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ID 114979
Title Alternative
Protein Phosphatase 1δ with Nucleophosmin
Author
Hirashima, Kanji The University of Tokushima
Kimura, Koji The University of Tokushima
Morimoto, Hiroyuki University of Occupational and Environmental Health
Keywords
protein phosphatase
nucleophosmin
osteoblast
Content Type
Journal Article
Description
Protein phosphorylation and dephosphorylation has been recognized as an essential mechanism in the regulation of cellular metabolism and function in various tissues. Serine and threonine protein phosphatases (PP) are divided into four categories: PP1, PP2A, PP2B, and PP2C. At least four isoforms of PP1 catalytic subunit in rat, PP1α, PP1γ1, PP1γ2, and PP1δ, were isolated. In the present study, we examined the localization and expression of PP1δ in human osteoblastic Saos-2 cells. Anti-PP1δ antibody recognized a protein present in the nucleolar regions in Saos-2 cells. Cellular fractionation revealed that PP1δ is a 37 kDa protein localized in the nucleolus. Nucleophosmin is a nucleolar phosphoprotein and located mainly in the nucleolus. Staining pattern of nucleophosmin in Saos-2 cells was similar to that of PP1δ. PP1δ and nucleophosmin were specifically stained as dots in the nucleus. Dual fluorescence images revealed that PP1δ and nucleophosmin were localized in the same regions in the nucleolus. Similar distribution patterns of PP1δ and nucleophosmin were observed in osteoblastic MG63 cells. The interaction of PP1δ and nucleophosmin was also shown by immunoprecipitation and Western analysis. These results indicated that PP1δ associate with nucleophosmin directly in the nucleolus and suggested that nucleophosmin is one of the candidate substrate for PP1δ.
Journal Title
Acta Histochemica et Cytochemica
ISSN
00445991
13475800
NCID
AA00508022
Publisher
The Japan Society of Histochemistry and Cytochemistry
Volume
45
Issue
1
Start Page
1
End Page
7
Published Date
2011-11-05
Rights
This is an open access article distributed under the Creative Commons Attribution License(https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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DOI (Published Version)
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language
eng
TextVersion
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departments
Oral Sciences