The effect of proteasome inhibitors on mammalian erythroid terminal differentiation
| Autor: | Judith Tamburlin, Stephen T. Koury, Diane P. Bofinger, Lynne Pajak, Cheng Yao Chen |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Cytoplasm
Proteasome Endopeptidase Complex Cancer Research Reticulocytes Leupeptins Proteolysis Blotting Western Lactacystin macromolecular substances Biology Mice chemistry.chemical_compound Western blot Reticulocyte Multienzyme Complexes hemic and lymphatic diseases MG132 Genetics medicine Animals Erythropoiesis Protease Inhibitors Molecular Biology Cell Line Transformed Erythroid Precursor Cells medicine.diagnostic_test Ubiquitin Nuclear Proteins Cell Differentiation Cell Biology Hematology Cell Transformation Viral Molecular biology Acetylcysteine Friend murine leukemia virus Blot Cysteine Endopeptidases medicine.anatomical_structure chemistry Proteasome Cell culture Protein Processing Post-Translational |
| Zdroj: | Experimental Hematology. 30:634-639 |
| ISSN: | 0301-472X |
| DOI: | 10.1016/s0301-472x(02)00826-3 |
| Popis: | Objective Murine erythroblasts infected with the anemia-inducing strain of Friend virus (FVA cells) terminally differentiate to the reticulocyte stage after 48 hours of culture in vitro in response to erythropoietin (EPO). The objective of this study was to determine the possible role of proteasome-mediated proteolysis during the terminal differentiation of FVA cells. Materials and Methods The proteasome inhibitors MG132 and lactacystin were used to perturb the normal function of proteasomes during terminal differentiation. Effects of proteasome inhibitors on terminal differentiation were quantitated by evaluation of cellular morphology after benzidine staining and by Western blot analyses. Results Treatment of EPO-stimulated FVA cells with lactacystin or MG132 at later periods of culture increased accumulations of nuclear and cytosolic ubiquitinated proteins and decreased nuclear extrusion to less than 40% of controls. Conclusion Our results suggest that the proteasomal degradation of ubiquitinated proteins plays an important role in the enucleation of mammalian erythroblasts. |
| Databáze: | OpenAIRE |
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