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Verfasst von:Rapp, Stephan [VerfasserIn]   i
 Saffrich, Rainer [VerfasserIn]   i
 Anton, Markus [VerfasserIn]   i
 Jäkle, Ursula [VerfasserIn]   i
 Ansorge, Wilhelm [VerfasserIn]   i
 Gorgas, Karin [VerfasserIn]   i
 Just, Wilhelm W. [VerfasserIn]   i
Titel:Microtubule-based peroxisome movement
Verf.angabe:Stephan Rapp, Rainer Saffrich, Markus Anton, Ursula Jäkle, Wilhelm Ansorge, Karin Gorgas, Wilhelm W. Just
E-Jahr:1996
Jahr:01 April 1996
Umfang:13 S.
Fussnoten:Gesehen am 22.04.2025
Titel Quelle:Enthalten in: Journal of cell science
Ort Quelle:Cambridge : Company of Biologists Limited, 1853
Jahr Quelle:1996
Band/Heft Quelle:109(1996), 4, Seite 837-849
ISSN Quelle:1477-9137
Abstract: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.
DOI:doi:10.1242/jcs.109.4.837
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1242/jcs.109.4.837
 DOI: https://doi.org/10.1242/jcs.109.4.837
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1923355228
Verknüpfungen:→ Zeitschrift

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