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Behavior of nucleolar proteins during the course of apoptosis in camptothecin‐treated HL60 cells
Author(s) -
Martelli Alberto M.,
Robuffo Iole,
Bortul Roberta,
Ochs Robert L.,
Luchetti Francesca,
Cocco Lucio,
Zweyer Marina,
Bareggi Renato,
Falcieri Elisabetta
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(20000801)78:2<264::aid-jcb9>3.0.co;2-3
Subject(s) - fibrillarin , nucleophosmin , nucleolin , immunolabeling , immunoelectron microscopy , camptothecin , nucleolus , biology , apoptosis , microbiology and biotechnology , antibody , cancer research , immunology , immunohistochemistry , genetics , biochemistry , cytoplasm , myeloid leukemia
By means of immunofluorescence and immunoelectron microscopy we have studied the fate of different nucleolar components during the apoptotic process in camptothecin‐treated HL60 cells. We have found that RNA polymerase I disappeared while UBF was associated with previously described fibrogranular threaded bodies. In contrast, fibrillarin, C23/nucleolin, and B23/nucleophosmin remained detectable in granular material present amid micronuclei of late apoptotic cells. Double immunolabeling experiments showed colocalization of both C23 and B23 with fibrillarin. Immunoblotting analysis showed that UBF was proteolytically degraded, whereas fibrillarin, C23/nucleolin, and B23/nucleophosmin were not. These results may help explain the presence of anti‐nucleolar antibodies seen in various pathological disorders. J. Cell. Biochem. 78:264–277, 2000. © 2000 Wiley‐Liss, Inc.