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Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease

MPG-Autoren
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Shoeman,  Robert L.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://www.sciencedirect.com/science/article/pii/S0309165106800020/pdf?md5=16fbbd3ed9cb0ea121a08ea48f611b71&pid=1-s2.0-S0309165106800020-main.pdf
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https://doi.org/10.1016/S0309-1651(06)80002-0
(beliebiger Volltext)

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Zitation

Höner, B., Shoeman, R. L., & Traub, P. (1992). Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease. Cell Biology International Reports, 16(7), 603-612. doi:10.1016/S0309-1651(06)80002-0.


Zitierlink: https://hdl.handle.net/21.11116/0000-0000-602E-1
Zusammenfassung
Triton X-100-extracted human skin fibroblasts were exposed to human immunodeficiency virus type 1 protease and analysed by 2D-gel electrophoresis and immunofluorescence microscopy. Vimentin, two of the tropomyosin isoforms, a protein with M(r) approximately 90,000 and a protein with M(r) approximately 200,000 were found to be degraded. Structurally, this was accompanied by the disintegration of the vimentin filament network and the disappearance of the microfilament network. In contrast to our in vivo observations (Höner et al., 1991), prominent stress fibers and chromatin structure seemed to be rather resistant to the action of this protease.