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Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells.

Whyte, P and Eisenman, R N (1992) Dephosphorylation of the retinoblastoma protein during differentiation of HL60 cells. Biochemistry and cell biology = Biochimie et biologie cellulaire, 70 (12). pp. 1380-1384. ISSN 0829-8211

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Abstract

Immunoprecipitated retinoblastoma protein from HL60 cells migrated as a series of bands during electrophoresis. The heterogeneity appeared to be generated by phosphorylation of the retinoblastoma protein. Treatment of the cells with the phorbol ester, tetradecanoyl phorbol acetate (TPA), resulted in both a loss of the heterogeneity of the pRB species and a significant decrease in the level of pRB phosphorylation. These changes accompanied differentiation of the HL60 cells into macrophages. Treatment of the cells with dibutyryl cAMP also resulted in dephosphorylation of pRB as well as cell cycle arrest, although no recognizable differentiation occurred. These results are consistent with a model in which TPA and dibutyryl cAMP dependent pathways can activate pRB by altering its phosphorylation.

Item Type: Article
Additional Information: This article does not have a URL available at the journal website.
PubMed ID: 1338571
Keywords or MeSH Headings: Bucladesine/pharmacology; Cell Differentiation; Cyclic AMP/pharmacology; Humans; Immunosorbent Techniques; Leukemia, Promyelocytic, Acute/metabolism/pathology; Macrophages/pathology; Phosphorylation; Protein Kinase C/metabolism; Retinoblastoma Protein/metabolism; Tetradecanoylphorbol Acetate/pharmacology; Tumor Cells, Cultured;
Subjects: Diseases > Hematologic and lymphatic diseases > Leukemia
Molecules > Proteins
Cellular and Organismal Processes > Cell Physiology > Cell differentiation
Depositing User: Library Staff
Date Deposited: 02 Dec 2008 18:49
Last Modified: 21 May 2010 22:57
URI: http://authors.fhcrc.org/id/eprint/140

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