Erythropoietin stimulates nuclear localization of diacylglycerol and protein kinase C βII in B6SUt.EP cells
Erythropoietin (EPO) is a hormone, as well as a hematopoietic growth factor, that specifically regulates the proliferation and differentiation of erythroid progenitor cells. Although the membrane-bound receptor for EPO has no intrinsic kinase activity, it triggers the activation of protein kinases v...
Saved in:
Published in | Journal of lipid mediators and cell signalling Vol. 17; no. 3; pp. 135 - 150 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.12.1997
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Erythropoietin (EPO) is a hormone, as well as a hematopoietic growth factor, that specifically regulates the proliferation and differentiation of erythroid progenitor cells. Although the membrane-bound receptor for EPO has no intrinsic kinase activity, it triggers the activation of protein kinases via phospholipases A
2, C, and D. A cascade of serine and threonine kinases, including Raf-1, MAP kinase and protein kinase C (PKC) is activated following tyrosine phosphorylation. In this study, we have examined whether changes in nuclear PKC and 1,2-diacylglycerol (DAG) are induced following EPO treatment of the murine target cell line, B6SUt.EP. Western blot analysis using isoform-specific antibodies demonstrated the presence of PKC
βII, but not PKC
α,
βI,
γ,
ε,
δ,
η, or
ζ in the nuclei of cells stimulated with EPO. The increase in nuclear
βII levels was accompanied by an immediate rise in DAG mass levels with both of the increases peaking by 1 min. These rapid increases in nuclear DAG and PKC
βII expression suggest a mechanism for EPO-induced changes in gene expression necessary for cell proliferation. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0929-7855 |
DOI: | 10.1016/S0929-7855(97)00027-8 |