|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:dateCreated |
1997-1-7
|
|
pubmed:abstractText |
To test the role of Rho GTP-binding proteins in growth regulation of human myelomonocytic tumour cells we used recombinant C3 exoenzyme of Clostridium botulinum to specifically ADP-ribosylate and inactivate Rho proteins in situ. In homogenates of HL60 cells, the C3 exoenzyme [32P]ADP-ribosylated one protein that was identified as RhoA by immunoblot and two-dimensional gel electrophoresis. [32P]ADP ribosylation of RhoA in HL60 homogenates in vitro was reduced to 10-20% when cells in culture were pretreated with C3 exoenzyme (10 micrograms, 24 h), indicating that 80-90% of RhoA could be ADP-ribosylated in situ. The C3 exoenzyme inhibited HL60 cell proliferation by up to 80% and the degree of growth inhibition correlated with the amount of in situ ADP-ribosylated RhoA in a time- and dose-dependent manner. Cell cycle analysis demonstrated that the C3 exoenzyme-treated HL60 cells accumulated in mitosis, and nuclear staining revealed binucleated cells. These findings suggest that RhoA has a key role in human myelomonocytic tumour cell growth by regulating cytoplasmic division.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1328215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1379745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1383236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1400407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1522900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1577714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1601841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1643657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1710770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-1903516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2116664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2118140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-236308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2493391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2498316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2501082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-2506852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-3047011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-3855947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-7680658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8183900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8192667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8195713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8198524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8259209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8402896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8417362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8434008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8436590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8948442-8502473
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0264-6021
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
308 ( Pt 3)
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
853-8
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8948442-ADP Ribose Transferases,
pubmed-meshheading:8948442-Biological Markers,
pubmed-meshheading:8948442-Blotting, Western,
pubmed-meshheading:8948442-Botulinum Toxins,
pubmed-meshheading:8948442-Cell Cycle,
pubmed-meshheading:8948442-Cell Differentiation,
pubmed-meshheading:8948442-Cell Division,
pubmed-meshheading:8948442-Cell Nucleus,
pubmed-meshheading:8948442-Clostridium botulinum,
pubmed-meshheading:8948442-Cytochalasin D,
pubmed-meshheading:8948442-Cytoplasm,
pubmed-meshheading:8948442-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:8948442-Flow Cytometry,
pubmed-meshheading:8948442-GTP-Binding Proteins,
pubmed-meshheading:8948442-Humans,
pubmed-meshheading:8948442-Monocytes,
pubmed-meshheading:8948442-Recombinant Proteins,
pubmed-meshheading:8948442-Ribose,
pubmed-meshheading:8948442-Staining and Labeling,
pubmed-meshheading:8948442-Tumor Cells, Cultured,
pubmed-meshheading:8948442-rhoA GTP-Binding Protein
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
ADP-ribosylation of the GTP-binding protein RhoA blocks cytoplasmic division in human myelomonocytic cells.
|
|
pubmed:affiliation |
Institut für Prophylaxe und Epidemiologie der Kreislaufkrankheiten, University of Munich, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
