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pubmed-article:12185196pubmed:abstractTextWe examined the expression and cytolocalization of the protein phosphatase type 1 delta (PP1delta) isoform and nucleolin in human osteoblastic MG63 and Saos-2 cells. Cellular fractionation of MG63 cells was done and protein was prepared from each fraction. Anti-nucleolin antibody interacted with the 100- and 95-kD proteins present in the whole-cell lysate. The 100-kD protein was detected in nuclear and nucleolar fractions. The 95-kD protein was detected in cytosolic and nucleoplasmic fractions. PP1delta and nucleolin were co-localized in the nucleolus in MG63 and Saos-2 cells revealed by an immunofluorescence method. PP1delta and nucleolin were also co-immunoprecipitated with anti-nucleolin and anti-PP1delta antibodies. In the actinomycin D-treated cells, the subcellular localization of PP1delta and nucleolin was changed. Expression of PP1delta was upregulated with actinomycin D treatment. The level of 100-kD protein did not change in the actinomycin D-treated cells. However, the level of the 95-kD band increased with actinomycin D treatment. These results indicate that PP1delta was associated with nucleolin in the nucleolus of MG63 and Saos-2 cells and that nucleolin is a possible candidate substrate for PP1delta.lld:pubmed
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pubmed-article:12185196pubmed:pagination1187-93lld:pubmed
pubmed-article:12185196pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:12185196pubmed:articleTitleInteraction of protein phosphatase 1 delta with nucleolin in human osteoblastic cells.lld:pubmed
pubmed-article:12185196pubmed:affiliationDepartment of Histology and Oral Histology, School of Dentistry, The University of Tokushima, Tokushima, Japan.lld:pubmed
pubmed-article:12185196pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12185196pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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