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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-3-15
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pubmed:abstractText |
The human A and B subunits of nucleoside diphosphate kinase (NDP kinase), encoded by the nm23-H1 and nm23-H2 genes, respectively, associate as homo- or heterohexamers to be catalytically active for the synthesis of nucleoside triphosphates. Despite 88% identity, they appear to possess specific functions. The nm23-H1 gene is implicated in tumor progression and metastasis, and the nm23-H2 gene product is a transcription factor for c-myc. To determine if these distinct functions reflect different subcellular localizations, the distribution of the A and B NDP kinases was analyzed by immunocytofluorescence microscopy in human breast cancer cell lines (MCF-7 and MDA-MB-231) using highly specific polyclonal and monoclonal antibodies. Interphasic cells exhibited a granular and filamentous cytoplasmic staining, particularly intense around nuclei, with both anti-NDP kinase A and B antibodies. The filamentous component observed with either anti-A or anti-B antibodies was altered in parallel to tubulin labeling with compounds interacting with microtubules, such as taxol and colchicine. Confirming published biochemical data, a partial colocalization with the vimentin network was observed in the MDA-231 cell line. A nuclear and nucleolar localization of NDP kinase B was shown by confocal microscopy which was not observed with the A enzyme. In dividing cells, NDP kinase labeling was punctiform and was not colocalized with the mitotic spindle. In conclusion, the A and B NDP kinases are similarly distributed in cytosol, associated partly to microtubules supporting a role in nucleotide channeling. Only the B enzyme is present in nuclei in accord with its role as a DNA binding protein. Their altered localization in dividing cells suggests colocalization with yet unidentified structures which are not intermediate filament aggregates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NM23 Nucleoside Diphosphate Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/NME1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Diphosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Vimentin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
246
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
355-67
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9925751-Animals,
pubmed-meshheading:9925751-Antibody Specificity,
pubmed-meshheading:9925751-Breast Neoplasms,
pubmed-meshheading:9925751-Cell Division,
pubmed-meshheading:9925751-Cell Nucleus,
pubmed-meshheading:9925751-Cytoskeleton,
pubmed-meshheading:9925751-Female,
pubmed-meshheading:9925751-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:9925751-Humans,
pubmed-meshheading:9925751-Interphase,
pubmed-meshheading:9925751-Microtubules,
pubmed-meshheading:9925751-Mitosis,
pubmed-meshheading:9925751-Monomeric GTP-Binding Proteins,
pubmed-meshheading:9925751-NM23 Nucleoside Diphosphate Kinases,
pubmed-meshheading:9925751-Nucleoside-Diphosphate Kinase,
pubmed-meshheading:9925751-Rabbits,
pubmed-meshheading:9925751-Transcription Factors,
pubmed-meshheading:9925751-Tumor Cells, Cultured,
pubmed-meshheading:9925751-Vimentin
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pubmed:year |
1999
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pubmed:articleTitle |
Cytoskeletal association of the A and B nucleoside diphosphate kinases of interphasic but not mitotic human carcinoma cell lines: specific nuclear localization of the B subunit.
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pubmed:affiliation |
INSERM U402, CHU Saint-Antoine, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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