 7-day and 18-day chick embryos after injection of 3H-fucose into the right eye. In the 7-day embryos an axonal transport of labelled glycoproteins could be traced towards axon tops in the anteromedial aspect of the left optic lobe. The glycoprotein radioactivity reached the distal parts of the growing optic axons between 2 and 4 h after intraocular injection of labelled precursor indicating a rapid axonal transport of the order of at least 20 to 50 mm day-1. In the 18-day embryos fucose labelled glycoproteins reached the optic tectum at 2 h after 3H-fucose injection. When the fate of the glycoproteins was analyzed at later survival times an accumulation of radioactivity in the tectal layers containing synapses of optic origin could be found for at least 48 h after precursor injection in the 18-day embryos. The present data indicate that throughout development glycoproteins synthesized in the nerve cell bodies reach the distal parts of growing and maturing axons. The hypothesis is proposed that glycoproteins rapidly reach the preterminal portion of the optic axons where they become integral proteins of the axolemma. From this location they may flow within the membrane structure to reach the synapse.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231541
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  • 6
    Electronic Resource
    Electronic Resource
    Dynamic properties of axonal transport of proteins and glycoproteins: A study based on the effects of metaphase blocking drugs in the developing optic pathway of chick embryos (1975)
    Springer
    Cell & tissue research 161 (1975), S. 303-316 
    Details
    ISSN: 1432-0878
    Keywords: Axonal transport ; Optic pathway ; Glycoproteins ; Vinblastine ; Neuronal maturation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Some properties of the axonal transport of proteins and glycoproteins along the optic pathway of chick embryos and newly hatched chicks were studied by labelling retinal ganglion cells with 3H-proline or3H-fucose. A study of the effects of colchicine (COL) and vinblastine (VLB) on embryonic axonal transport was also carried out. Marked changes in the efficiency of axonal transport were found throughout development. In particular, the fraction of retinal ganglion cell proteins which is rapidly exported toward tectal terminals increases during embryonic life but steadily decreases after hatching. Glycoprotein transport behaves similarly except that its efficiency is relatively higher at stages when critical events of synaptic maturation in the tectum are reported to occur. Embryonic axonal transport is blocked by COL and VLB at very low intravitreal concentrations. Retinal protein synthesis and the morphology of ganglion cells are profoundly altered by the drugs: in general, COL and VLB effects were much more marked in embryonic than in mature neurons. An analysis of the time course of rapid transport along embryonic optic axons was carried out by reducing the efflux of labelled proteins from the eye by giving VLB intravitreally 2 h after the pulse. It revealed some peculiar features in the retino-tectal migration of glycoproteins and confirmed their progressive accumulation within terminals as previously described by radioautography. These results suggest that axonal transport of proteins during embryonic life undergoes changes in parallel with synaptic maturation. It may thus be considered as one of the factors controlling the genesis of neuronal networks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220000
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  • 7
    Electronic Resource
    Electronic Resource
    Vanadate-treated baby hamster kidney fibroblasts show cytoskeleton and adhesion patterns similar to their rous sarcoma virus-transformed counterparts (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 151-159 
    Details
    ISSN: 0730-2312
    Keywords: vanadate ; phosphotyrosine ; transformation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Rous sarcoma virus-trans formed baby hamster kidney fibroblasts (RSV/B4-BHK) adhere to a fibronectin-coated substratum by means of dot-like adhesion sites called podosomes in view of their shape and function as cellular feet (Tarone et al.: Exp Cell Res 159:141, 1985). Podosomes concentrate tyrosine-phosphorylated proteins, including pp60v-src, and appear in many cells transformed by oncogenes coding for tyrosine kinases. In this paper we used orthovanadate, an inhibitor of phosphotyrosine phosphatases, in order to increase the cellular concentration of phosphotyrosine and to study whether this treatment induced the cytoskeleton remodeling leading to the formation of podosomes. Indeed, orthovanadate (10-100 μM) induced in a time-and dose-dependent manner the redistribution of F-actin and the formation of podosomes in BHK cells. Cytoskeleton remodeling occurred along with a marked increase of tyrosine phosphorylatcd proteins. The vanadate effect on the cytoskeletal phenotype was enhanced by the simultaneous treatment of cells with a phorbol ester. Under the latter conditions almost all BHK cells showed podosomes. The vanadate effect was reversible insofar as podosomes and tyrosine-phosphorylated proteins disappeared. Then, vanadate treatment of normal cells induced the cascade of events leading to the cytoskeletal changes typical of transformation and suggested that the transformed cytoskeletal phenotype may he primarily induced by the tyrosine phosphorylation of unknown target(s) operated by endogenous kinases.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240370203
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  • 8
    Electronic Resource
    Electronic Resource
    Colocalization of the p185HER2 oncoprotein and integrin α6β4 in Calu-3 lung carcinoma cells (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 55 (1994), S. 409-418 
    Details
    ISSN: 0730-2312
    Keywords: HER2/neu ; integrins ; laminin ; tyrosine phosphorylation ; oncoprotein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Anti-p185HER2 monoclonal antibodies often show intense reactivity with the basement membrane of tumor cells that overexpress the HER2/neu gene product (p185HER2). To evaluate a possible interaction between p185HER2 and adhesion molecules or their receptors, the polarity of p185HER2 was tested in lung carcinoma cell line Calu-3, which overexpresses this protein, in cultures grown as confluent monolayers or as aggregates. MAb immunostaining patterns indicated that p185HER2 is concentrated on the baso-lateral membrane of cells and that it colocalizes with the integrin α6β4 at the cell-cell junctions where laminin is also found. The same membrane region showed intense reactivity with antiphosphotyrosine antibodies. Furthermore, integrin clustering induced by the specific antibody was accompanied by the clustering of p185HER2, as indicated by immunoelectron microscopy, and by a subsequent increase in p185HER2 tyrosine phosphorylation. Treatment with exogenous laminin also resulted in increased basal levels of p185HER2 phosphorylation. These data suggest a physical interaction between the integrin and the oncoprotein that might be functionally relevant in directly controlling the tyrosine phosphorylation of the catalytic domain of p185HER2. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240550402
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