Introduction of the beta isozyme of protein kinase C accelerates induced differentiation of murine erythroleukemia cells

Proc Natl Acad Sci U S A. 1990 Jun;87(12):4417-20. doi: 10.1073/pnas.87.12.4417.

Abstract

Induction of differentiation in murine erythroleukemia cells (MELCs) involves a protein kinase C (PKC)-mediated step. Vincristine-resistant cells respond more rapidly to hybrid polar/apolar inducers than the parental cells. These vincristine-resistant MELCs contain elevated levels of the beta isozyme of PKC (PKC-beta). Exogenous homologous murine PKC-beta, incorporated into permeabilized MELCs, accelerates induced differentiation. Neither rat PKC-beta, nor mouse PKC-alpha, nor rat PKC-alpha, incorporated into permeabilized MELCs, is effective in altering the kinetics of induced differentiation. This provides direct evidence for a rate-limiting role for this PKC isozyme during N,N'-hexamethylenebisacetamide-mediated induced differentiation of a transformed cell.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetamides / pharmacology
  • Animals
  • Brain / enzymology
  • Cell Differentiation
  • Cell Line
  • Drug Resistance
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism*
  • Kinetics
  • Leukemia, Erythroblastic, Acute
  • Leukemia, Experimental
  • Mice
  • Protein Kinase C / isolation & purification
  • Protein Kinase C / metabolism*
  • Rats
  • Tumor Cells, Cultured / cytology*
  • Tumor Cells, Cultured / drug effects
  • Tumor Cells, Cultured / enzymology
  • Vincristine / pharmacology

Substances

  • Acetamides
  • Isoenzymes
  • Vincristine
  • Protein Kinase C
  • hexamethylene bisacetamide