The Wilms tumor protein is persistently associated with the nuclear matrix throughout the cell cycle.
In order to investigate the subnuclear interactions of the WT1 gene product, nuclear fractionation analyses were performed with human osteosarcoma HOS and myelogenous leukemia K562 cells. The WT1 protein was tightly associated with the nucleus and was resistant to high-salt or detergent extraction and DNase I digestion. Both the expression level and stability of WT1 and its resistance to high salt and DNase I treatments remained constant during the cell cycle. In addition, human WT1 ectopically expressed in mouse NIH3T3 cells was also resistant to these treatments. These results suggest that WT1 functions in tight association with the nuclear matrix.
Dobashi
Y
Y
Department of Oncogene Research, Research Institute for Microbial Diseases, Osaka University, Japan.
Kudoh
T
T
Ishidate
T
T
Shoji
M
M
Toyoshima
K
K
Akiyama
T
T
D016475:3T3 Cells / Q000378:metabolism; D000818:Animals; D002453:Cell Cycle / Q000502:physiology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006801:Humans; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism; D051379:Mice; D015530:Nuclear Matrix / Q000378:metabolism; D012516:Osteosarcoma / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014407:Tumor Cells, Cultured / Q000378:metabolism; D025721:WT1 Proteins
D004268:DNA-Binding Proteins; D014157:Transcription Factors; D025721:WT1 Proteins