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Journal of Histochemistry and Cytochemistry, Vol. 50, 1187-1193, September 2002, Copyright © 2002, The Histochemical Society, Inc.

ARTICLE

Interaction of Protein Phosphatase 1 Delta with Nucleolin in Human Osteoblastic Cells

Hiroyuki Morimotoa, Hirohiko Okamuraa, and Tatsuji Hanejia
a Department of Histology and Oral Histology, School of Dentistry, The University of Tokushima, Tokushima, Japan

Correspondence to: Tatsuji Haneji, Dept. of Histology and Oral Histology, School of Dentistry, University of Tokushima, 3-18-15, Kuramoto, Tokushima 770-8504, Japan. E-mail: tat-hane@dent.tokushima-u.ac.jp

We examined the expression and cytolocalization of the protein phosphatase type 1 delta (PP1{delta}) 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. PP1{delta} and nucleolin were co-localized in the nucleolus in MG63 and Saos-2 cells revealed by an immunofluorescence method. PP1{delta} and nucleolin were also co-immunoprecipitated with anti-nucleolin and anti-PP1{delta} antibodies. In the actinomycin D-treated cells, the subcellular localization of PP1{delta} and nucleolin was changed. Expression of PP1{delta} 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 PP1{delta} was associated with nucleolin in the nucleolus of MG63 and Saos-2 cells and that nucleolin is a possible candidate substrate for PP1{delta}. (J Histochem Cytochem 50:1187–1193, 2002)

Key Words: protein phosphatase, nucleolin, osteoblast


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