| Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C. | |
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MedLine Citation:
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PMID: 1386358 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Treatment of murine erythroleukemia cells (MELC) attached to fibronectin-coated dishes with dimethyl sulfoxide causes the cells to become committed to the erythroid differentiation pathway. These cells mature extensively and acquire the characteristics of erythroid cells. The cells lose their cell-surface fibronectin receptors and accumulate red cell-specific membrane proteins, such as band 3, in amounts comparable to those in erythrocytes. Previous studies of MELC have shown that the presence of protein kinase C (PKC) is required for commitment to differentiation, but that the level of PKC activity declines progressively during maturation. In this study, we have established a role for PKC in the maturation of MELC committed to differentiation. Our results show that down-regulation of PKC by addition of phorbol 12-myristate 13-acetate (PMA) to committed MELC blocks subsequent maturation of the cells. Treatment of MELC with the PKC inhibitors H7 and sphingosine had similar effects. Down-regulation of PKC was assayed by measuring cytosolic PKC activity as well as by Western blotting using PKC antibodies. MELC maturation was monitored by loss of the cell-surface fibronectin receptor, release of cells from fibronectin plates, and accumulation of the band 3 anion transport protein. Immunoprecipitation of surface-labeled proteins by an anti-fibronectin receptor (integrin) antibody showed that PMA-treated cultures had more fibronectin receptor protein than untreated cultures 6 days post-induction. As a result, cultures of committed MELC treated with PMA remained attached to fibronectin-coated plates, whereas non-PMA-treated cells were released into the culture medium. Furthermore, PKC-depleted cells accumulated much smaller amounts of band 3 protein and band 3 mRNA than did non-PKC-depleted controls. Our results show that although PKC activity declines progressively during post-commitment maturation of MELC, its continued presence is critical for the process of cellular maturation. |
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Authors:
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B GuptaRoy; C M Cohen |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 267 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1992 Aug |
Date Detail:
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Created Date: 1992-08-28 Completed Date: 1992-08-28 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 15326-33 Citation Subset: IM |
Affiliation:
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Department of Biomedical Research, St. Elizabeth's Hospital of Boston, Massachusetts 02135. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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genetics Animals Anion Exchange Protein 1, Erythrocyte / genetics Blotting, Northern Cell Differentiation / drug effects, physiology* Cell Membrane / enzymology Globins / genetics Leukemia, Erythroblastic, Acute / enzymology, pathology Mice Phosphoproteins / isolation & purification, metabolism Protein Kinase C / metabolism* RNA, Neoplasm / genetics, isolation & purification Receptors, Fibronectin Receptors, Immunologic / analysis, metabolism Tetradecanoylphorbol Acetate / pharmacology* Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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HL 24382/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Anion Exchange Protein 1, Erythrocyte; 0/Phosphoproteins; 0/RNA, Neoplasm; 0/Receptors, Fibronectin; 0/Receptors, Immunologic; 16561-29-8/Tetradecanoylphorbol Acetate; 9004-22-2/Globins; EC 2.7.11.13/Protein Kinase C |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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