Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease.
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.
Höner
B
B
Max-Planck-Institut für Zellbiologie, Ladenburg/Heidelberg, FRG.
Shoeman
R L
RL
Traub
P
P
D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D005455:Fluorescent Antibody Technique; D016333:HIV Protease / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D013379:Substrate Specificity; D014746:Vimentin / Q000378:metabolism
D003598:Cytoskeletal Proteins; D014746:Vimentin; D016333:HIV Protease