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Viscum album agglutinin‐I induces degradation of cytoskeletal proteins in leukaemia PLB‐985 cells differentiated toward neutrophils: cleavage of non‐muscle myosin heavy chain‐IIA by caspases
Author(s) -
Lavastre Valérie,
Binet François,
Moisan Éliane,
Chiasson Sonia,
Girard Denis
Publication year - 2007
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.2007.06692.x
Subject(s) - cytoskeleton , myosin , microbiology and biotechnology , actin , apoptosis , vimentin , gelsolin , biology , chemistry , cell , immunology , biochemistry , immunohistochemistry
Summary The role of the anti‐cancer agent Viscum album agglutinin‐I (VAA‐I) in leukaemia PLB‐985 cells differentiated toward a neutrophil‐like phenotype by dimethylsulphoxide (PLB‐985D) has never been studied. This study investigated whether or not VAA‐I can induce cytoskeletal breakdown in PLB‐985D cells, as previously observed in undifferentiated PLB‐985 cells. VAA‐I was found to induce apoptosis in PLB‐985D cells, as assessed by cytology and by degradation of gelsolin, an event known to occur via caspase‐3 activation. VAA‐I induced cytoskeletal breakdown based on the disruption of the F‐actin network and cleavage of paxillin, vimentin and lamin B 1 . In addition, we demonstrated, for the first time, that non‐muscle myosin heavy chain IIA (NMHC‐IIA) was cleaved by VAA‐I treatment. Degradation of NMHC‐IIA was reversed by the pan caspase inhibitor z‐VAD‐fmk in PLB‐985D cells and neutrophils. However, unlike lamin B 1 , no NMHC‐IIA was detected on the cell surface of apoptotic neutrophils. In conclusion, PLB‐985D cells responded in a similar manner to neutrophils regarding the degradation of the tested cytoskeletal. Therefore, PLB‐985D cells may provide a suitable substitute for neutrophils in screening experiments, preventing extensive neutrophil cell isolation.