Document Detail

Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C.
MedLine Citation:
PMID:  1386358     Owner:  NLM     Status:  MEDLINE    
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.
B GuptaRoy; C M Cohen
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  267     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1992 Aug 
Date Detail:
Created Date:  1992-08-28     Completed Date:  1992-08-28     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  15326-33     Citation Subset:  IM    
Department of Biomedical Research, St. Elizabeth's Hospital of Boston, Massachusetts 02135.
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MeSH Terms
Actins / genetics
Anion Exchange Protein 1, Erythrocyte / genetics
Blotting, Northern
Cell Differentiation / drug effects,  physiology*
Cell Membrane / enzymology
Globins / genetics
Leukemia, Erythroblastic, Acute / enzymology,  pathology
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
Reg. No./Substance:
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 Kinase C

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