Abstract |
An intracellular adriamycin (ADM)- binding protein purified from the cytosol of L1210 mouse lymphocytic leukemia cells had a molecular weight of 700-1500 kDa and hydrolyzed Suc-LLVY-MCA. When L1210 cells were incubated with a photoactive ADM analogue, N-(p-azidobenzoyl)- adriamycin (NAB-ADM), most of the NAB-ADM was found to localize in the nuclei. In situ photoaffinity labeling of L1210 cells with NAB-ADM resulted in low protease activity in the cytosol and nuclear extracts and the cells showed selective photoincorporation of NAB-ADM into the proteasome. These results suggest that the proteasome is a translocator of ADM from the cytoplasm to the nucleus and might therefore become a new candidate for cancer chemotherapy.
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Authors | K I Kiyomiya, S Matsuo, M Kurebe |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 273
Issue 3
Pg. 928-32
(Jul 14 2000)
ISSN: 0006-291X [Print] United States |
PMID | 10891349
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 2000 Academic Press. |
Chemical References |
- Multienzyme Complexes
- Photoaffinity Labels
- Doxorubicin
- Cysteine Endopeptidases
- Proteasome Endopeptidase Complex
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Topics |
- Animals
- Cysteine Endopeptidases
(chemistry, isolation & purification)
- Doxorubicin
(analogs & derivatives, chemistry)
- Electrophoresis, Polyacrylamide Gel
- Leukemia L1210
(pathology)
- Mice
- Multienzyme Complexes
(chemistry, isolation & purification)
- Photoaffinity Labels
- Proteasome Endopeptidase Complex
- Tumor Cells, Cultured
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