Characterization of the ubiquitin-proteasome system in bortezomib-adapted cells.
作者： T Rückrich , M Kraus , J Gogel , A Beck , H Ovaa
DOI: 10.1038/LEU.2009.8
关键词: Proteasome 、 Cancer research 、 Biology 、 Unfolded protein response 、 Bortezomib 、 Proteases 、 Activator (genetics) 、 Proteasome inhibitor 、 Ubiquitin 、 Protein biosynthesis
摘要: Resistance towards the proteasome inhibitor bortezomib is poorly understood. We adapted HL-60, ARH-77 and AMO-1 cell lines (myeloid leukemia, plasmocytoid lymphoma, myeloma) to exceeding therapeutic plasma levels, compared characteristics of ubiquitin-proteasome system, alternative proteases unfolded protein response (UPR) between cells parental lines. Adapted showed increased transcription rates, activities polypeptide levels bortezomib-sensitive beta5, but also beta2 subunit consistently retained elevated active beta1/beta5-type subunits in presence bortezomib. Bortezomib-adapted HL-60 expression association 11S activator, did not accumulate poly-ubiquitinated protein, activate UPR or UPR-mediated apoptosis The rate biosynthesis was reduced, chaperone genes downmodulated. observe major changes TPPII, cathepsins deubiquitinating proteases. conclude that different types bortezomib-adapted lines, including myeloma, show similar patterns proteasomal machinery which result residual activity a quantitative balance destruction.
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