Open AccessMyosin heavy chain degradation during apoptosis in endothelial cells
Author(s) -
SuarezHerta N.,
Lecocq R.,
Mosselmanst R.,
Galand P.,
Dumont J.e,
Robaye B.
Publication year - 2000
Publication title -
cell proliferation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.647
H-Index - 74
eISSN - 1365-2184
pISSN - 0960-7722
DOI - 10.1046/j.1365-2184.2000.00169.x
Subject(s) - proteolysis , myosin , apoptosis , microbiology and biotechnology , cytoskeleton , vimentin , proteases , biology , fragmentation (computing) , programmed cell death , intermediate filament , cell , biochemistry , enzyme , immunology , ecology , immunohistochemistry
The cytoskeleton undergoes dramatic changes during apoptosis and many cytoskeletal proteins are known to be degraded during this process. The number of proteases found to be involved in apoptosis is growing but the role of the proteolysis they cause remains poorly understood. This report describes for the first time that myosin heavy chain is cleaved in aortic endothelial cell apoptosis induced either by tumour necrosis factor‐α or okadaic acid. The cleavage was specific since a well‐defined major 97 kDa fragment of myosin heavy chain was produced. The intermediate filament component vimentin was also cleaved into well‐defined fragments (31, 28 and 23 kDa). Kinetic studies showed that proteolysis occurred concomitantly with the morphological changes associated with apoptosis, i.e. cellular condensation and fragmentation in apoptotic bodies. These data suggest that the degradation of myosin and vimentin could be involved in the execution of the morphological alteratins observed during apoptotic cell death.