کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1225675 | 968242 | 2012 | 13 صفحه PDF | دانلود رایگان |
Dystrobrevin is a dystrophin-related component of the dystrophin-associated protein complex (DAPC). Using alpha-dystrobrevin as indicator, we aimed to elucidate the interaction network of the DAPC with other proteins during apoptosis of promyelocytic HL-60 cells. The precise role(s) of DBs are not known, but we and others have shown that they play a role in intracellular signal transduction and cellular organization. Apoptosis was induced with etoposide in the absence or presence of Z-VAD to block caspase activity, and we then followed the cellular distribution of α-DB and its association with other proteins, using confocal imaging and cell fractions analyses after immune-precipitation with anti-α-DB and mass spectrometry. Confocal imaging revealed distinct spatial relocalizations of α-DB between the cell membrane, cytosol and nucleus after induction of apoptosis. The expression levels of the identified proteins were evaluated with computer-assisted image analysis of the gels. We thus identified associations with structural and transport proteins (tropomyosin, myosin), membrane (ADAM21, syntrophin), ER-Golgi (TGN51, eIF38) and nuclear (Lamins, ribonucleoprotein C1/C2) proteins. These results suggest that apoptosis-induction in HL-60 cells involves not only classical markers of apoptosis but also a network α-DB-associated proteins at the cell membrane, the cytoplasm and nucleus, affecting key cellular transport processes and cellular structure.
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► In apoptotic cells α-DB localizes between the cell membrane, cytosol and nucleus.
► α-DB associates with structural, transport, ER-Golgi and nuclear proteins.
► An apoptosis-induction in HL-60 cells involves a network of α-DB-associated proteins.
Journal: Journal of Proteomics - Volume 75, Issue 11, 18 June 2012, Pages 3291–3303