Interleukin-3 or erythropoietin induced nuclear localization of protein kinase C beta isoforms in hematopoietic target cells

• Published in: Cell proliferation Vol. 28; no. 3; p. 145
• Main Authors: Mason-Garcia, M, Harlan, R E, Mallia, C, Jeter, Jr, J R, Steinberg, H B, Fermin, C, Beckman, B S
• Format: Journal Article
• Language: English
• Published: England 01.03.1995
• Subjects: Animals; Cell Compartmentation; Cell Fractionation; Cell Nucleus - enzymology; Cells, Cultured; Erythropoietin - pharmacology; Hematopoietic Stem Cells - drug effects; Hematopoietic Stem Cells - enzymology; Image Processing, Computer-Assisted; Immunoblotting; Immunohistochemistry; Interleukin-3 - pharmacology; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Liver - cytology; Mice; Protein Kinase C - agonists; Protein Kinase C - isolation & purification; Protein Kinase C - metabolism; Protein Kinase C beta
• ISSN: 0960-7722
• DOI: 10.1111/j.1365-2184.1995.tb00063.x

Protein kinase C (PKC) has been implicated in the signal transduction pathways for the biological effect of both interleukin-3 (IL-3) and erythropoietin (EPO) in hematopoietic target cells. The goal of this study was to identify specific classical isoforms of PKC and their localization in hematopoietic cells in response to the growth factors, IL-3 or EPO. In addition to murine fetal liver cells as a source of normal erythroid progenitor cells, we have utilized the B6SUt.EP cell line, a non-transformed hematopoietic cell line that requires IL-3 for proliferation, but for which EPO can substitute as a growth factor. With polyclonal antibodies prepared against peptide sequences specific for the alpha, beta I, beta II and gamma isoforms of PKC, we have identified beta I and beta II as the predominant nuclear isoforms in target cells that proliferate in response to IL-3 or EPO.