Alpha-Dystrobrevin and its associated proteins in human promyelocytic leukemia cells induced to apoptosis

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• 作者：R奴ta Navakauskien臈^a ; ^b ; ^{ruta.navakauskiene@bchi.vu.lt} ; Gra啪ina Treigyt臈^a ; Veronika-Viktorija Borutinskait臈^a ; Dalius Matuzevi膷ius^c ; Dalius Navakauskas^c ; Karl-Eric Magnusson^d
• 关键词：Alpha-DB ; Leukemic cells ; Apoptosis
• 刊名：Journal of Proteomics
• 出版年：2012
• 期刊代码：P37_18743919
• 类别：ch
• 出版时间：18 June, 2012
• 卷：75
• 期：11
• 页码：3291-3303
• 文件大小：1736 K

摘要

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 伪-DB and its association with other proteins, using confocal imaging and cell fractions analyses after immune-precipitation with anti-伪-DB and mass spectrometry. Confocal imaging revealed distinct spatial relocalizations of 伪-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 伪-DB-associated proteins at the cell membrane, the cytoplasm and nucleus, affecting key cellular transport processes and cellular structure.