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  • The Company of Biologists  (2)
Medientyp
Verlag/Herausgeber
  • The Company of Biologists  (2)
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Erscheinungszeitraum
  • 1
    Online-Ressource
    Online-Ressource
    The Company of Biologists ; 1997
    In:  Journal of Cell Science Vol. 110, No. 23 ( 1997-12-01), p. 2955-2968
    In: Journal of Cell Science, The Company of Biologists, Vol. 110, No. 23 ( 1997-12-01), p. 2955-2968
    Kurzfassung: Peroxisomal motility was studied in vivo in CHO cells following transfection with a green fluorescent protein construct containing the C-terminal peroxisomal targeting signal 1 (GFP-PTS1). Time-lapse imaging and evaluation of difference images revealed that peroxisomes attach to microtubules in a Ca2+ requiring step and are transported in an ATP-dependent manner. Following microinjection of guanosine-5′-O-(3-thiotri-phosphate) (GTP(gamma)S), peroxisomal movements were arrested, indicating regulation by GTP-binding proteins. The effect of GTP(gamma)S was mimicked by AlF4- and mastoparan, two drugs which are known to activate heterotrimeric G proteins. Pertussis toxin which prevents Gi/Go protein activation completely abolished the effect of GTP(gamma)S and mastoparan on peroxisomal motility suggesting that the G protein belongs to the Gi/Go class. At least one effector of the G protein is phospholipase A2 as demonstrated by the observation that the phospholipase A2 activating protein peptide efficiently blocks peroxisomal motility, and that the effect of mastoparan and AlF4- is largely abolished by various phospholipase A2 inhibitors. In summary, these data provide evidence for a new type of regulation of organelle motility mediated by a Gi/Go-phospholipase A2 signaling pathway. This type of regulation has not been observed so far with other cell organelles such as mitochondria, the endoplasmic reticulum or axonal vesicles. Thus, motility is regulated individually for each cell organelle by distinct mechanisms enabling the cell to fulfill its vital functions.
    Materialart: Online-Ressource
    ISSN: 1477-9137 , 0021-9533
    Sprache: Englisch
    Verlag: The Company of Biologists
    Publikationsdatum: 1997
    ZDB Id: 219171-4
    ZDB Id: 1483099-1
    SSG: 12
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Online-Ressource
    Online-Ressource
    The Company of Biologists ; 1996
    In:  Journal of Cell Science Vol. 109, No. 4 ( 1996-04-01), p. 837-849
    In: Journal of Cell Science, The Company of Biologists, Vol. 109, No. 4 ( 1996-04-01), p. 837-849
    Kurzfassung: The association of peroxisomes with cytoskeletal structures was investigated both by electron microscopy and by kinetic analysis of peroxisome movement. The morphological studies indicated distinct interactions of peroxisomes with microtubules and frequently revealed multiple contact sites. The kinetic approach utilised microinjection and import of fluorescein-labeled luciferase in order to mark and track peroxisomes in vivo. Peroxisomal motility was analysed by time-lapse imaging and fluorescence microscopy. According to their movement peroxisomes were classified into two groups. Group 1 peroxisomes comprising the majority of organelles at 37°C moved slowly with an average velocity of 0.024±0.012 µm/second whereas the movement of group 2 peroxisomes, 10-15% of the total population, was saltatory exhibiting an average velocity of 0.26±0.17 µm/second with maximal values of more than 2 µm/second. Saltations were completely abolished by the microtubule-depolymerising drug nocodazole and were slightly reduced by about 25% by cytochalasin D which disrupts the actin microfilament system. Double fluorescence labeling of both peroxisomes and microtubules revealed peroxisome saltations linked to distinct microtubule tracks. Cellular depletion of endogenous levels of NTPs as well as the use of 5’-adenylylimidodiphosphate, a nonhydrolysable ATP analog, applied to a permeabilised cell preparation both completely blocked peroxisomal movement. These data suggest an ATPase dependent, microtubule-based mechanism of peroxisome movement. Both the intact and the permeabilised cell system presented in this paper for the first time allow kinetic measurements on peroxisomal motility and thus will be extremely helpful in the biochemical characterisation of the motor proteins involved.
    Materialart: Online-Ressource
    ISSN: 0021-9533 , 1477-9137
    Sprache: Englisch
    Verlag: The Company of Biologists
    Publikationsdatum: 1996
    ZDB Id: 219171-4
    ZDB Id: 1483099-1
    SSG: 12
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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